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  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry  (71)
  • Wiley-Blackwell  (71)
  • Copernicus
  • 1985-1989  (71)
  • 1986  (71)
  • 1
    Electronic Resource
    Electronic Resource
    Superoxide dismutase in the housefly, Musca domestica (L.) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 31-43 
    Details
    ISSN: 0739-4462
    Keywords: superoxide dismutase ; housefly ; Musca domestica ; enzyme purification and characterization ; rose bengal ; singlet oxygen ; enzyme deactivation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Four superoxide dismutase (SOD) (E.C. 1.15.1.1) isozymes were present in whole tissue homogenates of Musca domestica when examined by polyacrylamide gel electrophoresis. One of the isozymes contained manganese, and the other three contained copper and zinc. All were observed in each of the body tagma (head, abdomen, and thorax) and at each developmental stage (egg to adult).The copper- and zinc-containing isozymes purified from newly emerged, adult M. domestica had a relative molecular weight of 34,800 as determined by gel filtration chromatography but consisted of two equal-size subunits of 16,000 as measured by sodium dodecylsulfate polyacrylamide gel electrophoresis. An isoelectric point between 4.8 and 5.1 was measured. Approximately 2 mol each of copper and zinc were present per dimer. The three copper, zinc isozymes were identified as charge variants. The amino acid composition of the enzyme was similar to that of copper, zinc-containing superoxide dismutases from other sources.Purified housefly copper, zinc superoxide dismutase was neither deactivated nor able to protect lactic dehydrogenase against deactivation in the presence of light and rose bengal, a known generator of singlet oxygen. The role of SOD in the phototoxic reaction involving rose bengal is discussed.
    Additional Material: 2 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030105
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  • 2
    Electronic Resource
    Electronic Resource
    Biosynthesis and distribution of ecdysone and 20-OH-ecdysone in Aedes aegypti (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 19-30 
    Details
    ISSN: 0739-4462
    Keywords: Aedes aegypti ; methoprene ; ecdysone ; 20-OH-ecdysone ; egg development neurosecretory hormone ; HPLC ; TLC ; vitellogenesis ; RIA ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The distribution and biosynthesis of ecdysone and 20-hydroxyecdysone (20-OH-ecdysone) was followed in sugar- and blood-fed female Aedes aegypti. In both sugar- and early blood-fed animals most of the ecdysteroid determined by radioimmunoassay was found outside the ovary. Twenty-four to 40 h after blood feeding, however, ecdysteroid was distributed between ovary and carcass in the ratio of 1:1.5. Ecdysteroid titer reached a plateau between 18 to 40 h after the blood meal and decreased thereafter. Analysis of the ecdysteroid titer using thin layer chromatography (TLC) and high performance liquid chromatography (HPLC) revealed that both 20-OH-ecdysone and ecdysone were synthesized after the blood meal. The ratio of 20-OH-ecdysone to ecdysone remained essentially constant and fluctuated in parallel throughout egg development. Chromatography of the early ecdysteroid peak (8 h after feeding) using TLC and HPLC indicated that although it cross-reacted with ecdysteroid antibodies, it did not have the same elution times as ecdysone and 20-OH-ecdysone and is, therefore, probably a precursor of these ecdysteroids. Injections of egg development neurosecretory hormone (EDNH) preparation purified to near homogeneity, into ligated abdomens, induced ecdysteroid synthesis only if the abdomens were first treated with methoprene (12.5 pg). Methoprene at this concentration did not stimulate ecdysteroid synthesis in these abdomens. When blood-fed females were treated with [4-14C] cholesterol and analyzed using TLC and HPLC procedures, both [14C]labeled ecdysone and [14C]labeled 20-OH-ecdysone were synthesized in the ratio of 1:1.5. This report is the first to show that both ecdysone and 20-OH-ecdysone are synthesized in vivo in female A. aegypti.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030104
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  • 3
    Electronic Resource
    Electronic Resource
    Inhibition of hydrocarbon biosynthesis in the housefly by 2-Octadecynoate (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 75-86 
    Details
    ISSN: 0739-4462
