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  • Articles  (786)
  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (786)
  • 2010-2014
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  • Biology  (786)
  • 1
    Electronic Resource
    Electronic Resource
    Effects of allatectomy and ovariectomy on cuticular hydrocarbons in Calliphora vomitoria (diptera) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 363-373 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone ; ecdysteroids ; attractiveness ; ovaries ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The relationships between female attractiveness, cuticular hydrocarbons, and levels of juvenile hormone and ecdysteroids were studied in Calliphora vomitoria. The experiments were conducted at 48 and 72 h post-emergence, according to attractiveness appearance and increase. The 48-h-old allatectomized females were less attractive than the control females, whereas no changes occurred either in cuticular hydrocarbons total mass production or in the different hydrocarbon families. However, the 72-h-old allatectomized females were more attractive than the control females, and, in relative proportions, allatectomy led to an increase in monomethylalkanes and a decrease in n-alkanes.Only at 48 h were the ovariectomized females less attractive than the control females and did ovariectomy increase the relative proportions of monomethylalkanes. At 72 h, ovariectomy did not influence female attractiveness, but it decreased the total cuticular hydrocarbon production. Allatectomy and ovariectomy significantly decreased ecdysteroids levels at 48 and 72 h. Ovariectomy did not affect juvenile hormone production.These results suggest that attractiveness and cuticular hydrocarbon synthesis could be under the direct control of ecdysteroids and the indirect influence of juvenile hormone. © 1994 Wiley-Liss, Inc.
    Additional Material: 7 Tab.
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    URL: http://dx.doi.org/10.1002/arch.940250410
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  • 2
    Electronic Resource
    Electronic Resource
    Patterns of biosynthesis and accumulation of hydrocarbons and contact sex pheromone in the female german cockroach, Blattella germanica (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 375-391 
    Details
    ISSN: 0739-4462
    Keywords: pheromone biosynthesis ; hydrocarbon biosynthesis ; methyl ketone biosynthesis ; ovarian development ; feeding ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: De novo synthesis of contact female sex pheromone and hydrocarbons in Blattella germanica was examined using short in vivo incubations. Accumulation of pheromone on the epicuticular surface and the internal pheromone titer were related to age-specific changes in hydrocarbon synthesis and accumulation in normal and allatectomized females. The incorporation of radiolabel from [1-14C]propionate into the cuticular methyl ketone pheromone fraction was positively related to corpora allata activity during two gonotrophic cycles. During peak pheromone production the total internal lipid fraction contained greater titers of pheromone than the cuticular surface, and it too exhibited a cycle internally, preceding the rise in external pheromone. This suggests that synthesis and accumulation of pheromone internally are followed by transport of pheromone to the epicuticular surface where it accumulates. Radiolabel was incorporated efficiently into both cuticular and internal hydrocarbons after the imaginal molt and until the peak of pheromone synthesis, but it declined to lower levels before ovulation and throughout pregnancy. The internal hydrocarbon titer decreased 58% after oviposition, suggesting deposition in the egg case. It remained relatively unchanged during pregnancy and increased again during the second gonotrophic cycle. In allatectomized females, hydrocarbon synthesis was reduced relative to control females until oviposition in the latter. However, subsequent rates of hydrocarbon synthesis in allatectomized females (without oothecae) exceeded the rates in sham-operated females (with oothecae). In the absence of ovarian uptake of hydrocarbons, the internal titer increased without the decline found in control females at oviposition. As internal hydrocarbons increased, so did cuticular hydrocarbons and both internal and cuticular methyl ketone pheromones. These patterns corresponded well with feeding patterns in sham-operated and allatectomized females, suggesting that pheromone production is normally regulated by stage-specific feeding-induced hydrocarbon synthesis (precursor accumulation internally) and juvenile hormoneinduced conversion of hydrocarbon to pheromone. They also suggest that both the cuticle and the ovaries might be target sites for hydrocarbon and possibly methyl ketone deposition. © 1994 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940250411
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  • 3
    Electronic Resource
    Electronic Resource
    Sources of possible host regulatory factors in Cardiochiles nigriceps (hymenoptera: Braconidae) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 197-209 
    Details
    ISSN: 0739-4462
    Keywords: parasitoid ; protein secretions ; teratocytes ; parasitoid larvae ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Both larvae and teratocytes liberated upon hatching from the eggs of the endoparasitoid Cardiochiles nigriceps Viereck were found to release proteins into their surrounding environment as they develop. Teratocytes were found to synthesize and release a number of proteins into culture media in which they were incubated. The proteins released differed among the different teratocyte ages. Larvae were also found to release proteins into the culture media in which they were incubated. Ligation of the head or anal vesicle altered the protein pattern found in the media. The results demonstrate that both larvae and the associated teratocytes release proteins that may have important functions in the parasitoidhost interaction. © 1994 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940260210
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  • 4
    Electronic Resource
    Electronic Resource
    Preface (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 1-1 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940270102
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  • 5
    Electronic Resource
    Electronic Resource
    Diuretic activity of Mas-DP II, an identified neuropeptide from Manduca sexta: An in vivo and in vitro examination in the adult moth (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 3-10 
    Details
    ISSN: 0739-4462
    Keywords: diuresis ; excretion ; Malpighian tubules ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Mas-DP II, a recently identified 30 amino acid diuretic peptide isolated from the tobacco hornworm moth, Manduca sexta, was tested for its ability to increase fluid excretion in adult M. sexta, and for the ability to elevate the rate of fluid secretion from isolated Malpighian tubules cultured in vitro. Mas-DP II was found to increase fluid weight loss from decapitated adult moths in a dose-dependent manner; weight loss increased significantly at doses as low as 5 ng for female moths and 25 ng for male moths. Male moths injected with large doses of Mas-DP II continued to exhibit increased rates of fluid loss up to 4 h post-injection. In vitro, Mas-DP II stimulated fluid secretion from isolated Malpighian tubules at concentrations as low as 4 nM for tubules from both male and female moths. © 1994 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940270103
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  • 6
    Electronic Resource
    Electronic Resource
    Cyclic volumetric changes in corpus allatum cells in relation to juvenile hormone biosynthesis during ovarian cycles in cockroaches (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 53-64 
    Details
    ISSN: 0739-4462
    Keywords: endocrine gland development ; cell size ; egg case ; reproductive cycle ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Development and activity of the corpora allata (CA) were investigated in adult female Blattella germanica and Supella longipalpa. These two cockroach species differ in their reproductive modes, with relatively uninterrupted cycles of oocyte development in S. longipalpa and discrete patterns of oocyte development which are interrupted by pregnancy in B. germanica. During ovarian cycles in both cockroach species, elevated rates of juvenile hormone (JH) synthesis closely coincide with synchronous volumetric growth of the CA. Declines in CA activity before ovulation coincide with synchronous declines in the size of CA cells. However, in adult females of both species the number of CA cells remains relatively constant. Quantitative studies in normal and ovariectomized adult B. germanica females show that the volumetric changes in CA cells are paced and synchronized by ovarian factors. Without the ovaries, the enlargement of CA cells in newly eclosed females is slower and relatively asynchronous. Without an ootheca in ovariectomized females, the volume of CA cells fails to decline synchronously, resulting in variable but high rates of JH synthesis. The precise relationship between volume of CA cells and-JH biosynthesis in oviparous and viviparous cockroaches suggests that in cockroaches, cell volume, and not CA cell number, is a better predictor of JH biosynthetic activity. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940270107
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  • 7
    Electronic Resource
    Electronic Resource
    Acetylcholinesterase from the horn fly (Diptera: Muscidae) II: Biochemical and molecular properties (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 109-121 
    Details
    ISSN: 0739-4462
    Keywords: Haematobia irritans ; acetylcholinesterase ; kinetics ; inhibition ; molecular form ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Purified acetylcholinesterase (AChE) of the horn fly was characterized to elucidate the enzymological, inhibitory, and molecular properties of the enzyme. Maximum activity of the AChE against the substrate acetylthiocholine (ATCh) occurred when reactions were conducted at 37°C and pH 7.5. Km and Vmax values were (9.2 ± 0.35) × 10-6 M and 239.8 ± 10.8 units/mg, respectively, for ATCh and (1.5 ± 0.07) × 10-5 M and 138.5 ± 5.5 units/mg, respectively, for butyrylthiocholine (BTCh). The activity of AChE decreased when concentrations of ATCh or BTCh were higher than 1 mM. Studies of the interaction of AChE with different inhibitors revealed pl50 values of 8.88 for eserine, 6.90 for BW284C51, and 4.97 for ethopropazine. Bimolecular reaction constants (kis) for the organophosphorus (OP) anticholinesterases were (2.74 ± 0.14) × 106 M-1 min-1 for coroxon, (7.20 ± 0.28) × 105 M-1 min-1 for paraoxon, and (2.33 ± 0.12) × 105 M-1 min-1 for stirofos. Two major forms of native AChE molecules were found on non-denaturing polyacrylamide gel electrophoresis (PAGE) with Triton X-100, corresponding to bands AChE-2 and AChE-4 found on PAGE without Triton X-100. AChE-2 had an estimated molecular weight of 603,000 and was amphiphilic. AChE-4 had a molecular weight of 147,000 and was hydrophilic. Results of PAGE analyses indicated that the purified enzyme had two bands, one of about 123 kDa and the other greater than 320 kDa, prior to disulfide reduction and only one band at about 54 kDa after reduction on SDS-PAGE. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940270204
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  • 8
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of a diuretic peptide Manduca diuresin (MasDPII) in the brain and suboesophageal ganglion of the tobacco hawkmoth Manduca sexta (Lepidoptera: Sphingidae) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 137-152 
    Details
    ISSN: 0739-4462
    Keywords: Manduca sexta ; MasDPII ; neurosecretory cells ; diuretic hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A purified polyclonal antibody against synthetic Manduca diuresin (formerly named MasDPII) was used to localize immunoreactive cell clusters in the protocerebrum and the suboesophageal ganglion of adult, larval, and pupal stages of Manduca sexta. In adults and pharate adults, strong immunostaining was found in type IIb median neurosecretory cells and IIa1-3 cells. Moderate staining was observed in the maxillary, mandibular, and labial cell clusters in the suboesophageal ganglion. In larvae, immunostaining was found in four IIa cells and in the maxillary, mandibular, and labial cell clusters of the suboesophageal ganglion. In the early pupal stage, six to eight type IIa cells were immunopositive and two clusters of developing type IIb cells showed positive staining. Furthermore, maxillary, mandibular, and labial cell clusters in the pupal suboesophageal ganglion also contained immunoreactive material. In all stages, nervi corporis cardiaci-1+2 and the retrocerebral complex showed immunoreactivity. While preadsorption of purified antibody with another diuretic peptide from M. sexta brain, MasDH, slightly reduced the immunostaining by the Manduca diuresin antibody, preadsorption with Manduca diuresin completely abolished immunoreactivity in all of the cells previously mentioned. The findings suggest the presence of Manduca diuresin or Manduca diuresin-like peptides in larval and pupal type IIa cells and in the suboesophageal ganglion of M. sexta in all three developmental Stages. © 1994 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940270206
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  • 9
    Electronic Resource
    Electronic Resource
    Purification and characterization of the Manduca sexta neuropeptide processing enzyme carboxypeptidase E (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 193-203 
    Details
    ISSN: 0739-4462
    Keywords: Nα-(4-aminobenzoyl)-L-arginine ; carboxypeptidase M ; silver stain ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The neuropeptide processing enzyme carboxypeptidase E (CPE) (E.C.3.4.17.10) has been well studied in vertebrates but its presence in invertebrates has not yet been reported. CPE activity in insects is present in membrane-bound and soluble forms. The soluble CPE has been purified to homogeneity from the brain of the tobacco hornworm Manduca sexta. It is a 57 kDa glycoprotein containing 9% sugars. It is activated 9.2 ± 1.8 fold by CoCl2 and inhibited by chelating agents. Its sensitivity to guanidinoethyl-mercaptosuccinic acid, and its molecular mass, make this enzyme a good candidate to be the insect equivalent of the mammalian CPE. Furthermore, its lack of sensitivity towards p-(chloromercuri)benzenesulfonate puts it closer to the vertebrate carboxypeptidase M (CPM). We postulate that insects may possess a single protein fulfilling both CPE and CPM functions. © 1994 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940270305
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  • 10
    Electronic Resource
    Electronic Resource
    Synthesis and deposition of PCG-100, the main pupal cuticle glycoprotein of the medfly Ceratitis capitata (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 217-234 
    Details
    ISSN: 0739-4462
    Keywords: integument ; metamorphosis ; insect epidermis ; Ceratitis capitata ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have studied the developmental expression of the main pupal cuticle glycoprotein, PCG-100, in the Medfly Ceratitis capitata. A polyclonal antiserum was raised against this protein. Western blotting analysis showed that this glycoprotein is integument- and stage-specific. No PCG-100 or immunologically related polypeptides were detected in other tissues or instars. As studied by microinjection of [35S]methionine in individual flies, in vivo synthesis and deposition of PCG-100 begins approximately 48 h after the onset of pupariation, shortly after the time of head eversion. Synthesis is maximal at 54-64 h, decreases at 72 h, and practically ceases in fully shaped 4-day-old pupae. The time required for PCG-100 deposition into the cuticle was found to be less than 10 min after its synthesis. This is the first time such in vivo analysis has been performed. © 1994 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940270307
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  • 11
    Electronic Resource
    Electronic Resource
    Biosynthetic alternatives for acetogenic production of sorbic acid in the potato aphid (Homoptera: Aphididae) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 249-264 
    Details
    ISSN: 0739-4462
    Keywords: fatty acid synthetase ; peroxisomes ; clofibrate ; p-bromophenacyl esters ; Macrosiphum euphorbiae ; sorbic acid ; acetyl-CoA ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Following in vivo injection of [1-14C]-sodium acetate, triacylglycerols of the potato aphid, Macrosiphum euphorbiae (Thomas), were extracted and derivatized to p-bromophenacyl fatty acid esters for two-dimensional TLC and GLC-MSD (mass selective detector) analysis. Radiolabeled sorbic (E, E-2,4-hexadienoic) acid ester was detected, demonstrating that this short chain fatty acid unique to aphids is biosynthesized via an acetogenic pathway. Crotonic (E-2-butenoic) or hexenoic acids were not detected in labeled or unlabeled potato aphid samples or unlabeled samples from the oleander aphid, Aphis nerii Fonscolombe. Crotonic or hexenoic acids might have been expected if an incomplete cycling by fatty acid synthetase or a novel desaturase acting on the prevalent hexanoate, respectively, were responsible for sorbic acid synthesis in aphids. A peroxisomal β-oxidation route to sorbic acid from longer chain fatty acids was not indicated since injections of clofibrate, a peroxisomal proliferator, with or without C18 polyunsaturated lipids gave no substantial increase in C6 lipids. Also, some characteristic enzyme activities of peroxisomal β-oxidation were not found in an ultracentrifugal “peroxisomal” fraction from the potato aphid. Although the individual biochemical steps from acetate to sorbate in aphids remain unclear, an unusual acetate-malonate pathway is indicated. Clarification of the biosynthetic steps to sorbic acid should identify at least one novel enzyme for animals. © 1994 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940270403
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  • 12
    Electronic Resource
    Electronic Resource
    Characterization and biological effects of cotesia congregata polydnavirus on host larvae of the tobacco hornworm, manduca sexta (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 165-195 
    Details
    ISSN: 0739-4462
    Keywords: calyx fluid ; viral proteins ; glycoproteins ; venom ; parasitoid ; developmental arrest ; endocrine disruption ; metamorphosis ; hemolymph proteins ; SDS-PACE ; Western blot ; Lepidoptera ; Hymenoptera ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The ovaries of endoparasitic species of braconid and ichneumonid wasps contain large numbers of polydnavirus (PDV) virions that replicate in specialized calyx cells of the ovaries and are injected into the host larva during parasitization. In the braconid wasp Cotesia congregata that parasitizes the tobacco hornworm, Manduca sexta, the total amount of viral DNA present in the ovaries was determined to be 25-75 ng. Analysis of viral DNA on 0.4% agarose gels showed that the genome was comprised of 15-20 circles of double-stranded DNA. SDS-PAGE analyses showed that a large number (〉30) of structural polypeptides were present in the virions, and analysis of the venom likewise showed that multiple components were present. The major size classes of venom proteins differed from those present in the PDV. However, Western blots using polyclonal PDV antibodies showed that some cross-reacting PDV-like proteins were present in the venom, perhaps explaining the mild PDV-enhancing effect of the venom. Injection of PDV into unparasitized larvae provoked pronounced alterations in their growth, development, pigmentation, and hemolymph proteins. A densely staining band of hemolymph proteins of approximately 18-20 kD appeared in large amounts relative to other hemolymph proteins several days following injection of PDV; this band was undetectable in naturally parasitized larvae. Eggs which had been washed extensively to remove PDVs were encapsulated following injection, but development of the host still was disrupted, usually in the post-wandering prepupal stage. Thus, neither the parasites nor their host survived, despite mobilization of an “effective” host response.© 1994 WiIey-Liss, Inc.