    Keywords: hydrocarbon biosynthesis ; 2-octadecynoate ; housefly ; fatty acid synthetase ; fatty acid elongation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The elongation of [9,10-3H]oleoyl-CoA with malonyl-CoA to form 20, 22, and 24 carbon monounsaturated fatty acids was demonstrated in housefly microsomes by radio-GLC. These elongation reactions, which have been postulated to be involved in hydrocarbon biosynthesis, have not been previously demonstrated in insects. 2-Octadecynoate (18:1 Δ2=) inhibited the in vivo incorporation of [1-14C]acetate into both fatty acids and hydrocarbons in a dose-dependent manner. At doses of 10 μg per female housefly of the alkynoic acid, the incorporation of [1-14C]acetate into hydrocarbon was inhibited 93%, the incorporation of [9,10-3H]oleate into hydrocarbon was inhibited 64%, and the incorporation of [1-14C]acetate into total internal lipid was inhibited 65%. Partially purified FAS was inhibited 50% and 95% at 15 μM and 40 μM, respectively, of the alkynoic acid. These results show that 2-octadecynoate inhibits hydrocarbon biosynthesis in the housefly by inhibiting FAS, and the in vivo data suggest that the elongation of 18:1 to longer chain fatty acids is also inhibited.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030109
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  • 4
    Electronic Resource
    Electronic Resource
    In vitro ecdysteroid conjugation by enzymes of Manduca sexta midgut cytosol (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 109-126 
    Details
    ISSN: 0739-4462
    Keywords: Ecdysteroid phosphoester ; Manduca sexta ; midgut ; C18 SEP-PAK ; β-glucuronidase ; sulphatase ; acid phosphatase ; ATP:ecdysteroid phosphotransferase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In incubations with 80,000g supernatant of Manduca sexta midgut homogenates, [3H]ecdysone was converted to 3-[3H]epiecdysone and tritiumlabeled highly polar metabolites. C18 SEP-PAK cartridges were found suitable for the separation and purification of the free ecdysteroids and of the highly polar metabolites. Eighty to ninety percent of the metabolites were hydrolyzed by enzyme mixtures (mainly β-glucuronidase, sulphatase, and acid phosphatase) from molluscs, even when β-glucuronidase activity was completely inhibited by D-saccharic acid 1,4-lactone, or various human acid phosphatases (free of sulphatase activity). In each experiment, the hydrolysate contained a much higher proportion of 3-epiecydsone than the free (unconjugated) ecdysteroid fraction. [3H]ecdysone was not metabolized in anaerobic incubations of midgut supernatant that had been filtered through Sephadex G-25. Addition of 5 mM ATP and 5 mM Mg2+ restored the conjugate formation in incubations of Sephadex-filtered supernatant. Four ecdysone conjugates and two 3-epiecdysone conjugates were resolved by reversedphase ion-pair high-performance liquid chromatography. It is concluded that the midgut cytosol contains several ATP:ecdysteriod phosphotransferases. This is the first demonstration of the formation of ecdysteroid phosphoconjugates in a cell-free system.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030202
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  • 5
    Electronic Resource
    Electronic Resource
    The effect of L-canavanine and L-canaline on the hemolymph amino acid composition of the tobacco hornworm, Manduca sexta (L.) (Sphingidae) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 265-275 
    Details
    ISSN: 0739-4462
    Keywords: L-canavanine ; L-canaline ; Manduca sexta ; plant-insect interactions ; hemolymph amino acids ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Tobacco hornworm larvae, Manduca sexta (L.) (Sphingidae), were administered L-canaline either by parenteral injection or by dietary consumption. The overt toxicity and the alteration of hemolymph amino acids caused by these nonprotein amino acids were evaluated. The LD50 value for parenterally administered canavanine and canaline is 1.0 and 2.5 mg/g fresh body weight, respectively. A dietary concentration of 5.2 mM for canavanine and over 20 mM for canaline represent the respective LC50 values. A large percentage of the larvae reared on diets supplemented with additional arginine, ornithine, or 2,4-diaminobutyric acid in addition to canavanine or canaline were unable to complete larval-pupal ecdysis. These toxic effects were associated with a decreased glutamic acid hemolymph titer and dramatically elevated ornithine. On the other hand, larvae administered canavanine or canaline alone, either by dietary consumption or parenteral injection, experienced less drastic developmental aberrations. These symptoms were in some cases correlated with increased ornithine and glutamic acid titers. Evidence is presented that even a canavanine- and canaline-sensitive insect such as M. sexta has a marked ability to eliminate these protective allelochemicals.
    Additional Material: 2 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030305
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  • 6
    Electronic Resource
    Electronic Resource
    Masthead (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986) 
    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.940030401
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  • 7
    Electronic Resource
    Electronic Resource
    Isolation and in vitro synthesis of trypsin from the biting fly, Stomoxys calcitrans (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 307-318 
    Details
    ISSN: 0739-4462
    Keywords: trypsin ; protease ; midgut ; fat body ; Stomoxys calcitrans antibodies ; blood digestion ; TAME ; TLCK ; hide-powder azure ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The synthesis of [3H]trypsinlike enzyme by the fat body was followed in Stomoxys calcitransin vitro using a radioimmunoassay (RIA) developed against mammalian trypsin. Using high specific activity [3H]valine, trypsinlike activity was followed in midgut epithelial cells, thoracic muscle, and fat body removed from sugar-fed flies. Excreta protease of S. calcitrans was partially purified using charge and hydroxylapatite gel chromatography. Seventy-five percent of the enzyme eluted from these gels was inhibited by tosyl-L-lysine chloromethyl ketone HCI (TLCK) and was classified as trypsinlike. Electrophoresis of the trypsinlike enzyme indicated that it was only 50% pure. Trypsinlike activity from S. calcitrans bound to α1-globulin IV-I and formed a complex that was dissociated on a P-100 Bio-Gel column. Binding between the protease and the α1-gobulin IV-I caused a 1.4-fold increase in the apparent molecular weight of the protease on the P-100 Bio-Gel column. Trypsinlike activity was characterized in the midgut and excreta by affinity binding to covalently linked TLCK and tosyl-L-lysine chloromethyl ketone HCI (TAME)Sepharose 4B gels. Between 50% and 55% of the excreta protease and 5669% of the midgut protease bound to the affinity gels and was trypsinlike. Protease activity that did not bind to the gels was not inhibited by TLCK and did not have the esterolytic activity of trypsin.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030308
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  • 8
    Electronic Resource
    Electronic Resource
    Utilization of Δ5,7 - and Δ8-sterols by larvae of Heliothis zea (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 349-362 
    Details
    ISSN: 0739-4462
    Keywords: Heliothis zea ; cholesterol ; 7-dehydrocholesterol ; 24-dihydrolanosterol ; 4,4-dimethylcholesterol ; ergosterol ; lanosterol ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Larvae from two populations of Heliothis zea were reared on artificial diets containing various sterols, which supported suboptimal growth, and their tissue sterols were characterized in order to determine how these dietary sterols are utilized by this insect. The sterols studied included Δ5,7-sterols (7-dehydrocholesterol or ergosterol), Δ8-sterols (lanosterol and/or 24-dihydrolanosterol), and a Δ5-sterol (4,4-dimethylcholesterol). Although larvae did not develop on 4,4-dimethylcholesterol, those fed primarily Δ8-4,4,14-trimethylsterols developed to the third instar. When the latter sterols were spared with cholesterol, the larvae reached the sixth instar and contained 4,4,14-trimethylsterols as well as cholesterol in their tissues. When larvae were fed 7-dehydrocholesterol, 〈1% of the larvae from one population developed to the sixth instar and these larvae contained 7-dehydrocholesterol as their principal sterol. The other larvae successfully completed their larval stage when they were transferred from the diet containing 7-dehydrocholesterol (or no sterol) to a diet containing cholesterol within at least 9 days. The sterol composition of larvae transferred from a diet containing cholesterol to a diet containing 7-dehydrocholesterol, after they had reached 60% of their final weight, was 54% cholesterol and 46% 7-dehydrocholesterol. The major sterol isolated from the tissues of the larvae fed ergosterol was also 7-dehydrocholesterol. Therefore, although the larva of H. zea can dealkylate and saturate the side chain of the Δ5,7,22-24β-methylsterol, it carries out little metabolism of the B ring of the nucleus. These studies demonstrate that, when Δ5,7- or Δ8-sterols are the principal sterols in the diet of H. zea, they are absorbed and incorporated into its tissues, although they slow the rate of growth and may prevent complete development of the larva.
    Additional Material: 5 Tab.
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    URL: http://dx.doi.org/10.1002/arch.940030404
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  • 9
    Electronic Resource
    Electronic Resource
    Biosynthesis of makisterone A and 20-hydroxyecdysone from labeled sterols by the honey bee, Apis mellifera (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 415-421 
    Details
    ISSN: 0739-4462
    Keywords: campesterol ; cholesterol ; sitosterol ; 24-methylenecholesterol ; ecdysteroids ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In an effort to determine the sterol precursor(s) of the 28-carbon ecdysteroid, makisterone A, honey bee pupae (13 days post-oviposition) were injected with radiolabeled sterols and subsequently examined for labeled ecdysteroids. High performance liquid chromatography of the pupal extracts revealed that [3H]campesterol was converted to a compound that behaved chromatographically identical to authentic makisterone A, and [14C]cholesterol was incorporated into a compound chromatographically like 20-hydroxyecdysone. No incorporation of either 24-[3H]methylenecholesterol or [14C]sitosterol into an ecdysteroid was observed. The neutral sterols of uninjected honey bee pupae contained 49.8% 24-methylenecholesterol on a relative percent basis and, with three other C28 and C29 sterols, accounted for over 99% of the total sterols present.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030502