    Additional Material: 13 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940260209
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  • 13
    Electronic Resource
    Electronic Resource
    Biochemical and developmental alterations of Heliothis virescens (F.) (lepidoptera, noctuidae) larvae induced by the endophagous parasitoid Cardiochiles nigriceps viereck (Hymenoptera, braconidae) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 211-233 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: All larval stages of Heliothis virescens (F.) parasitized by the endophagous larval parasitoid Cardiochiles nigriceps Viereck, a braconid species belonging to the subfamily Microgasterinae, exhibit developmental arrest at last instar and fail to pupate. The major part of larval development of the parasitoid is synchronized with the arrested host last larval instar and the parasitoid first molt is never observed before the host attains the late digging stage. At this time, the total ecdysteroid titer of the hemolymph of parasitized hosts is very low and subsequently shows a slow and gradual increase, characterized by a low titer of 20-hydroxyecdysone (20-HE) associated with consistent amounts of inactive ecdysteroid polar metabolites. Juvenile hormone esterase (JHE) activity is high in both control and parasitized host larvae at the early digging stage of development, and juvenile hormone analogs (JHA) applied to parasitized host last instar larvae appear to suppress the parasitoid molt. Concurrent with these changes was an increase in the hemolymph titer of proteins which was maintained at a high level in parasitized larvae in contrast to the observed decrease in control larvae at the cell formation stage of development. Neck-ligation of newly molted host 5th instar parasitized larvae, prior to both JHE release and the increase in protein titers, inhibited growth and molting of the parasitoid. In contrast, ligation after JHE release and with high hemolymph protein titers resulted in parasitoid molting and growth. These data suggest that the host ecdysteroid hormones are not directly involved in the regulation of the parasitoid molt, although high juvenile hormone (JH) levels probably prevent it. More likely, molting is triggered by other biochemical changes, such as proteins or other factors occurring in the hemolymph. Molting of C. nigriceps larvae in vitro into an ecdysone-free semidefined medium further supported the view that host ecdysone is not necessary for the molt. Teratocytes of C. nigriceps seem to play an important role in the inactivation of 20-HE through its conversion to inactive polar metabolites, and along with female calyx fluid and venom which depress the secretory activity of the host prothoracic glands, they are the most important sources of host regulatory factors. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940260211
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  • 14
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    Biosynthesis, secretion, and immunocytochemistry of trypsin modulating oostatic factor of Aedes aegypti (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 27-38 
    Details
    ISSN: 0739-4462
    Keywords: hormone ; HPLC ; ovary ; antibody ; PAGE ; pulse-chase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Trypsin modulating oostatic factor (TMOF) was followed by RIA in the ovary of female Aedes aegypti before and after the blood meal. The amount of TMOF in a pair of ovaries from females fed sugar for 3 days or blood for 24 h was low (1.7 ng). Between 24 and 48 h after the blood meal the amount of TMOF in the ovaries rapidly increased and reached a peak of 104 ng at 48 h. The amount of TMOF in the head of a female A. aegypti was very low (0.05 to 0.1 ng) during sugar and blood feeding. Immunocytochemical methodology identified the follicular epithelium as the site of biosynthesis of TMOF in the ovary. Females ovariectomized and fed a blood meal continued to synthesize trypsin for 64 h, whereas intact controls stopped at 40 h, indicating that a factor from the ovary regulates trypsin biosynthesis. Ovaries incubated in vitro with [3H]proline synthesized [pro-3H]TMOF that was identified by HPLC and by anti-TMOF serum. The ovary started to synthesize TMOF in vitro 24 h after the blood meal, and the synthesis reached a peak at 36 h and then declined. The synthesis of TMOF by the ovary is closely correlated with the termination of trypsin biosynthesis in the female mosquito's midgut. Ovaries that were pulsed with [3H]proline for 30 min synthesized [pro-3H]TMOF which was chased into the medium with unlabeled proline, indicating that the hormone is secreted by the ovary. These results indicate that TMOF is a secretory peptide, synthesized by the ovarian follicular epithelium and that it modulates trypsin biosynthesis in the mosquito's gut. © 1994 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/arch.940270105
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  • 15
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    Benzodioxole-1,3-benzodioxole derivatives and their effects on the reproductive physiology of insects (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 39-51 
    Details
    ISSN: 0739-4462
    Keywords: Mediterranean fruit fly ; juvenile hormone ; microtubules ; chemosterilant ; Ceratitis capitata ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Alkyl ethers of methylenedioxy analogs of obtusastyrene or benzyl-1,3-benzodioxole derivatives (BBDs) and related benzylphenols have been shown to interfere with various phases of reproduction in insects. BBDs have also been shown to interfere with sex attractancy, to induce precocious development, and to antagonize juvenile hormone (JH) functions in insects. Because representative BBDs were reported to show low toxicity to mammals and to be negative in assays testing for potential mutagens, these compounds held much promise to be environmentally safe insect chemosterilants. The mode of action of BBDs does not involve blocking or competition for putative JH receptor sites on follicular cells or hemolymph JH binding proteins. However, BBDs were shown to interfere with (1) in vitro biosynthesis and release of JH from corpora allata of Mediterranean fruit fly females, and (2) microtubule assembly in insects. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940270201
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    Cytochrome b5 involvement in cytochrome P450 monooxygenase activities in house fly microsomes (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 205-216 
    Details
    ISSN: 0739-4462
    Keywords: cytochrome b5 ; microsomal cytochrome P450 monooxygenase ; microsomes ; fatty acyl CoA desaturase ; insect ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The involvement of cytochrome b5 in different cytochrome P450 monooxygenase and palmitoyl CoA desaturase activities in microsomes from insecticide-resistant (LPR) house flies was determined using a specific polyclonal antiserum developed against house fly cytochrome b5. Anti-b5 antiserum inhibited the reduction of cytochrome b5 by NADH-cytochrome b5 reductase. The antiserum also inhibited palmitoyl CoA desaturase, methoxycoumarin-O-demethylase (MCOD), ethoxycoumarin-O-deethylase (ECOD), and benzo[a]pyrene hydroxylase (aromatic hydrocarbon hydroxylase, AHH) activities. However, methoxyresorufin-O-demethylase (MROD) and ethoxyresorufin-O-deethy-lase (EROD) activities were not affected by this antiserum. These results demonstrate that cytochrome b5 is involved in fatty acyl CoA desaturase activities and in certain cytochrome P450 monooxygenase activities (i.e., MCOD, ECOD, and AHH) in LPR house fly microsomes. Other cytochrome P450 monooxygenase activities (i.e., MROD and EROD) may not require cytochrome b5. The results suggest that cytochrome b5 involvement with cytochrome P450 monooxygenase activities is dependent upon the cytochrome P450 isoform involved. © 1994 Wiley-Liss, Inc.
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    Inhibition by azadirachtin of phospholipid transfer from lipophorin to the oocytes in Rhodnius prolixus (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 287-299 
    Details
    ISSN: 0739-4462
    Keywords: oogenesis ; lipid ; lipoprotein ; vitellogenin ; vitellin ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The growth of oocytes was severely reduced in female Rhodnius prolixus treated with azadirachtin A (AZA). When administered in a blood meal, AZA (1 μg/ml) inhibited phospholipid transfer to the ovaries without altering the availability of yolk protein in the hemolymph or its uptake by 1 mm oocytes. The lipid composition of lipophorin, its concentration in the hemolymph, and its density were normal in AZA-treated females. Partial inhibition of phospholipid transfer was observed when lipophorin from AZA-treated females was injected into normal females, or when lipophorin from normal females was injected into AZA-treated females. The two effects were additive, so that the transfer of phospholipids from the lipophorin of AZA-treated females to the oocytes of AZA-treated females was nearly eliminated. In combination, these effects of AZA on phospholipid transfer to the oocytes limit the capacity of AZA-treated females to produce eggs. © 1994 Wiley-Liss, Inc.
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    Characterization of genital tract growth factor-like activity from testis sheaths and fat body of Heliothis virescens (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 263-277 
    Details
    ISSN: 0739-4462
    Keywords: male reproduction ; Lepidoptera ; growth factors ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Testis sheaths and fat body from developing male pupae of Heliothis virescens synthesize soluble growth factor-like products when exposed to 20-hydroxyecdysone (20HE). These factors promote growth and development of the genital tract. Saline extracts of modified Grace's medium and 20HE-treated testis sheaths and fat body were subjected to heat, freeze-thaw, organic solvents, and low pressure size exclusion chromatography. Although extracts were stable to repeated freeze-thawing, activity was lost after exposure to organic solvents; activities of fractions heavier than 6.5 KDa were inhibited by heating to 100°C. Size exclusion chromatography yielded 10 active testis extract fractions and 9 active fat body fractions. Although the approximate molecular weights of most of the extract fractions were similar, enzyme studies using protease, lipase, and α-amylase indicated differences in the chemistry of active fractions derived from the two tissues. Active factors were inhibited by protease or lipase or both enzymes. © 1994 Wiley-Liss, Inc.
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    Inhibitory effect of 10,11-methyl-enetetradec-10-enoic acid on a Z9-desaturase in the sex pheromone biosynthesis of Spodoptera littoralis (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 279-286 
    Details
    ISSN: 0739-4462
    Keywords: sex pheromone biosynthesis ; desaturase ; inhibition ; Spodoptera littoralis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effect of 10,11-methylenetetradec-10-enoic acid on the sex pheromone biosynthetic pathway of Spodoptera littoralis is reported. This new cyclopropene fatty acid inhibited the biosynthesis of the main pheromone component from labeled myristicacid. The study of each Z desaturation step revealed that the Z9-desaturase of E11-14:Acid was inhibited, whereas the Z11-desaturase of 16:Acid was not affected. The results presented in this article agree with our hypothesis that the methylenehexadecenoic acids are beta-oxidized in the pheromone gland to the corresponding methylenetetradecenoic acids. © 1994 Wiley-Liss, Inc.
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    Digestive enzymes in midgut cells, endo-and ectoperitrophic contents, and peritrophic membranes of Spodoptera frugiperda (lepidoptera) larvae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 299-313 
    Details
    ISSN: 0739-4462
    Keywords: microapocrine secretion ; immobilized enzymes ; peritrophic membrane ; membrane-bound enzymes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the midgut of Spodoptera frugiperda larvae, subcellular fractionation data suggest that aminopeptidase and part of amylase, carboxypeptidase A, dipeptidase, and trypsin are bound to the microvillar membranes; that major amounts of soluble dipeptidase, cellobiase, and maltase are trapped in the cell glycocalyx; and finally that soluble carboxypeptidase, amylase, and trypsin occur in intracellular vesicles. Most luminal acetylglucosaminidase is soluble and restricted to the ectoperitrophic contents. Aminopeptidase occurs in minor amounts bound to membranes both in the ectoperitrophic contents and incorporated in the peritrophic membrane. Amylase, carboxypeptidase A, and trypsin are found in minor amounts in the ectoperitrophic contents (both soluble and membrane-bound) and in major amounts in the peritrophic membrane with contents. Part of the activities recovered in the last mentioned contents corresponds to enzyme molecules incorporated in the peritrophic membrane. The results suggest that initial digestion is carried out in major amounts by enzymes in the endoperitrophic space and, in minor amounts, by enzymes immobilized in the peritrophic membrane. Intermediate and final digestion occur at the ectoperitrophic space or at the surface of midgut cells. The results also lend support to the hypothesis that amylase and trypsin are derived from membrane-bound forms, are released in soluble form by a microapocrine mechanism, and are partly incorporated into the peritrophic membrane. © 1994 Wiley-Liss, Inc.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940260201
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  • 23
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    Isomeric and quaternary properties of homogenous 33 kDa protein from the venom of chelonus near curvimaculatus (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 83-95 
    Details
    ISSN: 0739-4462
    Keywords: parasitoid ; polydnavirus ; dimerization ; toxin ; GP46/M-2 ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The 33,000 Dalton venom protein of Chelonus near curvimaculatus was characterized for structural properties of charge, quaternary associations, and relationship to polydnavirus encoded proteins. Homogenous isoforms of the protein were isolated from the venom by sequential steps of (1) microdissection, (2) separation based on charge (Mono-Q column HPLC or narrow-range electrofocusing), and (3) centrifugal filtration based on molecular weight using Centricon microconcentrators. The purified protein dimerized under native conditions, and this quaternary association became denaturation resistant under certain conditions. Chemical modification of lysine epsilon amino groups did not disrupt such dimerization. The cDNA for the protein did not possess high similarity to any sequence encoded in the polydnavirus, as indicated by results of Southern blotting, but does possess similarity in its repeats to the repeats of the immunologically protective surface glycoprotein of Leishmania amazonensis. © 1994 Wiley-Liss, Inc.
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    Actions of acromelic acid on nervous system l-glutamate receptors (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 87-94 
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    ISSN: 0739-4462
    Keywords: excitatory amino acids ; identified motor neurone ; insect ; kainic acid analogue ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Acromelic acid, a naturally occurring kainoid, isolated from the mushroom Clitocybe acromelalga, is a weak displacer of [3H]L-glutamate binding to cockroach (Periplaneta americana) nerve cord membranes. Acromelic acid (1 mM) displaces ∼60% of specifically bound [3H]L-glutamate. When applied by bath perfusion to the cell body membrane of the cockroach fast coxal depressor motor neurone, acromelic acid generated slow, prolonged, dose-dependent depolarizations at concentrations of 0.3 μM and above. Thus acromelic acid is among the most potent of the excitatory amino acids tested to date on insect neurones. © 1994 Wiley-Liss, Inc.
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    Yolk formation in Locusta migratoria and Schistocerca gregaria: Related ligands and oocyte receptors (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 107-120 
    Details
    ISSN: 0739-4462
    Keywords: vitellogenesis ; receptor-mediated endocytosis ; vitellogenin receptor protein ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During vitellogenesis the transport of yolk precursor proteins, the vitellogenins (VTG), from the hemolymph into the oocyte is achieved by receptor-mediated endocytosis. Recently the receptor for the VTG of Locusta migratoria has been isolated. Now a new protocol has been developed for the purification of the VTG receptor of this locust from ovarian membranes. By CHAPS solubilization of the membranes followed by ion exchange and immunoaffinity chromatography, a 100-fold purification of the VTG receptor was achieved. The amino acid composition of the receptor protein has been determined. However, first attempts to sequence the receptor failed due to the N-terminal blocking of the molecule. With the same methods the VTG receptor of another locust, Schistocerca gregaria, has been isolated, purified, and characterized. This receptor has an apparent Mr of 186 kDa under nonreducing conditions. It recognizes L. migratoria VTG and vice versa. However, in cross-competition experiments in which the Schistocerca VTG competed with Locusta VTG for binding to the Locusta VTG receptor, the Schistocerca VTG was less efficient. Furthermore, the VTG receptor proteins of S. gregaria and L. migratoria are immunologically related as revealed by Western blotting with anti-Locusta VTG receptor antibodies. It appears that important structural elements required for efficient and specific endocytosis of VTG have been conserved. © 1994 Wiley-Liss, Inc.
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    Announcement (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 175-176 
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    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
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  • 27
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940250301
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    Midgut proteinase activities of three keratinolytic larvae, Hofmannophila pseudospretella, Tineola bisselliella, and Anthrenocerus australis, and the effect of proteinase inhibitors on proteolysis (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 159-173 
    Details
    ISSN: 0739-4462
    Keywords: serine endopeptidase ; metalloendopeptidase ; keratinolytic larvae ; proteinase inhibitor ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The midgut proteinase activities were characterized from the keratinolytic larvae of two lepidopterans, Hofmannophila pseudospretella (Stainton) (Oecophoridae) and Tineola bisselliella (Hummel) (Tineidae), and one coleopteran, Anthrenocerus australis (Hope) (Dermestidae). The major endopeptidase activities, characterized using specific enzyme inhibitors, were serine proteinases with hydrolytic activity against N-benzoyl-DL-arginine-p-nitroanilide and against N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-leucine-p-nitroanilide. No significant levels of metalloendopeptidase or cysteine endopeptidase activities were detected. Aminopeptidase activity was present in all larvae. The enzyme levels and properties of the two moth larvae were similar to each other and to those of phytophagous lepidopteran larvae but different from those of the beetle larva. Whereas only a limited number of serine proteinase inhibitors inhibited the midgut proteolysis of the lepidopteran larvae, most inhibitors inhibited the midgut proteolysis of the beetle larva. © 1994 Wiley-Liss, Inc.
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    Inhibition of cuticular lipid synthesis and its effect on insect survival (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 177-191 
    Details
    ISSN: 0739-4462
    Keywords: Triatoma infestans ; insect cuticle ; hydrocarbon biosynthesis ; water loss ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A new approach to insect control - using sodium trichloroacetate (NaTCA) to inhibit synthesis of the hydrophobic cuticular lipids that protect insects from dehydration - was tested on Triatoma infestans. In vivo and in vitro studies of incorporation of radioactive precursors showed diminished cuticular hydrocarbon synthesis after NaTCA treatment. Thin layer chromatography and scanning electron microscopy showed disruption of the cuticular lipid layer of NaTCA-treated insects, which also have increased mortality and altered molting cycles. NaTCA treatment enhanced the penetration and increased the lethality of a contact insecticide. © 1994 Wiley-Liss, Inc.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
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    URL: http://dx.doi.org/10.1002/arch.940250401
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    Introduction (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 259-259 
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    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
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    Structure and activity of Bombyx PBAN (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 261-270 
    Details
    ISSN: 0739-4462
    Keywords: silkworm ; structure-activity relationship ; sex pheromone ; myotropic peptide ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two structurally related molecular species of pheromone biosynthesis activating neuropeptides (PBANs), PBAN-I and -II, were isolated from adult heads of the silkworm, Bombyx mori, and characterized. PBAN-I is a carboxyl-terminally amidated 33-residue peptide. Structure-activity relationship studies revealed that 1) its carboxyl-terminal pentapeptide is the smallest size showing activity, 2) the carboxyl-terminal amide is indispensable for activity, and 3) oxidation of three Met residues in PBAN-I to Met(O) (methionine sulfoxide) caused marked enhancement of activity, and the three Met(O) residues contribute equally to the enhancement of activity. Molecular design of PBAN analogs using a carboxyl-terminal hexapeptide showed that modification of the amino-terminal amino group brought about a dramatic increase in activity. This increase was presumed to be mainly due to the increased stability in hemolymph. PBANs share the common carboxyl-terminal sequence, -Phe-Xaa-Pro-Arg-Leu-NH2, with myotropic peptides isolated from locust and cockroach. Examination of cross-activity of these two groups of peptides revealed that PBAN and its analogs exhibited myotropic activity comparable to myotropic peptides, while myotropic peptides showed extremely high pheromonotropic activity. In B. mori, PBAN activates sex pheromone (bombykol) production presumably by promoting the reduction reaction from acyl to alcohol, which is the last step in the biosynthesis of bombykol. © 1994 Wiley-Liss, Inc.
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    Pheromonotropic stimulation of moth pheromone gland cultures in vitro (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 287-299 
    Details
    ISSN: 0739-4462
    Keywords: pheromone biosynthesis activating neuropeptide (PBAN) ; Helicoverpa spp. ; (Z)-11-hexadecenal ; RIA ; cyclic-AMP ; phorbol esters ; diacylglycerol analog ; ionomycin ; Ca2+ ; lithium ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The direct neurohormonal control of pheromone biosynthesis by pheromone biosynthesis activating neuropeptide (PBAN) was demonstrated in Helicoverpa (Heliothis) spp. using pheromone gland cultures in vitro. Pheromone gland activation involved the de novo production of the main pheromone component (Z)-11-hexadecenal as revealed by radio-TLC, radio-HPLC, and radio-GC. Activation was found to be a specific response attributed to pheromone gland cultures alone. Specificity of pheromonotropic activation was demonstrated to be limited to nervous tissue extracts. A sensitive and specific radioimmunoassay was developed using [3H]-PBAN, and the spatial and temporal distribution of PBAN-immunore-activity was studied. PBAN-immunoreactivity in brain complexes was found throughout the photoperiod and in all ages. From the distribution of PBAN-immunoreactivity it appears that PBAN release is affected by photoperiod. Pheromone gland cultures were found to be competent to pheromone production irrespective of age and photoperiod. Therefore, the neuroendocrine control of pheromone production operates at the level of neuropeptide synthesis and/or release and not at the level of the target tissue itself. The involvement of cyclic-AMP as a second messenger system was demonstrated. Brain extracts and PBAN were shown to stimulate dose- and time-dependent changes in intracellular cyclic-AMP levels. The role of cyclic-AMP in this mechanism was further verified by the ability of cyclic-AMP mimetics to mimic the pheromonotropic effect of brain extracts and PBAN. However, dose-response studies using PBAN and a hexapeptide C-terminal fragment of PBAN suggested that PBAN induces a two mechanism response, one occurring at low PBAN concentrations (high affinity receptor) and another at higher PBAN concentrations (low affinity receptor). Further evidence indicating a dual receptor system was obtained with the observation that the active phorbol ester (phorbol-12-myristate 13-acetate), the diacyl-glycerol analog (1,2-dioleolyl-sn-glycerol), and the intracellular calcium ionophore (ionomycin) mimicked the physiological action of PBAN and that lithium chloride had a pheromonostatic effect. The results indicate that pheromone glands also possess receptors that are linked to inositol phosphate hydolysis. © 1994 Wiley-Liss, Inc.
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    Mating-induced loss of sex pheromone and sexual receptivity in insects with emphasis on Helicoverpa zea and Lymantria dispar (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 317-327 
    Details
    ISSN: 0739-4462
    Keywords: male accessory glands ; pheromonostatic peptides ; sperm transfer ; corn earworm ; gypsy moth ; Diptera ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Mating in most species of insects leads to a transient or permanent loss in sexual receptivity of the females. Among moths, this loss of receptivity is often accompanied with a loss of the sex pheromone in the absence of calling, which also could be temporary or permanent. Most of the earlier work on changes in reproductive behavior after mating was done with Diptera in which sperm and/or male accessory gland secretions were shown to be responsible for termination of receptivity. In the corn earworm moth, Helicoverpa zea, mated females become depleted of pheromone and become nonreceptive to further mating attempts, but only for the remainder of the night of mating. A pheromonostatic peptide isolated from the accessory glands of males may be responsible for the depletion of pheromone, while the termination of receptivity is independently controlled. In the gypsy moth, Lymantria dispar, the changes in behavior following mating are permanent. In this species, the switch from virgin to mated behavior involves three steps: a physical stimulation associated with mating, transfer of viable sperm to the spermatheca, and commencement of oviposition. Signals generated by these factors operate through neural pathways and, unlike in H. zea, accessory gland factors seem not to be involved. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
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    Factors affecting pheromone production in beetles (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 347-362 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone ; pheromone biosynthesis ; Scolytidae ; Cucujidae ; Curculonidae ; Tenebrionidae ; stereochemistry ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Pheromone production and/or release by beetles is coordinated with a variety of behavioral, physiological, and environmental factors. To data, two basic mechanisms for the regulation of pheromone biosynthesis in beetles have been proposed. Pheromone biosynthesis may simply be dependent on the availability of biosynthetic precursors. Alternatively, certain stimuli or events may trigger pheromone biosynthesis via juvenile hormone (JH) action. JH may either act directly at the site of pheromone biosynthesis to enhance pheromone production or may act indirectly, through a brain hormone (which might be related to the pheromone biosynthesis activating neuropeptide) or through effects on antennal sensory response. Knowledge of the regulation of the initiation and termination of pheromone biosynthesis is reviewed. Mechanisms by which pheromone stereochemistry is controlled are also discussed. This is an important aspect of pheromone production in Coleoptera, since slight changes in the stereochemistry can completely alter the activity of the molecule. © 1994 Wiley-Liss, Inc.
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    Stimulation of vitellogenin production by methoprene in prepupae and pupae of manduca sexta (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 21-37 
    Details
    ISSN: 0739-4462
    Keywords: cDNA ; ecdysone ; fat body ; hemolymph ; juvenile hormone ; juvenile hormone analog ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Denaturing electrophoresis of hemolymph from prepupae of M. sexta showed trace amounts of polypeptides with mobilities corresponding to those of vitellogenin (Vg) apoproteins from adult females. Absence of the polypeptides in allatectomized insects suggested regulation by juvenile hormone (JH). Daily administration of 10 μg of the JH analog methoprene from day 4 of the fifth stage to day 0 of the pupal stage caused accumulation of these polypeptides. They were identified as apovitellogenins (apoVgs) immunochemically with Vg antiserum. Stimulation of Vg in response to methoprene varied with age. In all cases, day 0 female pupae were highly responsive. Vg synthesis was not stimulated when pupae were injected with 20-hydroxyecdysone (20-HE) in addition to methoprene. Methoprene-stimulated Vg synthesis was also abolished by inhibitors of mRNA or protein synthesis (α-amanitin, actinomycin, cycloheximide). This result indicated that methoprene-stimulated Vg accumulation requires gene expression. A Vg cDNA (2.1 kb) obtained by immunoscreening of the λgt 11 library, when used as a radiolabelled probe, hybridized with a 5.1 kb mRNA from total RNA of female fat body. It also hybridized with fat body RNA of normal prepupae and methoprene treated day 0 pupae but not with that of early fifth instars or solvent control pupae. The results indicate that the trace amounts of Vg found in prepupal stages are due to a weak expression of the Vg gene, which is stimulated by JH and repressed by 20-HE. © 1994 Wiley-Liss, Inc.
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    Announcement (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 85-86 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
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    URL: http://dx.doi.org/10.1002/arch.940250107
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    Purification and characterization of a flavin-binding storage protein from the hemolymph of Galleria mellonella (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 55-72 
    Details
    ISSN: 0739-4462
    Keywords: riboflavin ; serum protein ; protein structure ; waxmoth ; development ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The 85K storage protein that accumulates in the hemolymph of Galleria mellonella during the final larval instar was isolated and purified from newly molted pupae. The separation of fresh hemolymph proteins from larvae or pupae by different chromatographic and electrophoretic procedures indicated the native protein had a Mr of 170,000 and consisted of two identical 85K subunits. Crosslinking experiments using fresh hemolymph followed by Western blotting also indicated a dimeric structure for the native protein. Analyses of the dimer purified from pupal hemolymph indicated that 85K was a glycoprotein, containing approximately 6.5% neutral sugar and about 1.9% amino sugar. Like other insect flavin-binding proteins, 85K has a relatively high histidine content but an uncharacteristically high arginine content. The purified 85K dimer did not bind riboflavin, suggesting that the integrity of the molecule had been altered during purification. However, 85K purified in low yield by Affi-Gel Blue chromatography, did bind riboflavin, indicating that under certain, undefined conditions the functional integrity of the protein could be retained during purification. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
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    Toxicokinetics of [3H]-dihydroazadirachtin in the variegated cutworm Peridroma saucia (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 95-106 
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    ISSN: 0739-4462
    Keywords: azadirachtin ; tissue distribution ; elimination ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The excretion, retention, and tissue distribution of [3H]-dihydroazadirachtin was investigated in the variegated cutworm, Peridroma saucia (Noctuidae). The candidate compound was rapidly cleared from the hemolymph following either oral exposure or topical administration, with maximum concentrations at 6 h post-treatment and peak appearance of label in the frass at 12 h. However, approximately 45 and 55% of the labelled material was retained in the body at 72 h in respective treatments. Major depots for retained radioactivity were the gut (24% of the administered oral dose, 18.8% of the administered topical dose) and integument (12.2% of the oral dose and 30.7% of the topical dose). The variation in tissue distribution of dihydroazadirachtin with respect to the mode of application is discussed. A single polar metabolite fraction was obtained from the frass of dihydroazadirachtin-fed larvae. The physiological and behavioral effects of 22,23-dihydroazadirachtin and azadirachtin are quantitatively similar. © 1994 Wiley-Liss, Inc.