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  • 10
    Electronic Resource
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    Larval development, developmental arrest, and hormone levels in the couple Galleria mellonella (lepidoptera-pyralidae) - Pseudoperichaeta nigrolineata (diptera-tachinidae) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 457-469 
    Details
    ISSN: 0739-4462
    Keywords: Tachinidae ; host-parasitoid interactions ; developmental arrest ; juvenile hormones ; ecdysteroids ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During their growth on the substitution host Galleria mellonella, about onethird of Pseudoperichaeta nigrolineata larvae undergo a developmental arrest in the middle of the second stage. To assess the extent of endocrine involvement, juvenile hormone (JH) and ecdysteroid (ECD) determinations by radioimmunoassays were made both on G. mellonella and P. nigrolineata throughout the larval development of this parasitoid. The transfer of G. mellonella larvae from the usual rearing temperature (27.5°C) to that required for infestation (21°C) significantly affects hormone titers: the JH level increases 10 to 20 times, while the ECD level becomes 10 times lower. The JH levels are lower in hosts with parasitoids in developmental arrest than in those with P. nigrolineata in continuous growth, but the high variability makes it seem unlikely that the titer of this hormone is critical in regulating development of the parasitoid. ECD levels are depressed in the hosts with parasitoids in developmental arrest and are increased when the parasitoids resume growth. Therefore, we propose that the main cause of the developmental arrest of P. nigrolineata is the low ECD levels characterizing some G. mellonella larvae for which the transfer to 21°C has induced some physiological disturbances.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030506
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  • 11
    Electronic Resource
    Electronic Resource
    Ecdysone 20-hydroxylation in imaginal wing discs of Pieris brassicae (lepidoptera): Correlations with ecdysone and 20-hydroxyecdysone titers in pupae (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 501-512 
    Details
    ISSN: 0739-4462
    Keywords: ecdysone ; 20-hydroxyecdysone ; ecdysone 20-hydroxylase ; imaginal discs ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Ecdysone 20-hydroxylase activity has been detected in pupal wing discs of Pieris brassicae. This activity is due to an enzyme system located in microsomal fractions. Its apparent Km is 58 nM for ecdysone. The enzyme is inhibited by the reaction product 20-hydroxyecdysone with an apparent Ki of 2.6 μM. Its activity varied during pupal-adult development with a maximum on day 4, when ecdysone levels are the highest in the animal. Although low, the peak activity is sufficient to assure 25% of the conversion of endogenous ecdysone into 20-hydroxyecdysone in pupae. Ecdysone and 20-hydroxyecdysone levels were measured in hemolymph and whole animals; ecdysone appears to be mainly located in hemolymph, whereas 20-hydroxyecdysone seems to be equally distributed between hemolymph and tissues. All these findings are discussed in relation to the roles of ecdysone and 20-hydroxyecdysone during pupal-adult development.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030602
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  • 12
    Electronic Resource
    Electronic Resource
    Yolk polypeptide processing in the fat body of Sarcophaga bullata (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 87-96 
    Details
    ISSN: 0739-4462
    Keywords: yolk polypeptides ; 20-hydroxyecdysone ; in vitro translation ; processing ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In Sarcophaga bullata there are at least three genes coding for the major yolk polypeptides. By means of the reticulocyte cell-free translation system in combination with dog pancreatic microsomal membranes, it was demonstrated that minor processing of the peptides occurs in Sarcophaga. Prior to secretion, only the cleavage of the signal peptide is observed.In vitro translation experiments also revealed that Sarcophaga males require only 20-hydroxyecdysone and not juvenile hormone for the induction of the yolk polypeptide transcription. Following a single injection of 20-hydroxyecdysone in males, in vivo pulse labeling experiments showed that translation of the yolk polypeptides continues for no longer than 24-36 h; only a continuous stimulation by 20-hydroxyecdysone results in prolonged synthesis of the yolk polypeptides.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030710
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  • 13
    Electronic Resource
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    Into the lair of the gene (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 143-155 
    Details
    ISSN: 0739-4462
    Keywords: Drosophila ; P elements ; regulatory sequences ; polytene chromosomes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A new picture of gene and chromosome structure is emerging in Drosophila that differs considerably from that largely derived from polytene chromosome banding patterns and saturation mutagenesis. In particular, gene transfer has enabled us to more clearly limit the functional unit of a number of genes. Gene regulation may be studied at the molecular level with such techniques. The possible complexity of regulatory elements that may pose problems in their analysis is discussed.
    Additional Material: 2 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030715
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  • 14
    Electronic Resource
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    Absence of female-specific protein in the hemolymph of stable fly Stomoxys calcitrans (L.) (Diptera: Muscidae) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 205-213 
    Details
    ISSN: 0739-4462
    Keywords: Stomoxys calcitrans ; stable fly ; vitellogenin ; ovary ; fat body ; hemolymph ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Changes, during the reproductive cycle, in fat body, hemolymph, and ovarian proteins of the stable fly Stomoxys calcitrans were characterized quantitatively and qualitatively using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Protein content of all three tissues increased after blood feeding. Fat body protein increased first, followed by hemolymph and ovarian proteins. SDS-PAGE failed to identify vitellogenin in both female hemolymph and fat body samples. No single protein or group of proteins predominated at any stage of the reproductive cycle. Comparisons between male and female stable fly hemolymph and fat body proteins failed to detect female-specific proteins. Female-specific proteins, however, were detected in the hemolymph of four other species of Diptera.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030210
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  • 15
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    Possible inactivation of ingested ecdysteroids by conjugation with long-chain fatty acids in the female tick Ornithodoros moubata (acarina:argasidae) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 235-252 
    Details
    ISSN: 0739-4462
    Keywords: ticks ; Ornithodoros moubata ; metabolism of ingested ecdysteroids ; detoxification ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Ornithodoros moubata females proved to be extremely sensitive to ingested 22,25-dideoxyecdysone; 15-20 ng provoked molting in all females and temporarily inhibited vitellogenesis. In contrast, this tick was very resistant to ingested ecdysteroids containing 22-OH groups, such as ecdysone, 20-hydroxyecdysone, ponasterone A, and makisterone A. Dosages about 500 times greater were necessary to produce supermolting and reduce fecundity [Connat et al: Z Ang Ent 96, 520 (1983)]. Ingested tritiated ecdysone, 20-hydroxyecdysone, 2-deoxyecdysone, and ponasterone A were rapidly converted to apolar esterase-labile metabolites having approximately the same retention time as the AP2 identified as esters of ecdysteroids at C-22 with long-chain fatty acids (C16:0, C18:0, C18:1, C18:2) [Diehl et al: Int J Invert Reprod Dev 8, 1 (1985)]. These products were then gradually transformed to the more polar apolar conjugates, AP1. A more detailed study with ingestion of large quantities of 20-hydroxyecdysone (10 μ/ml blood) demonstrated that only small amounts of free hormone were present in the hemolymph during the first day after the blood meal. The hormone was rapidly metabolized to AP2, then to AP1, in the intestinal cells and to a lesser extent in the peripheral tissues. Finally, AP1 accumulated in the intestinal cells and midgut content, probably because excretion outside the animal is impossible in this tick species.In contrast, ingested 22,25-dideoxyecdysone was not metabolized to apolar products. This could account for its high biological activity. This compound was converted to unidentified more polar products. Two of them comigrated with ecdysone and 20-hydroxyecdysone on RP-18 HPLC column, but not on silica column, and therefore cannot correspond to these compounds.We hypothesize that esterification of ecdysteroids at the C-22 position with fatty acids represents a detoxification mechanism for ingested ecdysteroids that might be present in blood from herbivorous or parasite-infected hosts.
    Additional Material: 9 Ill.
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    URL: http://dx.doi.org/10.1002/arch.940030303
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  • 16
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    Clones of Aedes albopictus cells resistant to methylmercaptopurine riboside (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 293-306 
    Details
    ISSN: 0739-4462
    Keywords: Aedes albopictus cells ; methylmercaptopurine riboside resistance ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Four clones of A. albopictus cells resistant to 6-methylmercaptopurine riboside (MMPR) (MMPR-10, -11, -12, and -21) were isolated after mutagenesis of the parental LT C-7 cells. As assayed by plating efficiencies these clones were from ten- to 20-fold more resistant to MMPR than the LT C-7 cells. Resistance was also demonstrated by the fact that concentrations of MMPR, which reduced the levels of ATP and GTP in LT C-7 cells, had no such effect in the MMPR-resistant cells. When de novo purine biosynthesis was measured by the incorporation of [14C]formate into ATP and GTP, MMPR had little effect on the MMPR-10 cells (15% inhibition) but did depress synthesis considerably in the MMPR-11 cells (80% inhibition) although not as severely as in the LT C-7 cells (95% inhibition). Three of the resistant clones which were tested also showed considerable resistance to guanosine. Although the mechanism of resistance to MMPR in these cells is not clear it likely involves some alteration in one of the early enzymes involved in purine biosynthesis. Resistant as well as sensitive cells showed a new high-performance liquid chromatography peak after treatment with MMPR suggesting that there was no defect in the uptake of MMPR. The conversion of labeled adenosine to AMP, ADP, and ATP in the resistant cells indicated that these cells were not deficient in adenosine kinase, another possible mechanism of resistance to MMPR. All clones showed a reduction in GTP following treatment with ribavirin; however, they varied considerably with respect to the amount of ribavirin triphosphate which they formed. In the case of the MMPR-11 cells the amount of ribavirin triphosphate formed was markedly sensitive to cultural conditions. The fact that the various MMPR-resistant cells responded differently to ribavirin, and that quantitative differences were also seen in their responses to MMPR (as measured by [14C]formate incorporation) and to guanosine, suggests that there are significant phenotypic differences among these resistant clones.