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    Controlled ecdysteroid accumulation in eggs of the silkworm, Bombyx mori, by an imidazole compound (KK-42), and embryogenesis in these eggs (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 121-135 
    Details
    ISSN: 0739-4462
    Keywords: follicles ; oogenesis ; fertilization ; hatching ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: An imidazole compound (KK-42), a potent inhibitor of ecdysone synthesis, was applied to the female pharate adult of the silkworm, Bombyx mori, to control ecdysteroid accumulation in developing ovaries and mature eggs. KK-42 applied on day 2 or later completely suppressed an increase in ecdysteroid content in developing ovaries. The inhibitory action of KK-42 was restricted to vitellogenic follicles, i.e., those in which active ecdysteroid synthesis is occurring. Ecdysteroid content in the mature eggs of moths remained at the level accumulated in ovaries before KK-42 application. Thus, KK-42 was shown to be a novel agent to suppress the ecdysteroid accumulation in eggs. Eggs containing different amounts of ecdysteroids showed different levels of embryonic development. About 80% of the eggs which contained less than 10 ng free ecdysteroids/g eggs were not fertilized. More than 80% of the eggs containing less than 40 ng/g eggs of free ecdysteroids initiated embryogenesis but failed to hatch. Larvae hatched from almost all eggs which accumulated free ecdysteroids of more than 150 ng/g. Thus, maternal ecdysteroids appear to be required at different titers for fertilization, embryogenesis, and hatching of the silkworm larvae. © 1994 Wiley-Liss, Inc.
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    Properties and significance of a riboflavin-binding hexamerin in the hemolymph of Hyalophora cecropia (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 137-157 
    Details
    ISSN: 0739-4462
    Keywords: vitellogenin ; flavin fluorescence ; pupal-adult molt ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A riboflavin-binding hexamerin isolated from pupal hemolymph of Hyalophora cecropia has a native Mr of 510,000, subunit Mr of 85,000, and a 5% carbohydrate content. An intrachain cross-link was confirmed in protease limit digests. Ellman titration confirmed the presence of a sulfhydryl group, which is needed for this linkage. Though Cu2+ is known to promote the linkage, heavy metals were not detected in the isolate. Heat denaturation released ligand with the absorbency, fluorescence spectra, and chromatographic behavior of riboflavin. Binding resulted in substantial quenching of the fluorescence of both the isoalloxazine in riboflavin and of aromatic groups in the apoprotein. Kinetic analysis indicated a KD of 2.5 × 10-7 M for riboflavin, 1.3 × 10-7 M for lumiflavin, and greater than 1 × 10-6 M for FMN and FAD. Over four moles of flavin were bound per mole of hexamerin. The amount of riboflavin in pupal hemolymph is sufficient to occupy only 2-3 of these sites. Riboflavin is also associated with lipophorin and vitellogenin, but the molar ratios after protein isolation were low. On a standard laboratory diet, riboflavin is in great excess, but most of it is apparently excreted before the apoprotein first appears in the hemolymph, just before wandering. The concentration of riboflavin-binding hexamerin rises to 15-30 mg/ml in pupae; relative to other hexamerins, very little is stored in the fat body. All of the apoprotein and 75% of riboflavin disappear from the hemolymph during adult development. An amount of flavin at least equal to that stored in pupal hemolymph is transferred to the eggs formed during this period. © 1994 Wiley-Liss, Inc.
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    Hydrocarbon biosynthesis in Triatoma infestans eggs (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 193-206 
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    ISSN: 0739-4462
    Keywords: fatty acid elongation ; methyl-branched lipids ; insect egg ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Triatoma infestans eggs are shown to synthesize hydrocarbons. Radio-gas chromatography was used to demonstrate metabolism of [1-14C]propionate into precursor methyl-branched fatty acids and into methyl-branched hydrocarbons in T. infestans eggs. These reactions have not been demonstrated previously in insect eggs. An in vivo study showed that hydrocarbons are also transported to eggs by the hemolymph. Inhibition of hydrocarbon synthesis by sodium trichloroacetate (NaTCA) was correlated with reduced oviposition, reduced hatchability, and reduced insect survival. Scanning electron microscopy showed impoverishment of the eggs' epicuticular waxes following NaTCA treatment. © 1994 Wiley-Liss, Inc.
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    Developmental changes and acetylcholinesterase activity in the metamorphosing brain of Tenebrio molitor: Correlation to ecdysteroid titers (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 207-226 
    Details
    ISSN: 0739-4462
    Keywords: Coleoptera ; metamorphosis ; molecular forms ; 20-hydroxyecdysone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The brain of Tenebrio molitor exhibited marked fluctuations in acetylcholinesterase (AChE) activity throughout metamorphosis. This was true AChE activity, since it was inhibited by high substrate concentrations and by 10 μM of the specific AChE inhibitor BW284C51 [(1,5-bis'4-allyldimethylammoniumphenyl)-pentan-3-one dibromide] but not by iso-OMPA (tetraisopropylpyrophosphoramide), a cholinesterase (but not AChE) inhibitor. The histochemical AChE activity was localized in the neuropile and the nuclear envelope of neurons and glial cells. The enzyme extracted from brains with 1% Triton X-100 and 1 M NaCl sedimented as a single peak in a sucrose density gradient, with a sedimentation coefficient of 5.4S. This single AChE sedimentation peak was mainly due to an amphiphilic dimeric form. AChE activity per brain increased in newly ecdysed pupa. AChE activity per milligram of protein exhibited a peak in the mid-pupa which could be correlated to the increase in ecdysteroid titers. © 1994 Wiley-Liss, Inc.
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    Characterization of a 24 kD parasitism-specific hemolymph protein from pharate pupae of the caribbean fruit fly, Anastrepha suspensa (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 227-244 
    Details
    ISSN: 0739-4462
    Keywords: sialoglycoproteins ; host-parasite relationship ; microheterogeneity ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A parasitism-specific protein was originally identified in the hemolymph of the Caribbean fruit fly Anastrepha suspensa parasitized by the braconid wasp Diachasmimorpha (Biosteres) longicaudata using single-dimensional (1-D) sodium dodecyl sulfate (SDS) PAGE. We now show that the protein is comprised of two closely migrating species both of which are glycoproteins of ≍ 24,000 Daltons (24 kD). The proteins were poorly resolved from whole hemolymph by 1-D SDS PAGE, but were well resolved by two-dimensional (2-D) PAGE and isoelectric focusing. They have pl's of ≍ 6.3 and 6.7 and contain Man residues, based on their affinity for concanavalin A (Con A). The presence of GlcNAc, NeuAc, and GalNAc residues in both proteins was implicated by their binding to wheat germ agglutinin (WGA). The proteins bound WGA more intensely following mannosidase treatment which eliminated their affinity to Con A and further implicated the presence of internal GlcNAc residues. However, binding of the proteins to WGA in the presence of competing GlcNAc (1 M) was reduced but not eliminated and suggested that in addition to GlcNAc, other WGA-binding sugar moieties, possibly NeuAc, a Sia, were present. To evaluate the presence of NeuAc, we treated the hemolymph with Vibrio cholerae neuraminidase which specifically cleaves terminal Sia. Samples of the neuraminidase-digested proteins were evaluated by WGA binding and Western blotting with the use of an anti-24 kD rabbit polyclonal serum to determine whether desialation eliminated the proteins' affinity to WGA or their immunoreactivity. Our results show that partial digestion of the 24 kD proteins with Vibrio cholerae neuraminidase resulted in two immunoreactive bands in Western blots of 1-D gels but only one of these, the upper undigested 24 kD band, bound WGA. This confirmed the presence of Sia residues in the proteins and demonstrated that desialation increased their relative electrophoretic mobilities. © 1994 Wiley-Liss, Inc.
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    Chitin synthesis in Spodoptera frugiperda wing imaginal discs: I. Chlorfluazuron, diflubenzuron, and teflubenzuron inhibit incorporation but not uptake of [14C]N-acetyl-D-glucosamine (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 245-258 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroid ; 20-hydroxyecdysone ; tissue culture ; benzoylphenyl urea ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The purpose of this study was to determine the effects of potent inhibitors of chitin synthesis on an organ culture test system as a basis for determining the mode of action of such compounds. Consequently, we investigated the action of chlorfluazuron (CFA), diflubenzuron (DFB), and teflubenzuron (TFB) on uptake and incorporation into chitin of [14C]N-acetyl-D-glucosamine ([14C]GlcNAc) in wing imaginal discs cultured in vitro. Spodoptera frugiperda wing imaginal discs provided a highly responsive test system for studying the inhibition of ecdysteroid-dependent chitin synthesis in a target tissue in vitro.All three inhibitors blocked ecdysteroid-dependent [14C]GlcNAc incorporation into chitin by the wing imaginal discs. The effectiveness of the inhibitors was not affected by the time of their application, i.e., exposures before, during, or after 20-hydroxyecdysone treatment were equally effective in inhibiting chitin synthesis. Thus, exposure of freshly dissected discs to CFA for periods as short as 15 min inhibited approximately 90% of the chitin synthesis measured 72 h later. In contrast to previous in vivo studies all three inhibitors were similar in their effectiveness in vitro. However, while all three compounds inhibited [14C]GlcNAc incorporation in a similar dose-dependent manner, only DFB and TFB reduced but did not block uptake of GlcNAc. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
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    Regulation of pheromone production in virgin and mated females of two tortricid moths (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 271-285 
    Details
    ISSN: 0739-4462
    Keywords: Epiphyas postvittana ; Planotortrix octo ; pheromone biosynthesis-activating neuropeptide ; PBAN ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Sex pheromone titers in females of two tortricid moths, Epiphyas postvittana and Planotortrix octo, did not significantly vary between the scotophase and photophase. Pheromone production in these two species is controlled by a factor located in the head of the respective females, probably the pheromone biosynthesis-activating neuropeptide (PBAN). Unlike that reported for the related tortricid, Argyrotaenia velutinana, the bursa copulatrix in female E. postvittana and P. octo does not appear to contain a factor that stimulates pheromone production. After mating, female E. postvittana permanently shut down pheromone production. In contrast, pheromone titer in mated P. octo females is reduced to a level approximately half that of similar-age virgins. While the abdominal nervous system is involved in the inactivation of pheromone production in mated E. postvittana females and probably acts to stop release of PBAN from the corpora cardiaca, the abdominal nervous system is not involved in effecting the decreased pheromone titers of mated P. octo females. It is possible that in the latter species, a humoral factor(s) is responsible for effecting the decreased pheromone titers, possibly through affecting the release of PBAN from the corpora cardiaca. Bioassaying head extracts allowed changes in PBAN titer in female E. postvittana to be inferred. PBAN titers remain roughly constant in virgins but increase after mating. This suggests that PBAN is biosynthesized throughout the life of an adult virgin female at approximately the same rate as it is released. Furthermore, it appears that the decline in pheromone titer observed in older E. postvittana females is probably due to a decline in competency of the gland to produce pheromone rather than to a decrease in PBAN titer in older females. © 1994 Wiley-Liss, Inc.
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    Pheromonotropic and pheromonostatic activity in moths (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 301-315 
    Details
    ISSN: 0739-4462
    Keywords: insects ; PBAN ; pheromone ; mating ; ecdysteroid ; RIA ; neuropeptide ; juvenile ; hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Pheromone biosynthesis in many species of moths requires a pheromonotropic neurosecretion, the pheromone biosynthesis activating neuropeptide (PBAN), from the brain-subesophageal ganglion-corpora cardiaca complex. Some investigators suggest that PBAN is released into the hemolymph and acts directly on sex pheromone glands (SPG) via a Ca++/calmodulin-dependent adenylate cyclase. Others suggest, however, that PBAN acts via octopamine that is released by nerves from the terminal abdominal ganglion innervating the SPG. These findings suggest that there are controversies on the mode of action of PBAN and other pheromonotropic factors, sometimes even within the same species.Mating in many insects results in temporary or permanent suppression of pheromone production and/or receptivity. Such a suppression may result from physical blockage of the gonopore or deposition of pheromonostatic factor(s) by the male during copulation that result in suppressed pheromone production and/or receptivity in females either directly or by a primer effect. In several species of insects, including moths, a pheromonostatic factor is transferred in the seminal fluid of males. Similar to the controversies associated with the pheromonotropic activity of PBAN, sometimes even within the same species, there appear to be controversies in pheromonostasis in heliothines as well.This paper reviews these conflicting findings and presents some data on pheromonostatic and pheromonotropic activity in Heliothis virescens that support and conflict with current information, raising further questions. Answers to some of the questions are partly available; however, they remain to be answered unequivocally. © 1994 Wiley-Liss, Inc.
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    Juvenile hormones: Their role in the regulation of the pheromonal communication system of the armyworm moth, Pseudaletia unipuncta (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 329-345 
    Details
    ISSN: 0739-4462
    Keywords: corpora allata ; pheromone biosynthesis ; calling behavior ; male responsiveness ; PBAN ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Recently, much effort has been devoted to the elucidation of the neuro-endocrine mechanisms regulating the biosynthesis and emission of sex pheromones in the Lepidoptera. The available data indicate that the hormonal mechanisms involved vary considerably among species. For example, compelling evidence that juvenile hormones (JH) play a role in the control of sex pheromone production has been presented only for the armyworm moth, Pseudaletia unipuncta. In this species, females that are allatectomized at emergence neither produce nor release pheromone, but both activities are restored following replacement therapy with synthetic JH. However, injection of synthetic JH into neck-ligated females does not induce pheromone biosynthesis, whereas treatment with either a brain homogenate or synthetic PBAN results in a rise in the pheromone titer. These results indicate that the role played by JH is an indirect one and that the tropic factor is a PBAN-like substance.Studies on in vitro JH biosynthesis by isolated corpora allata of P. unipuncta have shown that the low JH output observed early in the life of adult females coincides with the absence of both calling behavior and pheromone production. The subsequent increase in the rates of JH biosynthesis correlates with the onset of pheromone production and release. We have therefore proposed that JH titers must pass a threshold level before the circadian release of PBAN and calling behavior can begin. Furthermore, recent experiments suggest that the continuous presence of JH is necessary for calling behavior to be maintained once initiated. Lastly, we present data suggesting a role for JH or JH acids in the receptivity of P. unipuncta males to the female sex pheromone. © 1994 Wiley-Liss, Inc.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994) 
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    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
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    Cellular defense mechanisms in C. capitata: Recognition and entrapment of E. coli by hemocytes (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 1-14 
    Details
    ISSN: 0739-4462
    Keywords: cellular immunity ; phenoloxidase ; Diptera ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The mechanism of recognition of foreignness and entrapment of invaders by the immune system of insects is unknown. In this report using hemocyte monolayer preparations and biochemical analysis we demonstrate the requirements for recognition of E. coli in vitro, their entrapment by hemocytes, and nodule formation. A model system consisting of an isolated hemocyte protein (47 KDa), isolated hemocyte tyrosinase, isolated hemocytes, tyrosine, and E. coli was used to obtain these results. The 47 kDa polypeptide has the ability to form adducts with tyrosine derivatives generated by the action of tyrosinase and to attach to the E. coli surface. The latter process takes place independently of tyrosinase activity. When the E. coli-47KDa protein complex was overlaid on hemocyte monolayers followed by tyrosine and tyrosinase or vice versa, the bacteria were entrapped by hemocytes. The same results were obtained when the monolayers were overlaid with 47 KDa protein, followed by E. coli-47 KDa protein complex and then tyrosine and tyrosinase. The same experimental procedure in test tubes resulted in nodule formation. These results permit us to propose that the most likely explanation for the entrapment of E. coli to hemocytes and the formation of nodules is the production of E. coli-47 KDa complexes, and their crosslinking through a quinone intermediate generated by the action of tyrosinase on hemocytes. © 1994 Wiley-Liss, Inc.
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    Storage protein uptake in helicoverpa zea: Arylphorin and VHDL share a single receptor (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 15-26 
    Details
    ISSN: 0739-4462
    Keywords: receptor mediated endocytosis ; storage protein receptor ; arylphorin ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The major lepidopteran storage protein arylphorin is selectively taken up into perivisceral fat body of prepupae by receptor mediated endocytosis. The arylphorin receptor was identified by ligand blotting and in vitro binding studies. Fat body membranes contain a glycosylated receptor protein with an apparent molecular weight of 80,000 that binds arylphorin with a KD of 9.02 × 10-8 M. Competitive binding experiments revealed that the arylphorin receptor is identical with the previously identified VHDL receptor. Apparently a single receptor mediates the uptake of structurally distinct storage proteins. This storage protein receptor is present only in perivisceral fat body and only during the period around pupation when both storage proteins are sequestered. © 1994 Wiley-Liss, Inc.
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    Peptide amidation in an invertebrate: Purification, characterization, and inhibition of peptidylglycine α-hydroxylating monooxygenase from the heads of honeybees (apis mellifera) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 27-48 
    Details
    ISSN: 0739-4462
    Keywords: neuropeptide formation ; inhibition of amidating enzyme ; glycyl peptide hydroxylation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Peptidylglycine α-hydroxylating monooxygenase (PHM), an enzyme involved in formation of neuropeptides with a C-terminal amide functionality in mammals and amphibians, was isolated from the head of an invertebrate, the honeybee, Apis mellifera, and purified 220-fold in 1% overall yield. The bee PHM has a molecular weight of 71,000, is membrane associated but can be solubilized with a detergent (n-octyl-β-D-glucopyranoside), and cross-reacts with rabbit antibodies generated toward bacterially expressed rat PHM. In the presence of copper, oxygen, and ascorbic acid, the enzyme hydroxylates model tripeptides such as dansyl-L-Phe-L-Phe-Gly on the methylene carbon of the glycine residue with retention of configuration. Using this tripeptide as substrate, the Km is 1.7 μM and the Vmax is 2.3 nmol • μg-1 • h-1. Treatment of the insect PHM with D-Phe-L-Phe-D-vinylglycine, a substrate analogue and mechanism-based inactivator of PHM from pig pituitary, results in irreversible loss of activity. The diastereomeric analogue, D-Phe-L-Phe-L-vinylglycine, is only a competitive inhibitor (lC50 = 320 μM). © 1994 Wiley-Liss, Inc.
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    Biosynthesis of sorbic acid in aphids: An investigation into symbiont involvement and potential relationship with aphid pigments (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 49-67 
    Details
    ISSN: 0739-4462
    Keywords: 2,4-hexadienoic acid ; triglyceride ; mycetocyte ; UV ; antibiotic ; aphin ; acetogenin ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Studies were undertaken to determine the role of symbionts and UV exposure in biosynthesis of the aphid-specific polyketides, sorbic acid and quinone pigments. Injection of adult potato aphids, Macrosiphum euphorbiae (Thomas), with the antibiotic rifampicin did not alter the level of sorbic or myristic acid in triglycerides of resultant progeny; pigmentation was also unaffected. However, antibiotic injection did produce marked physiological effects; progeny from injected aphids were smaller, slower to mature, and not fecund. Light microscopy confirmed that only 8% of rifampicin-treated aphids contained mycetocytes; thus, symbiont involvement in the production of this unusual UV-quenching short chain fatty acid is not supported. Following multigenerational exposure to long wavelength UV light, no substantial changes in sorbic acid content were detected in the potato aphid or the oleander aphid, Aphis nerii Fonscolombe. Pigments from UV-exposed oleander aphids had a peak absorbance at 390 nm, 70 nm lower than unexposed aphids. This suggests a photo-protective role for the pigments of the sunlight-inhabiting A. nerii; by contrast, no changes were observed in pigments of M. euphorbiae which usually feeds in the shade. Injection of adult potato aphids with sodium [1-14C]-acetate rapidly labeled both sorbic acid and pigments, particularly among the latter a yellow pigment which co-chromatographed with the dominant C15 yellow pigment of the oleander aphid. These data support the hypothesis that aphid C30 pigments are built up by coupling of “monomeric type” C15 pigments. Although aphid and not symbiont enzymes appear to synthesize these acetogenins, a possible biosynthetic link between sorbic acid and aphid pigments requires further clarification. © 1994 Wiley-Liss, Inc.
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    Effect of the pheromone biosynthesis activating neuropeptide on sex pheromone biosynthesis in Spodoptera littoralis isolated glands (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 77-87 
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    ISSN: 0739-4462
    Keywords: Spodoptera littoralis ; sex pheromone ; pheromone biosynthesis activating neuropeptide ; hormonal control ; reduction ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The control of Spodoptera littoralis sex pheromone biosynthesis has been investigated with synthetic pheromone biosynthesis activating neuropeptide (PBAN) and different labeled tracers using an in vitro isolated gland system. Responsiveness of the glands to PBAN stimulation was impaired by careless tissue manipulation. The fact that PBAN is active in the isolated gland system suggests that this might be a target organ for this peptide in S. littoralis. As reported previously with Br-SOG extracts and intact females, label incorporation into the pheromone increased in glands treated with PBAN from all the precursors tested. However, the formation of labeled intermediates from d5E11-14:Acid also occurred in glands incubated in the absence of the peptide, but the amounts of d5Z9, E11-14:Acid were lower in PBAN treated glands than in controls. These results indicate that PBAN controls pheromone biosynthesis in S. littoralis by regulating the reduction of acyl moieties. © 1994 Wiley-Liss, Inc.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
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    Cyclodiene resistance at the insect GABA receptor/chloride channel complex confers broad cross resistance to convulsants and experimental phenylpyrazole insecticides (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 69-79 
    Details
    ISSN: 0739-4462
    Keywords: cyclodienes ; insecticide resistance ; convulsants ; chloride channel ; GABA receptor ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: This study investigated the pharmacological profile of cyclodiene resistance in Drosophila melanogaster and the mode of action of a phenylpyrazole insecticide, JKU 0422. Toxicological studies were performed with a sucrose bait assay containing the synergist piperonyl butoxide. The Maryland strain of D. melanogaster was resistant to dieldrin, lindane, picrotoxinin, TBPS, p-CN-TBOB, and JKU 0422. In contrast, this strain was susceptible to cypermethrin and the avermectins MK-243, abamectin, and abamectin 8,9-oxide. Neurophysiological studies showed that both TBPS and JKU 0422 reversed the inhibitory action of GABA in central nerve preparations from susceptible D. melanogaster. However, the response to these compounds was attenuated in nerve preparations from the resistant Maryland strain, which indicated that the resistance was expressed at the level of the nerve. Topical toxicity bioassays with JKU 0422 on susceptible (CSMA) and cyclodiene-resistant (LPP) strains of German cockroach revealed a resistance ratio of 553-fold for this compound. These studies demonstrate that cyclodiene resistance in D. melanogaster confers broad cross resistance toward compounds thought to block the GABA-gated chloride channel in a manner similar to the cyclodienes. Moreover, the cross resistance extends to JKU 0422, and resistance to this compound is also present in a strain of cyclodiene-resistant German cockroach. These toxicological results, along with the neurophysiological studies, confirm that JKU 0422 has a mode of action that is similar to the cyclodienes and TBPS. These findings suggest that the introduction and use of new chloride channel antagonists as insecticides should be managed carefully in order to prevent the rapid development of resistance in the field. © 1994 Wiley-Liss, Inc.
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    Octopamine enhances phagocytosis in cockroach hemocytes: Involvement of inositol trisphosphate (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 249-261 
    Details
    ISSN: 0739-4462
    Keywords: amine ; IP3 ; insect defense ; agonist ; antagonist ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Octopamine and 5-hydroxytryptamine (5-HT) were previously shown to affect phagocytosis in cockroach hemocytes through unidentified receptor-mediated events. In the present study, we examined the ability of 5-HT and octopamine to enhance inositol trisphosphate (IP3) production using hemocyte membranes of the American cockroach, Periplaneta americana. Octopamine enhanced IP3 production with a maximal peak at 100 nM. Similarly, 5-HT enhanced IP3 production with a maximal effect at 10 nM. The effects of 5-HT and octopamine are not additive, suggesting that both are working through the same receptor. Phentolamine, a general octopamine antagonist, blocked the effects of octopamine and 5-HT, while a mammalian 5-HT2 antagonist that blocks 5-HT-sensitive receptors in insect peripheral tissue, ketanserin, did not. A pharmacological profile indicates that the receptor is similar to an octopamine1-type.Octopamine at 1 μM increased phagocytosis in cockroach hemocytes exposed to Staphylococcus aureus in vitro, and this effect was mimicked by IP3 (10 μM). The octopamine-treated hemocytes were shown to increase IP3 production in the latter stage of phagocytosis.Adult cockroaches exposed to an LD50 dose of S. aureus in conjunction with either 0.1 mM octopamine or the octopamine1 agonist, clonidine, had higher survival rates compared to saline-treated cockroaches. Correspondingly, the octopamine1 antagonist, chlorpromazine, partially blocked the octopamine-mediated increase in cockroach survival. © 1994 Wiley-Liss, Inc.
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    Covalent modificaition of juvenile hormone binding proteins by photoaffinity labeling: An unexpected gel shift effect (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 287-297 
    Details
    ISSN: 0739-4462
    Keywords: methyl farnesoate ; methoprene analog ; JH II analog ; Manduca sexta ; hemolymph ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The 32 kD juvenile hormone binding protein (JHBP) and two 80 kD proteins in larval Manduca sexta hemolymph were labeled with [3H]FDK, a photoaffinity analog of methyl farnesoate (MF). The labeling could be completely displaced by a 30-fold excess of either MF or JH II, demonstrating that [3H]FDK binds specifically to the JH binding sites of the 32 kD JHBP and the 80 kD proteins. In addition, a high molecular-mass protein was labeled with [3H]FDK; labeling could be displaced by excess MF but not by JH II, demonstrating the selectivity in binding MF. The 32 kD JHBP also appeared to weakly bind the potent juvenoid, methoprene, at the JH binding site.Covalent modification by [3H]FDK induced a change in the apparent size and the isoelectric point of the JHBP. These changes were not induced by substrate alone, nor by UV irradiation alone. The same effect was also observed during labeling with [3H]MDK, an analog of methoprene. These data provide an important caveat for anticipating artifactual changes of protein properties during chemical or photochemical affinity labeling experiments. The molecular dimensions of [3H]FDK more closely resemble those of JH II than those of [3H]EHDA, a photoactivatable analog of JH II. We suggest that covalent modification by a diazoketone photolabel involves a hydrophilic amino acid important in the recognition of the ester group of JH. © 1994 Wiley-Liss, Inc.
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    Occurrence of three different binding sites for Bacillus thuringiensis δ-endotoxins in the midgut brush border membrane of the potato tuber moth, phthorimaea operculella (zeller) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 315-327 
    Details
    ISSN: 0739-4462
    Keywords: Bacillus thuringiensis ; Phthorimaea operculella ; insecticidal crystal protein ; receptors ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The potato tuber moth is susceptible to at least three insecticidal crystal proteins (ICPs) from Bacillus thuringiensis: CrylA(b), CrylB, and CrylC. To design useful combinations of toxin genes either in transgenic plants or in new genetically modified B. thuringiensis strains, it is necessary to determine the binding characteristics of the different ICPs so as not to combine a pair sharing the same binding site. This has been accomplished using two different techniques: 125I-labeling of the ICPs with further measurement of the radioactivity bound to brush border membrane vesicles, and microscopic visualization of the bound ICPs by enzyme-linked reagents such as antibodies or streptavidin using biotinylated ICPs. Our results show that CrylA(b), CrylB, and CrylC bind to different sites in the brush border membrane of midgut epithelial cells. Also, the affinity of the binding sites for the ICPs and their concentration in brush border membrane vesicles has been determined in a laboratory strain and a storage collected population. No significant differences were found between these two strains. © 1994 Wiley-Liss, Inc.
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    Parasitoid-host interactions: Historical perspectives and current status (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 81-82 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The papers contained in this special issue of Archives of Insect Biochemistry and Physiology are published in connection with the symposium entitled “Physiological and Molecular Interactions Between Parasitoids and Their Hosts” held at the XIX International Congress of Entomology, Beijing, China. Speakers in the program discussed advances in the field and provided insight into future directions of study. As a preface to this special issue, we summarize the history of this field as reflected through the continuing series of symposia held in association with the International Congresses.
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    Changes in protein patterns in sperm and vas deferens during the daily rhythm of sperm release in the gypsy moth (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 65-75 
    Details
    ISSN: 0739-4462
    Keywords: circadian rhythms ; secretion ; epithelium ; sperm bundles ; Lymantria dispar ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the gypsy moth, Lymantria dispar, the release of sperm bundles from the testis into the upper vas deferens (UVD) is precisely timed within each 24 h period by a circadian mechanism located in the reproductive system. In males kept under light:dark cycles of 16:8, release of sperm bundles is limited to the 3 h period that starts before lights off. Sperm released from the testis remains in the UVD for about 12 h and then moves into the seminal vesicles, so that the UVD stays empty until the next cycle of sperm release begins. The rhythm of release appears to play a role in the terminal stages of sperm maturation and is essential for the fertility of males. Sperm bundles undergo substantial morphological changes during the release from the testis and while they are retained in the UVD. In this study, using gel electrophoresis, we compared protein patterns in sperm and in the UVD during the daily cycle of sperm release and maturation. Several protein bands evident in the sperm bundles contained in the testis were missing from the sperm bundles that had passed from the testis into the UVD. Furthermore, a number of new proteins appeared in the sperm bundles as they remained in the UVD. Some of these proteins appeared to be secreted from the UVD epithelium into the UVD lumen before being incorporated into sperm bundles. Correlations between changes in protein patterns and ultrastructural changes in sperm during the cycle of sperm release and maturation are discussed. © 1994 Wiley-Liss, Inc.