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    [N-Methyl-3H]Scopolamine binding sites in the central nervous system of the cockroach Periplaneta americana (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 339-347 
    Details
    ISSN: 0739-4462
    Keywords: Muscarinic acetylcholine receptors ; cockroach CNS ; [N-methyl-3H]scopolamine ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The binding of [N-methyl-3H]scopolamine to a cockroach nerve cord preparation has been investigated. Specific [N-methyl-3H]scopolamine binding was found to be saturable and of high affinity (Kd = 13.9 nM). Muscarinic ligands were found to displace [N-methyl-3H]scopolamine binding more effectively than nicotinic ligands. The distribution of these [N-methyl-3H]scopolamine binding sites was examined in the metathoracic ganglion at the light microscope level by autoradiographical techniques. Specific binding was found to be localized to distinct regions of the neuropile. This pattern showed certain similarities to that seen when the ganglion was stained for acetylcholinesterase, suggesting a functional role for these insect muscarinic acetylcholine receptors.
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    Presence and regulation of trehalose in the body of adult Phormia regina (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 381-395 
    Details
    ISSN: 0739-4462
    Keywords: blood sugar ; fat body ; hemolymph ; hypotrehalosemic hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Trehalose, the major blood sugar of Phormia regina, is present within its tissues in an amount exceeding that in the total blood volume. A major part of the reserve is found in the abdominal fat body. An investigation of trehalose regulation, pursued with the use of a trehalose tolerance test, indicates that within a period of 4 h the adult fly can remove from its blood amounts of this sugar in excess of twice its normal level. The surplus is dealt with in an as yet unknown way, being either sequestered in the tissues (not as trehalose or glucose), metabolized, or excreted in a form other than trehalose or glucose. The process is regulated by the head, and a link between the body and the head must be maintained throughout the entire period of activity.
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    The neutral sterols of Megalotomus quinquespinosus (say) (hemiptera: Alydidae) and identification of makisterone a as the major free ecdysteroid (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 423-430 
    Details
    ISSN: 0739-4462
    Keywords: molting hormones ; dietary sterols ; HPLC/RIA ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Last-stage nymphs of the broad-headed bug, Megalotomus quinquespinosus contain the C28 ecdysteroid makisterone A as their major ecdysteroid. No ecdysone or 20-hydroxyecdysone was detected in whole body extracts analyzed by high performance liquid chromatography and radioimmune assay. Analyses of the neutral sterols of this phytophagous hemipteran revealed that the sterol composition of the nymphs was highly reflective of their dietary sterols. The most abundant nymphal sterols were sitosterol (46.6%), Δ7-stigmastenol (13.8%) and spinasterol (13.4%). Cholesterol accounted for only 0.2% of the total sterols and indicates that this species is incapable of converting 24-alkyl sterols to cholesterol.
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    Erratum (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 499-499 
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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
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940030509
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    Effects of the tumor promoter 12-0-tetradecanoyl-phorbol-13-acetate on the wasp, Bracon hebetor (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 529-538 
    Details
    ISSN: 0739-4462
    Keywords: anti-vitellogenic benzo(a)pyrene ; braconid ; habrobracon ; TPA ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A single oral dose of the tumor promoter, 12-0-tetradecanoyl-phorbol-13-acetate (TPA), caused a rapid necrosis of the ovarioles, aberrations in the developmental sequence of oocytes, and a concomitant dose-dependent decline in egg production in the wasp, Bracon hebetor. TPA and its metabolities were found to have a biological half life of 26.7 h, with a peak concentration in the ovarioles in 3 h. Damage to ovariole tissue was persistent despite the relatively short half life. Other tissues in the wasp were largely unaffected, although TPA induced lethargy that persisted until death. There was no shortening of life span. Inhibition of intercellular transport and metabolic cooperation may account for decreased fecundity and fertility, but interaction with a phorbol ester receptor is more likely to account for developmental changes and central nervous system poisoning.
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    Neural correlates of flight activation and escape behavior in houseflies recovering from pyrethroid poisoning (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 551-559 
    Details
    ISSN: 0739-4462
    Keywords: permethrin ; deltamethrin ; giant axon ; escape behavior ; flight muscle ; Musca domestica ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Recovery from pyrethroid poisoning was studied in groups of adult female houseflies treated with LD50 doses of trans-permethrin or deltamethrin. The first overt sign of recovery was the appearance of normal posture, which was followed by jumping behavior and finally, coordinated flight when the flies had fully recovered. Prior to full recovery, treated houseflies were able to maintain normal posture and usually jump, but they could not fly. When tethered, these flightless houseflies responded to loss of tarsal contact by initiating normal patterned activity in the dorsolongitudinal flight muscles, yet the wings did not move. In flightless flies displaying jumping behavior, electrical stimulation of the brain evoked responses in the pleurosternal muscle, which controls thoracic tension during flight. Thus, many of the motor systems responsible for flight behavior seemed to be functional in flightless flies. Carbofuran, a carbamate anticholinesterase known to initiate spontaneous flight behavior from within the central nervous system, failed to elicit this response in flightless flies. These results suggested that the flightless condition was due to a disruption in central nervous pathways, and not to peripheral neuromuscular block. The pattern of recovery of different behaviors analyzed in this study was found to be consistent with the Jacksonian Hierarchy Principle, and the utility of this principle in guiding the design of new behavior-modifying compounds is discussed.