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    Isolation and characterization of a hemocyte aggregation inhibitor from hemolymph of Manduca sexta larvae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 123-136 
    Details
    ISSN: 0739-4462
    Keywords: hemolymph proteins ; tobacco hornworm ; hemolin ; HAIP ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A protein that inhibits hemocyte aggregation has been isolated from hemolymph of Manduca sexta larvae and named hemocyte aggregation inhibitor protein (HAIP). HAIP has a Mr = 50,000, pI = 8.5, and contains 7% carbohydrate. It is present at 230 ± 20 μg/ml in hemolymph of day 3 fifth instar larvae. Antibodies to HAIP do not cross-react with M. sexta hemolin, which is similar in size and charge and also inhibits hemocyte aggregation. HAIP and hemolin have some similarity in amino acid composition and NH2-terminal sequence, but are different in overall secondary structure, as determined by CD spectroscopy. The concentration of HAIP in hemolymph is not affected by injection of larvae with bacteria. A protein of approximately 50,000 daltons that reacts with antibody to M. sexta HAIP is present in hemolymph of Bombyx mori, Heliothis zea, and Galleria mellonella. Although the function of HAIP in vivo is not yet clear, it may have a role in modulating adhesion of hemocytes during defensive responses. © 1994 Wiley-Liss, Inc.
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    Molecular cloning of a Drosophila melanogaster gene coding for an homologue of human carboxypeptidase E (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 169-178 
    Details
    ISSN: 0739-4462
    Keywords: Carboxypeptidase B ; Carboxypeptidase E ; Carboxypeptidase M ; carboxypeptidase N ; proteolytic processing ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: PCR primers derived from two functional domains of vertebrate carboxypeptidase E (CPE) were used to generate a probe for screening a size-selected Drosophila melanogaster genomic library. A sequence representing about 50% of the expected complete sequence was obtained by translation of the two open reading frames present on a 1.6 kb DNA genomic fragment. This partial sequence, homologous to human CPE, CPM, and CPN, contained the conserved arginine and zinc binding domains. Similarities to the human enzymes were found with stretches that were equally divergent from the three vertebrate carboxypeptidases. Northern blot analysis revealed the presence of a 6.9 kb transcript for this gene in Drosophila embryos. I postulate that insects possess a single protein fulfilling CPE, CPM, and CPN functions. © 1994 Wiley-Liss, Inc.
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    “Reduced appendage”: A mutation affecting development of pupal and adult appendages of the moth, Plodia interpunctella (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 179-191 
    Details
    ISSN: 0739-4462
    Keywords: imaginal discs ; morphogenesis ; metamorphosis ; disc evagination ; Indianmeal moth ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A mutant that results in the reduced length of pupal and adult appendages was isolated from a laboratory colony of the Indianmeal moth, Plodia interpunctella (Hübner). “Reduced appendage” (rda) was determined to be an autosomal recessive mutation that affects the development of pupal and adult appendages during the larval/pupal molt. The rda mutation had no observed effect on the larval phenotype. After pupation, the appendages of rda were reduced in size as compared with wild-type. In addition, unsclerotized cuticle underlying the pupal appendages was exposed and the establishment of the boundary between the unsclerotized and sclerotized pupal abdominal cuticle appeared normal even though the imaginal discs of rda did not evaginate normally. This demonstrates that rda affects only imaginal discs and that the morphogenesis of structures that were not derived from the imaginal discs were not dependent on interactions with evagination of imaginal discs. Although the rda phenotype resulted in shorter antennae, mouth parts, legs, and wings in pupae and adults, the mutation did not affect the number of cells comprising the imaginal discs or the pupal appendages. Cell counts showed that forewing imaginal discs and pupal forewings from the rda mutants contained the same number of cells as did the imaginal discs and wings from the wild-type strain. Thus, rda appears to affect processes related to disc evagination and not cell proliferation. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
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    Aminopeptidase a from Rhynchosciara americana (Diptera) larval midguts: Properties and midgut distribution (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 301-315 
    Details
    ISSN: 0739-4462
    Keywords: aminopeptidase A ; aminopeptidase N ; terminal digestion ; aminopeptidase properties ; soluble aminopeptidases ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: L-aspartic acid α-(β-naphthylamide) (AspβNA) hydrolase activity is restricted mostly to the midgut caeca of Rhynchosciara americana larvae. The membrane-bound activity is solubilized in detergent and, after electrophoretic separation, proved to be identical to leucine p-nitroanilide (LpNA) hydrolases previously described. Differential centrifugation of midgut caeca homogenates, followed by assays of enzyme markers and aminopeptidase, suggests that the soluble AspβNA hydrolase is associated with the cell glycocalyx. Soluble aminopeptidases from R. americana midgut caeca are resolved into three fractions by gel electrophoresis. The slow migrating fraction hydrolyzes AspβNA well and displays a low activity on LpNA and proline β-naphthylamide (ProβNA). Thus, this enzyme is an aminopeptidase A (EC 3.4.11.7). It has a pH optimum of 7.5, Mr 117,000 (gel filtration), and is competitively inhibited by aspartate hydroxamate (Ki 0.1 mM). Nevertheless, this enzyme, in contrast to the vertebrate enzyme, is not activated by calcium ions. The aminopeptidase A seems to have a charge variant that displays an intermediate migration and is not resolved from an aminopeptidase N (enzyme very active on LpNA). These two activities are not resolved by either gel filtration or ion-exchange chromatography. The aminopeptidases N with intermediate and high migration, previously reported to be charge variants, were shown in this paper to differ in substrate specificities and in the strength with which they associate to the cell glycocalyx. © 1994 Wiley-Liss, Inc.
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    Development and partial characterization of monoclonal antibodies to venom of the parasitoid microplitis demolitor (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 123-136 
    Details
    ISSN: 0739-4462
    Keywords: polydnavirus ; hemolymph ; soybean looper ; braconid ; parasite ; wasp ; Lepidoptera ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The venom of Microplitis demolitor consists of a mixture of proteins. On native PAGE gels three major proteins designated a, b, and g were detected, while on SDS-PAGE gels two major proteins of Mr 64.5 and 30.8 kD and several minor proteins were detected. No proteins smaller than Mr 30.8 kD were present. Murine monoclonal antibodies were generated against different venom components. Analysis by Western blot of venom proteins separated on native and SDS-PAGE gels confirmed that antibodies from seven hybridoma lines recognized venom components. Two of the seven hybridoma lines reacted specifically with protein g on native PAGE gels and the Mr 30.8 k protein on SDS-PAGE gels, while four other lines cross-reacted with these and other venom proteins. The final hybridoma line reacted with protein a when venom was separated on native PAGE gels and an array of proteins when venom was separated on SDS-PAGE gels. Using an enzyme-immunoassay and specific monoclonal antibodies, M. demolitor females were estimated to inject 0.02 - 0.05 venom gland reservoir equivalents into its host, Pseudoplusia includens, at oviposition. Venom proteins persisted in host hemolymph for 6 - 12 h before dropping to undetectable levels. © 1994 Wiley-Liss, Inc.
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    Cloning of a VLP-protein coding gene from a Parasitoid Wasp Venturia canescens (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 137-145 
    Details
    ISSN: 0739-4462
    Keywords: VLP-protein ; Venturia canescens ; hybridization ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Virus-like particles (VLPs) that are bound to the egg surface of a parasitic wasp Venturia canescens are void of nucleic acid and unable to infect host tissue but instead provide a passive protection against the host's immune recognition. To investigate evolutionary and functional properties of Venturia particles, we isolated cDNAs coding for a VLP-protein by screening an expression library of the wasp, using antibodies against purified VLPs. The corresponding coding DNA is present in the wasp genome as a single-copy gene. © 1994 Wiley-Liss, Inc.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940270101
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    Effects of a nonsteroidal ecdysone agonist, tebufenozide, on host/parasitoid interactions (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 235-248 
    Details
    ISSN: 0739-4462
    Keywords: Ascogaster quadridentata ; Cydia pomonella ; testes ; tebufenozide ; codling moth ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Tebufenozide (RH-5992), a nonsteroidal ecdysone agonist, stimulated significant (P ≤ 0.05) growth in both testes of post-diapausing codling moth larvae and a dormant Ascogaster larva in its overwintering host's hemocoel. Tebufenozide elicited the same responses in post-diapausing testes and Ascogaster larvae as were reported earlier in insects treated with 20-hydroxyecdysone (20-OHE) [Friedlander, J Insect Physiol 35:29 (1989); Brown et al., Endocrinological Frontiers in Physiological Insect Ecology. Wroclaw: Wroclaw Technical University Press, pp 443-447 (1988)]. Only a trace (≤ 1%) of 14C-tebufenozide was recovered from gonads and exuviae of healthy larvae, or from Ascogaster larvae removed from parasitized hosts; however, the renewed growth of testes and Ascogaster larvae and apolysis of codling moth integument were an obvious response to the hormone agonist. Most of the injected 14 C-tebufenozide was recovered from host fat body, while the alimentary canal retained approximately 40% of the 14 C-tebufenozide fed in an artificial diet.Host exposure to tebufenozide did not cause apolysis in endo- or ectoparasitic hymenopterans feeding on treated codling moth larvae; however, the endoparasitoid trapped in the host's hemocoel died as its host's tissue deteriorated. Different results were observed on ectoparasitoids developing on treated hosts. Ectoparasitic Hyssopus sp. (Eulophidae) larvae feeding on tebufenozide treated hosts pupated in the normal length of time. Hyssopus adults which developed from larvae fed tebufenozide treated hosts were fertile and produced as many progeny as adults reared from solvent fed controls. There was no evidence of secondary poisoning to Hyssopussp. and codling moth exposure to tebufenozide may actually benefit the rearing of this eulophid by maintaining the host in the susceptible larval stage and preventing the host larva from spinning a cocoon. © 1994 Wiley-Liss, Inc.
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    Biosynthesis of (10R)-Juvenile hormone III from farnesoic acid by Aedes aegypti ovary (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 11-25 
    Details
    ISSN: 0739-4462
    Keywords: hormone ; HPLC ; gas chromatography ; tissue culture ; methoxyhydrin derivative ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Synthesis of (10R)-juvenile hormone III (JH III) outside the corpora allata (CA) was investigated in female Aedes aegypti. Intact females or ligated abdomens of blood-fed and sugar-fed females synthesized in vivo [12-3H]JH III-like molecules from [12-3H]-methyl farnesoate, indicating that an organ(s) in the female abdomen, other than the CA, converted methyl farnesoate into JH III. To find out the organ(s) that synthesized JH III-like molecules, ovaries, fat bodies, and midguts were incubated in vitro with [12-3H]methyl farnesoate and the synthesis of JH III-like molecules was compared with JH III synthesized by CA. To identify tissue(s) having both farnesoic acid methyl transferase and farnesoate epoxidase, enzymes that convert farnesoic acid into JH III, ovaries, and fat bodies were removed from sugar and blood-fed females and incubated with [12-3H]farnesoic acid. Chemical derivatization by methoxyhydrin formation followed by esterification with (+)-α-methoxy- α-trifluoromethyl phenylacetic (MTPA) acid chloride and reversed phase liquid chromatography identified (10R)-JH III methoxyhydrin (+)-MTPA ester as the sole JH III-like molecule produced in tissue culture incubation of ovaries. Since only (10R)-JH III is produced and not racemic JH III, the oxidation of farnesoic acid must be enzymatically mediated. Ovaries and corpora allata of female A. aegypti also synthesized [3H,14C]JH III from L-[methyl-3H]methionine and [14C]acetate which was characterized by HPLC and gas chromatography. These results suggest that mosquito ovary can synthesize (10R)-JH III from farnesoic acid, and that this tissue synthesizes JH III-like molecules from L-methionine and acetate. © 1994 Wiley-Liss, Inc.
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    Chitin synthesis in Spodoptera frugiperda wing imaginal discs. II. Selective action of chlorfluazuron on wheat germ agglutinin binding and cuticle ultrastructure (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 89-108 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroid ; 20-hydroxyecdysone ; benzoylphenyl urea ; tissue culture ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The action of the chitin synthesis inhibitor, chlorfluazuron, was investigated in Spodoptera frugiperda wing imaginal discs cultured in vitro. Electron microscopy and cytochemical labeling with a lectin, wheat germ agglutinin (WGA), were used to monitor morphogenesis, as well as the presence and localization of chitin and non-polymerized N-acetyl-D-glucosamine (GlcNAc). Chlorfluazuron (CFA) selectively inhibited 20- hydroxyecdysone-stimulated chitin synthesis and procuticle deposition in imaginal discs, without otherwise affecting their morphogenesis. Tracheole migration, evagination, exocytosis, and endocytosis in the epithelial cells, and the presence of non-polymerized GlcNAc in the extracellular matrix, were observed in both CFA-treated and control wing discs. On the other hand, CFA prevented the appearance of WGA-labeled chitin in newly formed procuticle, while the deposition of proteinaceous cuticulin and epicuticle was unaffected. A brief treatment with CFA resulted in WGA labeling of non-polymerized GlcNAc, but not chitin in the procuticle region. The lack of chitin in CFA treated wing discs was correlated with the appearance of an amorphous, non-lamellar procuticle region. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940270301
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    Immunological analysis of lipophorin in the haemolymph, ovaries, and testes of the fall webworm, Hyphantria cunea (Drury) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 153-167 
    Details
    ISSN: 0739-4462
    Keywords: haemolymph ; fat body ; testis ; lipophorin ; vitellogenesis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Lipophorin (LP) was purified from haemolymph in last instar larvae of Hyphantria cunea (Drury) by KBr density gradient ultracentrifugation and gel filtration. LP is composed of Apo-LP I and Apo-LP II with molecular weights of 230 kDa and 80 kDa, respectively.The level of haemolymph LP in early pupae was somewhat greater than in last instar larvae. In males, this LP concentration is maintained throughout pupal development, whereas the level of haemolymph LP decreases in female pupae beginning at day 7, coincident with the onset of vitellogenesis in the fall webworm. In both male and female adults, haemolymph LP concentrations were dramatically increased in comparison to their pre-adult levels. Actually, LP was found in the ovary by immunodiffusion, tandem-crossed immunoelectrophoresis, and Western blotting. Location of LP in the ovary was also traced by immunogold labelling. Also, LP appeared in small amounts in protein yolk bodies of the ovary at an early stage of vitellogenesis, when nurse cells are bigger than the oocyte, but in greater amounts at those stages when the oocyte is larger than nurse cells - that is, when vitellogenesis is actively taking place. This fact clearly reveals that LP is synthesized by fat body and released into the haemolymph, and then taken up by the growing ovary during vitellogenesis. Also, LP was detected in testes by immunological analysis. Western blotting showed that LP was present in testicular fluid but not in the peritoneal sheath and cysts. To test whether LP is also synthesized in testes, testes and fat body tissues were cultured in vitro, indicating that fat body synthsizes LP but testes do not. The result showed that the haemolymph LP itself is taken up into the testes. © 1994 Wiley-Liss, Inc.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940270401
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    Glycosylation and adhesiveness differentiate larval Ceratitis capitata tyrosinases (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 235-248 
    Details
    ISSN: 0739-4462
    Keywords: phenoloxidases ; Ceratitis capitata ; tyrosinase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Larval Ceratitis capitata phenoloxidases (POs) from hemocytes, serum, integument, and fat body were analyzed. Two types of PO were recorded: the tyrosinase type found in hemocytes, serum, integument, and fat body and the laccase type found in integument. Tyrosinase from all larval tissues and integumental laccase as well, showed similarity in molecular weight (93 KDa), activation by Escherichia coli at 5 mM Ca2+, and reactivity to antibodies raised against serum tyrosinase. However, the enzymes differed with respect to their glycosylation and adhesiveness. The serum and integumental enzyme forms contain concanavalin A reacting material, whereas hemocyte and integumental tyrosinase(s) are adhesive. These differences in enzyme forms, although not influencing their substrate specificity, seem to give advantages to performing their function, i.e., the adhesive enzyme form facilitates the adherence to E. coli cell wall and hemocyte surface (unpublished data) while the glycosylated form facilitated the secretion into serum. © 1994 Wiley-Liss, Inc.
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    Purification of a 24 kD parasitism-specific hemolymph protein from pharate pupae of the caribbean fruit fly, Anastrepha suspensa (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 265-285 
    Details
    ISSN: 0739-4462
    Keywords: chromatographic purification ; glycoforms ; protein sequence ; parasitism- specific protein ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report purification of a 24 kD parasitism-specific protein (24 kD PSP) from pharate pupal hemolymph of the Caribbean fruit fly, Anastrepha suspensa, after parasitization by the braconid wasp, Diachasmimorpha (= Biosteres) longicaudata. We previously utilized isoelectric focusing (IEF) and two-dimensional (2-D) gel electrophoresis to demonstrate that the 24 kD PSP consists of two variants with pl 6.7 (more abundant) and pl 6.3. Purification of the more abundant 24 kD PSP variant was accomplished by Concanavalin A (Con A) sepharose B affinity chromatography followed by DEAE column chromatography. A second protocol, utilizing wheat germ agglutinin (WGA) sepharose 6MB affinity chromatography between the ConA and DEAE chromatographic steps, resulted in the purification of a partially deglycosylated form of the 24 kD PSP which retained its immunore-activity with anti-PSP serum but which exhibited a greater relative migration in sodium dodecyl sulfate (SDS)-PAGE than the pl 6.7 24 kD PSP variant.For structural studies both 24 kD PSP variants were purified from whole hemolymph by flat bed IEF followed by SDS-PAGE. Peptide cleavage profiles in 1-D SDS-PAGE after treatment with BNPS-skatole, CNBr, and endproteinases Lys-C and Asp-N were identical for both 24 kD PSP variants. Primary N-terminus sequences of at least the first 20 amino acid residues of both variants were identical. A secondary sequence of five amino acids residues was detected in both variants at Thr, the seventh amino acid residue from the N-terminus of the primary sequence. These data indicate that both 24 kD PSPs are glycoforms of a branched, apparently homogeneous polypeptide. © 1994 Wiley-Liss, Inc.
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    Steady-state gradient in calcium ion activity across the intercellular bridges connecting oocytes and nurse cells in Hyalophora cecropia (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 9-20 
    Details
    ISSN: 0739-4462
    Keywords: ion-selective microelectrode ; ovarian follicle ; K+ ; Cl- ; Mg2+ ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Intracellular activities of K+, H+, Mg2+, Ca2+, and Cl-, measured with ion selective microelectrodes in the oocyte and the nurse cells in ovarian follicles of Hyalophora cecropia, indicated that a Ca2+ current is a key component of the electrical potential that is maintained across the intercellular bridges connecting these two cells. In vitellogenic follicles, Ca2+ activity averaged 650 nM in the oocyte and 190 nM in the nurse cells, whereas activities of the other ions studied differed between these cells by no more than 6%. Incubation in 200 μM ammonium vanadate caused a reversal of electrical potential from 8.3 mV, nurse cell negative, to 3.0 mV, oocyte negative, and at the same time the Ca2+ gradient was reversed: activities rose to an average 3.0 μM in the nurse cells and 1.6 μM in the oocyte, whereas transbridge ratios of the other cations remained at 0-3%. In immature follicles that had not yet initiated their transbridge potentials, Ca2+ activities averaged ∼ 2 μM in both oocyte and nurse cells. The results suggest that vitellogenic follicles possess a vanadatesensitive Ca2+ extrusion mechanism that is more powerful in the nurse cells than in the oocyte. © 1994 Wiley-Liss, Inc.
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    Biogenic amines in the two-spotted spider mite (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 1-8 
    Details
    ISSN: 0739-4462
    Keywords: Acarina ; Tetranychus urticae ; octopamine ; dopamine ; 5-hydroxytryptamine ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Whole body extracts of the two-spotted spider mite (Tetranychus urticae Koch) were analyzed using a 16-channel electrochemical array high performance liquid chromatography (HPLC)-based detection system that allows the simultaneous isolation and identification of a variety of biogenic amines. The spider mite extracts were found to contain the biogenic amines octopamine, dopamine, and 5-hydroxytryptamine (5-HT), as well as several precursors and metabolites including tyrosine, tyramine, tryptophan, and N-acetyl octopamine. Differences in the levels of biogenic amines were observed between eggs and the adult stages and between males and females. This is the first direct determination of biogenic amines in the Tetranychidae and the first demonstration of 5-HT in any mite species. © 1994 Wiley-Liss, Inc.
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    Hsp 78: A prominent heat shock protein of the lepidopteran Choristoneura fumiferana that is immunologically unrelated to members of the major Hsp families (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994), S. 39-53 
    Details
    ISSN: 0739-4462
    Keywords: spruce budworm ; Cf1 cells ; heat shock response ; lepidopteran cells ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cultured cells of the spruce budworm (Choristoneura fumiferana) respond to heat shock with the new and/or enhanced synthesis of six proteins with Mrs of 84,000, 78,000, 70,000, 68,000, 21,000, and 14,000, as measured by one- and two-dimensional PAGE. The most prominent hsp of these cells is a 78,000 Da protein which is maximally induced at 39°C and which consists of three isoforms with different pl. Hsp 78 is found in the detergent-soluble cytosolic fraction of cell lysates. In vitro translation of RNA extracted from cultured cells and from larvae shows that the induction of hsp 78 is regulated mainly at the transcriptional level. Hsp 78 does not cross-react with a variety of antibodies made to members of the hsp 70 and hsp 83 families. In particular, antibodies to hsp 70 that do cross-react with a 70 kDa protein of C. fumiferana do not cross-react with hsp 78. Homologous 75-78 kDa hsps are also present in heat-shocked cells from other lepidopterans (Spodoptera frugiperda and Bombyx mori). Cf1 cells exposed to elevated levels of arsenite or cadmium respond with the new and/or enhanced synthesis of only two of their hsps (hsp 84 and hsp 70); hsp 78 is not induced by these treatments. The data suggest that hsp 78 of C. fumiferana represents a new family of hsps unique to lepidopterans. © 1994 Wiley-Liss, Inc.
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940250201
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    Masthead (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 25 (1994) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940250101
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    Premature production of late larval storage proteins in larvae of trichoplusia ni parasitized by euplectrus comstockii (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 97-109 
    Details
    ISSN: 0739-4462
    Keywords: Hymenoptera ; venom ; host hemolymph ; plasma proteins ; regulation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Investigations were conducted to determine the titer of storage proteins in larvae of the cabbage looper, Trichoplusia ni (Hübner), that were parasitized by the ectoparasitoid Euplectrus comstockii Howard (Hymenoptera: Eulophidae). A gradual increase was noted in the titer of the storage proteins present in the hemolymph of parasitized third and fourth instar larvae and in the hemolymph of isolated thoracic and abdominal tissues of fourth instar larvae. The final amount present in parasitized third and fourth instar larvae was similar to that found in nonparasitized fifth instar larvae. The stimulation of storage proteins in envenomed larvae demonstrates the ability (competence) of early larval stages to produce a gene product that normally occurs in the last larval stadium of the lepidopteran larval host. The gene expression necessary for storage protein production in isolated tissues may be altered by mechanisms separate from inherent developmental processes and the intact endocrine system. © 1994 Wiley-Liss, Inc.This article is a US Government work and, as such, is in the public domain in the United States of America.
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    Reduction of testis growth of pseudaletia separata larvae after parasitization by cotesia kariyai (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 111-122 
    Details
    ISSN: 0739-4462
    Keywords: braconid parasitoid ; polydnavirus ; venom ; ecdysone receptor ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The braconid endoparasitoid, Cotesia (=Apanteles) kariyai physiologically influences its host, Pseudaletia separata, through three factors: polydnavirus, venom, and teratocytes. Inhibiting testis development of the host seems to be one factor that is important for successful development of the parasitoid. CkPV (polydnavirus of Cotesia kariyai) plus venom depressed testis development. Testes from unparasitized day 0 last instar transplanted into isolated abdomens increased in volume after stimulation with 20-hydroxyecdysone (20HE). However, day 0 testis preincubated with CkPV plus venom for 6 h and then transplanted into an isolated abdomen did not respond to 20HE. Southern blot analysis indicated CkPV-DNA hybridized to testes-DNA from parasitized hosts, suggesting the possibility that CkPV is involved in suppression of testes growth. Binding assays using PNA indicated a 2-fold increase in ecdysteroid receptor binding activity during the late stage of parasitism. The increase in receptor activity might be related to the maintenance of a low ecdysteroid titer in parasitized hosts due to a feedback response. © 1994 Wiley-Liss, Inc.
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    Evidence for an early immunosuppressive role for related campoletis sonorensis venom and ovarian proteins in heliothis virescens (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 26 (1994), S. 147-163 
    Details
    ISSN: 0739-4462
    Keywords: parasitoid ; Heliothis virescens ; insect immunity ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Shared epitopes among venom, ovarian, and viral proteins may indicate that related proteins have similar functional roles during parasitization of Heliothis virescens by Campoletis sonorensis. Venom and ovarian proteins are introduced directly into the hemolymph during parasitization where they may target hemocytes or other components of the immune system. Polydnavirus expression has been detected in hemocytes, fat body, and other tissues but has not been detected earlier than 4 h after parasitization. Therefore, effects on hemocytes at times earlier than 4 h may not be caused by polydnavirus proteins synthesized in the parasitized insect. Visualization of hemocyte F-actin with fluorescently labeled phallicidin indicated that a dramatic alteration of plasmatocyte and granulocyte cytoskeletons occurred within 1.5 h after parasitization. The predominant non-viral proteins in the ovary introduced during parasitization were immunologically related to venom and viral envelope proteins. These ovarian proteins persist in the hemolymph. Antisera to the ovarian proteins bound to granulocytes and to plasmatocytes to a lesser degree, suggesting that ovarian proteins may be involved in early suppression of the host's immune response after parasitization. © 1994 Wiley-Liss, Inc.
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    Conference report on workshops held at second international symposium on molecular insect science (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 27 (1994), S. 317-324 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The symposium, organized by the Center for Insect Science and held at Flagstaff, Arizona, July 17-22, 1993, was attended by over 500 people. Mornings were devoted to invited speakers and workshops were held each afternoon. Ninety posters were also on view each day. Abstracts for the speakers' presentations and the posters were distributed to participants and to selected libraries. We present here brief reviews of the workshops as prepared by the organizers. For further information contact Henry Hagedorn, Department of Entomology, University of Arizona, Tucson, AZ 85721. © 1994 Wiley-Liss, Inc.
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    In Memoriam: Albert S. Perry (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 1-3 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940220102
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    Glutamate receptor inhibitors as potential insecticides (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 25-39 
    Details
    ISSN: 0739-4462
    Keywords: glutamate receptors ; philanthotoxins ; polyamines ; neurotoxicology ; insecticides ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Philanthotoxin (PhTX) is a neurotoxic constituent of the paralytic venom of the digger wasp, Philanthus triangulum. PhTX inhibits glutamate receptors of insect muscles mostly as a channel blocker, thereby producing muscle paralysis. Since glutamate receptor blockers may be of value as selective insect control agents, numerous derivatives of Ph TX were synthesized and tested for their potencies as inhibitors of insect skeletal muscle glutamate receptors. Structure-activity relationship studies revealed that shortening the polyamine chain length reduced potency, and quaternarization of the nitrogen destroyed it. The potency was increased by a bulky anchoring group with moderate hydrophobicity at the end of the polyamine chain. The conversion of the tryosyl moiety to 3,5-diiodo-tyrosyl also increased potency and so did lengthening the butyryl chain from 4 to 10 carbons. Not only did Ph TXs inhibit different subtypes of glutamate receptors, including the mammalian N-methyl-D-aspartate receptor, but also nicotinic receptors of insects and vertebrates. Because of this low selectively, and the hydrophilicity of the derivatives tested, which interferes with their penetration to the target receptor, these compounds cannot be used as insecticides. Nevertheless, the insect skeletal muscle glutamate receptor is a viable target for selective insecticides and major changes in Ph TX structure may possibly produce derivatives that can be potential insecticides. © 1993 Wiley-Liss, Inc.
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    Chemical studies of pheromone receptors in insects (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 75-86 
    Details
    ISSN: 0739-4462
    Keywords: photoaffinity labeling ; pheromone receptor ; G-protein ; Ins(1,4,5)P3 ; perfluoroalkyl pheromone analogs ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the current molecular model for insect olfaction, pheromones are recognized in a minimum-energy conformation by specific receptor proteins in a dendritic membrane following their binding-protein-mediated transit through the extracellula sensory lymph. Binding to the receptor protein then triggers a G-protein-linked phospholipase C, which releases a short pulse of the second messenger inositol 1,4,5-trisphate (IP3). IP3 may act via its receptor to mobilize Ca+ + ions, eventually leading to a transmembrane ion current; alternatively, IP3 may directly gate the ion channel. To understand this process, we have synthesized photoaffinity labels for the pheromone receptor sites and for the IP3 receptor sites. The latter probe, [125I]-ASA-IP3, is now being employed in joint projects to identify membrane IP3 receptors in the rat brain, locust brain, rat olfactory cilia, catfish olfactory cilia, and in cockroach and moth sensilla. Fluorine-substituted pheromone analogs have also been synthesized as probes of receptor site hydrophobicity. The rationale for this approach is presented, and biological studies with selectively-fluorinated analogs of (Z)-5-decenyl acetate (Z5-10:Ac), (Z)-7-dodecenyl acetate (Z7-12:Ac), (Z)-9-dodecenyl acetate (Z9-12:Ac), (Z)-9-tetradecenyl acetate (Z9-14:Ac), (Z)-11-hexadecenal (Z11-16:Al), and several functional group derivatives for a number of economically important moth species are described. © 1993 Wiley-Liss, Inc.
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    Peptidergic innervation and endocrine cells of insect midgut (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 113-132 
    Details
    ISSN: 0739-4462
    Keywords: neuropeptides ; gut hormones ; stomatogastric nervous system ; prothoracicotropic hormone ; allatotropin ; diuretic hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Antibody against FMRFamide reacts with the stomatogastric innervation and with the midgut endocrine cells in the representatives of most insect orders. The innervation was not revealed in Homoptera, Heteroptera, and Hymenoptera, and the endocrine cells were not recognized in aphids. Other insects exhibited FMRF-amide positive endocrine cells of both open and closed types. The cells are mostly single, rarely grouped, and are distributed unequally in different midgut regions; some of the cells project cytoplasmic extensions indicative of a paracrine function. Investigations on Galleria revealed that the gut innervation persists during midgut reconstruction in the course of metamorphosis. The endocrine cells are sloughed off into the new gut lumen, but there they maintain their antigenic properties until a new population of endocrine cells becomes detectable.Antisera to most mammalian gastroenteropancreatic peptides react specifically with the innervation and/or the endocrine cells of insect midgut; only antisera to bombesin, neurotensin, secretin, motilin, and insulin failed to react. All insects seem to contain antigens that can be detected with antisera to pancreatic polypeptide, FMRFamide, enkephalins, and vasopressins. Stomatogastric innervation and the endocrine cells of some lepidopterans also possess allatotropinand diuretic hormone-like antigens; stomatogastric ganglia, in particular, a prothoracicotropic hormone-like antigen. © 1993 Wiley-Liss, Inc.