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    Preface (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 1-2 
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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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    URL: http://dx.doi.org/10.1002/arch.940030702
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    Grasshopper as a model system for the analysis of juvenile hormone delivery to chromatin acceptor sites (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 7-23 
    Details
    ISSN: 0739-4462
    Keywords: juvenile hormone-binding proteins ; grasshopper ; fat body ; vitellogenin ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the analysis of insect juvenile hormone (JH) function, metamorphosis is complicated by ecdysone and JH acting concurrently. Although JH stimulation of vitellogenin synthesis by the fat body is by no means simple, it is possible to focus on the events leading to selective transcription of a single gene. The two-striped grasshopper Melanoplus bivittatus was used to study nuclear binding of JH during vitellogenesis and to investigate proteins binding JH that have been found in hemolymph and fat body. M. bivittatus reproduction is regulated by JH. The fat body nuclei increased in ploidy with time after eclosion, and, because the antiallatotropin precocene completely inhibited vitellogenin production, we assume that this grasshopper differs little from Locusta migratoria in which JH stimulates transcription of the vitellogenin gene. Proteins that bind JH with high affinity were identified with the hydroxyapatite assay. Characterization of the JH-binding proteins included ion exchange chromatography, gel filtration, and polyacrylamide gel electrophoresis. Four proteins of hemolymph and three proteins of fat body bound JH with high affinity, and binding was competitively inhibited by JHIII. Short-term tissue culture was used to follow [3H]JH-III uptake by fat body and to determine the intracellular distribution of the hormone. Proteins that bound JH were extracted from nuclei with KCI, and they increased in number from the time of adult emergence to the time of maximum vitellogenin secretion. The JH-binding proteins from nuclei might be receptors that help regulate the selective expression of genes for vitellogenin and for other proteins induced by JH.
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    Properties of larval and imaginal membrane-bound digestive enzymes from Trichosia pubescens (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 181-192 
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    ISSN: 0739-4462
    Keywords: aminopeptidase ; α-glucosidase ; trehalase ; larval midgut enzymes ; adult midgut enzymes ; midgut membrane-bound enzymes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Trichosia pubescens larval midgut ceca cells display in their plasma membranes α-glucosidases (Mr 95,000; pHo 5.5; Km 5.7 mM; Ki for TRIS 8.9 mM), trehalases (Mr 69,000; pHo 5.3; Km 0.92 mM; Ki for TRIS 57 mM), and aminopeptidases (Mr 95,000; pHo 8.7; Km 0.19 mM) which are solubilized by Triton X-100. The enzymes were purified by electrophoresis and used to raise antibodies in a rabbit. T. pubescens imaginal midgut cells display in their plasma membranes an α-glucosidase (Mr 156,000; pHo 5.8; Km 2.3 mM; Ki for TRIS 0.2 mM), a trehalase (Mr 93,000; pHo 5.5; Km 0.72 mM; Ki for TRIS 45.5 mM), and an aminopeptidase (Mr 210,000; pHo 9.0; Km 0.47 mM). Antiserum produced against the larval enzymes shows no precipitation arc when tested by double immunodiffusion or by immunoelectrophoresis with Triton X-100-solubilized membrane proteins from imaginal midguts. Otherwise, a similar test showed that larval midgut cecal enzymes and larval ventriculus enzymes display complete immunological identity. The data suggest that, despite the fact the larval and imaginal aminopeptidase, α-glucosidase, and trehalase probably have similar functions, the genes coding for them in larvae and imagoes must differ.
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    Masthead (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986) 
    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.940030301
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    Studies on vitellogenin from the tobacco hornworm, Manduca sexta (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 217-233 
    Details
    ISSN: 0739-4462
    Keywords: Manduca sexta vitellogenin ; apoproteins ; immunology ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the tobacco hornworm moth, Manduca sexta, vitellogenin (Vg) is a very high-density (1.29 g/ml) phosphoglycolipoprotein containing 13% lipids, 3% carbohydrates, and 0.6% protein-bound phosphorus. Vitellogenin (Mr∼500,000) has two apoproteins designated apoVg-l (Mr 177,000 ± 3,600) and apoVg-ll (Mr45,000 ± 5,000). ApoVg-l and apoVg-II can be dissociated with 6 M guanidine HCI and separated from each other by gel permeation chromatography. Immunoblotting experiments using antibodies against the apoproteins showed that apoVg-l and apoVg-II antigens were immunologically distinct polypeptides. Antibodies against Vg reacted only with apoVg-l. Antibodies against Vg and apoVg-l reacted with Vg in double immunodiffusion experiments, whereas antibodies against apoVg-II did not. These results suggest that in the native Vg molecule, apoVg-II is positioned inside the molecule away from the aqueous environment. Only apoVg-I contained covalently bound carbohydrate as shown by fluorescein isothiocyanateconjugated concanavalin A, periodate-Schiff reagent, and in vivo labeling with 3H-Man. In vivo labeling with 32P-inorganic phosphate and chemical determination showed that apoproteins of both Vg and vitellin contain covalently bound phosphate groups.