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    Leads for insect neuropeptide mimetic development (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 181-197 
    Details
    ISSN: 0739-4462
    Keywords: pseudopeptides ; conformation ; turn ; pheromonotropic ; diuretic ; myotropic ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Insect neuropeptides mediate a number of physiological processes critical for insect survival. The numerous neuropeptide sequences that have been reported present an opportunity to decipher the chemical and conformational requirements for neuropeptide-receptor interactions. Chemical and conformational requirements for activity represent a “template” from which agonist/antagonist peptide mimetics, with the potential to disrupt critical insect processes, can be developed. Information on structural requirements is presented for three neuropeptide families: the sulfakinins, pyrokinins, and leucokinin/achetakinins, including active core size, important side chains, peptide superagonists, and new data on pseudopeptide modification of the N- and C-terminal regions. Members of these peptide families have been associated with a variety of physiological activities such as myotropism, pheromonotropism, diapause induction, and diuresis in a number of insects. Spectroscopic data coupled with computer molecular dynamics/graphics studies on conformationally restricted analogs of insect neuropeptides reveal information on the active conformation adopted at the receptor site. Routes to development of peptide-mimetics from neuropeptide templates are discussed. © 1993 Wiley-Liss, Inc.
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    Prospects of using Drosophila for insect neuroendocrine research (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 199-231 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Classical and in vitro approaches for the analysis of the molecular components of neuroendocrine systems often disrupt their close interaction with other bodily systems, which is a crucial aspect of their function in vivo. “Genetic dissection” is an alternative, noninvasive approach which involves the systematic generation of mutations in individual genes, followed by in vivo analysis of the phenotypic effects of altering a single protein at a time avoiding extraneous disruptions. Among insects Drosophila melanogaster is the most suitable model for this approach. This paper explores the application of genetic and molecular techniques available in Drosophila for studying its neuroendocrine system with special emphasis on the production of ecdysone and juvenile hormone.Strategies are described for the generation and identification of endocrine mutations, especially those affecting hormone synthesis and regulation. Once identified by a specific mutation, a gene in Drosophila can be cloned either by chromosomal microdissection and “chromosomal walk” or by transposon tagging. Methods for molecular analysis of the structure and function of a cloned gene and of the protein it encodes are available for further study.Alternatively, a gene can be cloned using heterologous DNA probes or oligonucleotides designed according to the amino acid sequence of a protein. Genes may also be cloned via their pattern of expression using stage- or tissue-specific cDNA libraries or through transposon-mediated “enhancer detection.” Anti-sense RNA, the replacement of the gene by in vitro manipulated versions, or mutagenesis of its endogenous copies can then be used for studying its function in vivo.Information about endocrine genes in Drosophila as well as material such as cloned genes and antibodies should be useful for the analysis of endocrine systems in other insects which are not amenable to genetic manipulations. Such information should be helpful in designing novel means for pest control based on the specific intervention with endocrine systems regulating insect development and reproduction. © 1993 Wiley-Liss, Inc.
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    URL: http://dx.doi.org/10.1002/arch.940220116
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    Insect detoxifying enzymes: Their importance in pesticide synergism and resistance (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 263-276 
    Details
    ISSN: 0739-4462
    Keywords: pyrethroid detoxification ; benzoylphenyl urea detoxification ; synergism ; resistance mechanism ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Pyrethroid esterases of Trichoplusiani, Spodoptera littoralis and Bemisia tabaci hydrolyze the trans-isomers of various pyrethroids more extensively than the cis-isomers. Profenofos fed to T. ni larvae at a level inhibiting the gut pyrethroid esterases by 65% with trans-permethrin and of 95% with cis-cypermethrin increased the toxicity of topically applied trans-permethrin by fourfold and cis-cypermethrin by 20-fold. Similar assays with S. littoralis resulted in an increase of about threefold in the toxicity of both compounds. Monocrotophos, profenofos, acephate, and methidathion inhibited pyrethroid esterase activity in B. tabaci and synergized considerably the toxicity of cypermethrin. The remarkable tolerance of the predator Chrysopa carnea to pyrethroids is attributed to the presence of a high level of pyrethroid esterase activity with a unique specificity for hydrolyzing the cis-isomer. Phenyl saligenin cyclic phosphonate, a potent inhibitor for larval pyrethroid esterases synergized the toxicity of trans-permethrin by 68-fold from an LD50 of 17,000 μg/g to 250 μg/g. In contrast, oxidase inhibitors such as piperonyl butoxide, SV-1, and MPP synergized considerably the toxicity of pyrethroids in Tribolium castaneum and Musca domestica. Hence the predominant pathway for pyrethroid detoxification in insects, whether hydrolytic or oxidative, depends largely on the insect species. The high toxicity of the recent developed acylureas results from their high retention in the insects. Assays using radiolabeled diflubenzuron and chlorfluazuron applied to fourth instar T. castaneum larvae revealed a rapid elimination of diflubenzuron (T1/2 ≅ 7 h) as compared with chlorfluazuron (T1/2 〉 100 h). Addition of 100 ppm DEF to the diet increased both the retention time and the toxicity of diflubenzuron in both T. castaneum and S. littoralis, which was due probably to the inhibition of diflubenzuron hydrolase activity. Esterases, hydrolyzing pyrethroids, and acylureas may serve as tools for evaluating potential synergists and for monitoring resistance in various agricultural pests due to increased metabolism. © 1993 Wiley-Liss, Inc.
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    Masthead (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993) 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940220301
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    Photostabilization of pesticides by clays and chromophores (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 467-486 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Mechanisms for the photostabilization of pesticides by the use of clays and chromophores are described. The main mechanisms include energy transfer and steric hindrance, whereas the importance of mechanisms such as light scattering and hypsochromic shift is marginal. As an example for energy transfer we describe a procedure where the potent and safe but photolabile insecticide bioresmethrin (BR) is coadsorbed on montmorillonite together with the organic cation methyl green (MG). It is shown that the effective photostabilization of BR occurs by the process of energy transfer, which depends on the matching of energy levels of donor (BR) and acceptor (MG) chromophores, on the distance between them and on their relative orientations. The methods for studying the intermolecular interaction between two coadsorbed organic molecules include Fourier-transform infrared (FTIR) and 13C solid state magic angle spinning nuclear magnetic resonance (MAS-NMR) spectroscopies. Energy transfer processes can also occur from the pesticide to the clay. The presence of transition metal ions in the clay can make it an efficient energy or charge acceptor. Such a mechanism was utilized in the photostabilization of the insecticide tetrahydro-2-(nitromethylene)-2H-1, 3-thiazine (NMH). In the latter case, improved photostabilization was achieved by an addition of the cationic dye acriflavine (AF). Steric hindrance: here the clay introduces a stereochemical factor in preventing or slowing down certain photochemical reactions. An example is the photostabilization of the dinitroaniline herbicide trifluralin (TF). The energy transfer approach was also shown to be effective in the photostabilization of microbial insecticides, such as the Bacillus thuringiensis (B.t.) toxin. Photoprotection was achieved by adsorption of cationic chromophores such as AF, MG and rhodamin B to B.t. © 1993 Wiley-Liss, Inc.
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    Cholinesterase profiles in two species of wild birds exposed to insecticide sprays in their natural habitat (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 501-509 
    Details
    ISSN: 0739-4462
    Keywords: brain acetylcholinesterase ; bimolecular rate constant ; plasma butyrylcholinesterase ; parathion ; paraoxon ; malaoxon ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During summer season, a field survey was conducted to assess the extent of stress to which two species of wild birds might have been subjected, due to their dwelling near cotton fields sprayed with insecticides. One of the bird species, the cattle egret Bubulcus ibis, showed no significant changes either in brain acetylcholinesterase (AChE) or in plasma butyrylcholinesterase (BuChE) activities in samples collected before, during, and after the spraying season. With the spur-wing plover, Hoplopterus spinosus, there was a significant decrease both in brain AChE and plasma BuChE activities in July and August, the period when insecticide spray was most frequent. In laboratory experiments it was found that this species could survive higher doses of parathion, and specimens surviving the treatment showed higher residual plasma BuChE activity and a faster return of that activity to normal compared to Bubulcus specimens. Brain AChE from the Hoplopterus showed a lower Ki value for inhibition by paraoxon or malaoxon compared to the same values recorded for the Bubulcus, indicating that the enzyme from the Hoplopterus brain is less sensitive to inhibition by paraoxon or malaoxon. The finding that the more resistant Hoplopterus showed a decrease in cholinesterase activity during the cotton spraying season may therefore be due to the territorial habits of this species. © 1993 Wiley-Liss, Inc.
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    Overview: New targets for insect management in crop protection (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 5-12 
    Details
    ISSN: 0739-4462
    Keywords: Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940220103
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    Biochemical characterization of insect neuronal sodium channels (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 41-53 
    Details
    ISSN: 0739-4462
    Keywords: saxitoxin receptor ; solubilization ; phosphorylation ; site-directed antibody ; Locusta ; Orthoptera ; Dyctioptera ; Diptera ; Lepidoptera ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The pharmacological uniqueness of the insect sodium channels is indicated by their ability to bind the excitatory and depressant insect selective neurotoxins derived from scorpion venom. The latter were shown to bind and modify sodium conductance exclusively in insect neuronal membranes. The insect sodium channel polypeptides were identified by immunoprecipitation using site-directed antibody, anti SP19 (corresponding to a highly conserved segment in the sodium channel α subunits), followed by radiophosphorylation and SDS-PAGE autoradiography. Sodium channel polypeptide in the central nervous system (CNS) of insects belonging to four distinct orders (Orthoptera, Dyctioptera, Diptera, and Lepidoptera) were shown to (1) serve as substrates for phosphorylation by cAMP-dependent protein kinase; (2) be devoid of disulfide linkage to smaller subunits unlike sodium channels in vertebrate CNS; (3) be glycoproteins as demonstrated by endoglycosidase F treatment and binding to lectins; and (4) reveal a diversity with regard to their apparent molecular mass (Mr 240,000-280,000) and partial peptide maps. The locust sodium channels were functionally solubilized (monitored by [3H]saxitoxin (STX) binding) by 1% cholate, 0.2% Triton X-100, and 0.22% phosphatidylcholine. About 40% of STX binding activity was recovered in the solubilized fraction without affecting affinity (Kd = 0.5 nM). The time and temperature dependent lability of STX binding activity, in the solubilized fraction, was prevented by 20 nM STX. Partial purification of the insect sodium channel by an anion exchanger yielded 20% recovery and a 3.5 times increase in specific STX binding activity. The presence of a radiophosphorylated 245,000 α-subunit band coincided with the STX binding activity during purification. In sum, the above information concerning the solubilization and characterization of the insect sodium channel will pave the way to the molecular identification of the receptor sites of the insect selective neurotoxins. © 1993 Wiley-Liss, Inc.
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    Insect neuropeptides: Discovery and application in insect management (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 87-111 
    Details
    ISSN: 0739-4462
    Keywords: peptide hormones ; bioassay ; genes ; insecticides ; metabolism ; structure ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: New approaches to the development of insect control agents have been revealed through the molecular description of neuropeptides, their biogenesis, action, and degradation. Prerequisite to the exploitation of a neuropeptide as a lead to control agent development is a thorough understanding of the biochemistry of the neuropeptide and appreciation of its physiological impact. Reliable bioassays must be coupled with advanced biochemical and molecular genetic technologies to overcome limitations imposed by the typically low endogenous levels of individual neuropeptides. Purification, amino acid sequencing, and gene cloning provide the molecular tools necessary for studies on neuropeptide synthesis, processing, secretion, receptor binding, and inactivation. Each of these areas consists of a number of amino acid sequence-, and enzyme-dependent steps which may be considered as targets for the development of highly specific control agents. These agents will include antagonists and superagonists, peptidomimetics, recombinant peptides delivered through the baculovirus technology, receptor blockers, and enzyme inhibitors. © 1993 Wiley-Liss, Inc.
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    Pheromone biosynthesis activating neuropeptide: From discovery to current status (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 22 (1993), S. 141-151 
    Details
    ISSN: 0739-4462
    Keywords: pheromone biosynthesis ; neuropeptide ; moths ; Helicoverpa zea ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Sex pheromone production in females of many species of moths is controlled by a pheromone biosynthesis activating neuropeptide (PBAN). PBAN from Helicoverpa zea (Hez-PBAN) is a 33 amino acid peptide produced in the suboesophageal ganglion of both female and male moths. PBAN-like activity is widespread among Lepidoptera and is also reported from a cockroach and a grasshopper. The C-terminal pentapeptide of Hez-PBAN represents the minimum sequence with pheromonotropic activity. Another pentapeptide fragment of the molecule also has high pheromonotropic activity. Presence of PBAN-like immunoreactivity and biological activity in the corpora cardiaca suggests that it is the possible site of PBAN release. There is evidence that PBAN action on pheromone gland is mediated by a second messenger. Several possible sites of action of PBAN have been suggested in the biosynthetic pathway of pheromones. The gene for Hez-PBAN has been cloned and sequenced. Cloning of a synthetic PBAN gene into a baculovirus has been attempted. Studies to isolate and identify the receptors for PBAN as well as the metabolic fate of PBAN have been initiated. © 1993 Wiley-Liss, Inc.
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    Expression of a parasitism-specific protein in lepidopteran hosts of Chelonus sp. (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 24 (1993), S. 149-169 
    Details
    ISSN: 0739-4462
    Keywords: Trichoplusia ni ; endoparasite ; secretory factor ; regulatory factor ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The hemolymph of each noctuid species successfully parasitized by Chelonus near curvimaculatus possessed a parasitism-specific protein (PSP) previously identified in host T. ni (Insect Biochem. 19:445; 21:845). Expression of PSP occurred in a stage-specific manner in the stadium during which the host undergoes precocious metamorphosis. The appearance of the protein was not due to nutritional stress associated with parasitism of hosts, since starved nonparasitized larvae did not produce the protein, or to low juvenile hormone titers occurring in precociously metamorphosing hosts, but rather was dependent on the presence of the endoparasite larva. Results of in vivo incorporation experiments with [35S]-methionine showed that synthesis and subsequent appearance of the protein in the hemolymph of parasitized hosts was abrogated by prior surgical removal of endoparasite. Immunoprecipitation analysis of proteins from C. near curvimaculatus larvae cultured in vitro using antibodies specific to PSP indicated that the source of the protein was the endoparasite. Synthesis of PSP by the endoparasitic larvae with its subsequent secretion into the hemocoel of hosts was specific to the advanced stages of parasite development prior to its egression from the host. © 1993 Wiley-Liss, Inc.
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