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    Announcements (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 319-320 
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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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    Announcement (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 414-414 
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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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    Masthead (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986) 
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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
    Type of Medium: Electronic Resource
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    Interactions of charatoxins and nereistoxin with the nicotinic acetylcholine receptors of insect cns and Torpedo electric organ (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 431-445 
    Details
    ISSN: 0739-4462
    Keywords: Perhydrohistrionicotoxin ; honey bee brain receptors ; α-bungarotoxin ; Periplaneta americana ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Interactions of charatoxin (4-methylthio-1,2-dithiolane; ChTX) and four openchain analogs as well as nereistoxin (NTX) with acetylcholine (ACh) receptors were studied using biochemical assays on the Torpedo electric organ and honey bee brain receptors and using electrophysiological assays on the response of the cell body of the fast coxal depressor motoneuron (Df) of the cockroach Periplaneta americana to ACh. The actions of ChTXs were complex. Except for ChTX Xl, they all potentiated the ACh-induced current in Periplaneta neurons, but at higher concentrations all ChTXs, except for ChTX XII, caused voltage-dependent block of this current. All CHTXs inhibited binding of [3H]perhydrohistrionicotoxin in the presence of ACh to the highaffinity noncompetitive blocker site on the Torpedo receptor, but all, except for ChTX XI, potentiated its binding in absence of ACh. The actions of ChTXs on the honey bee brain receptor were quite different from those on the Torpedo receptor. They inhibited, or had no effect on, [125I]α-bungarotoxin (α-BGT) binding to the Torpedo receptor, but all ChTXs, except for ChTX I, potentiated its binding to the honey bee receptor. It is suggested that the action of ChTXs on nicotinic ACh-receptors resulted from binding to lowaffinity noncompetitive blocker site. On the other hand, NTX was more potent than ChTXs on nicotinic ACh-receptors, and some similarities were noted between the actions of NTX on Torpedo and honey bee receptors NTX had a weak agonistlike effect in both cases and possibly bound to the ACh binding sites as well as the high-affinity noncompetitive blocker site. Thus the mechanisms of action of ChTXs and NTX on nicotinic ACh-receptors are different, and there are also differences in the responses to these toxins between receptors of insect central nervous system and Torpedo electric organ.
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    Masthead (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986) 
    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
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    Effect of conditioned media on three genotypes of Drosophila melanogaster: Physical, chemical, and biological aspects (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 485-497 
    Details
    ISSN: 0739-4462
    Keywords: interactions among genotypes ; uric acid ; biotic residues ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The uric acid contents in larvae, pupae, and culture media were studied during larval and pupal development in three genotypes of Drosophila melanogaster reared in both crowded and noncrowded conditions. The uric acid content and the response of genotypes in media supplemented with 10 and 15 mg/ml of uric acid were correlated with the outcome obtained in conditioned media. In addition, the behavior of genotypes in conditioned media is explained in terms of the physicochemical properties of the conditioned media, which include uric acid content, the amount of food ingested, the degree of free water, the physical disturbance within the cultures, and the particular response of each genotype to uric acid.
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    Studies on binding and uptake of vitellogenin by follicles of the tobacco hornworm, Manduca sexta (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 513-528 
    Details
    ISSN: 0739-4462
    Keywords: Manduca sexta ; vitellogenin ; follicles ; uptake ; receptor binding ; apoprotein ; deglycosylation ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: An in vitro system for the uptake of 125l-vitellogenin (VG) or vitellin into isolated follicles of the tobacco hornworm, Manduca sexta, is described. After incubation with 125l-VG, follicles were disrupted and the internal yolk contents separated from the follicle membranes. The results showed that 125l-VG was associated principally with the membranes (92%) after incubation at 4°C. However, at 27°C, 125l-VG was mainly in the yolk (92%). Furthermore, trypsin treatment removed approximately 70% of VG bound to the follicles at 4°C. Labeled VG was shown to bind to sonicated follicle membranes with high specificity and affinity (KD ⋍ 1.3 × 10-8 M). This binding was sensitive to pH and calcium concentration. The total binding sites were estimated at 4 × 1014 sites/g of membrane protein. Competition studies showed that binding of 125l-VG to follicle membranes was blocked by excess unlabeled vitellin and deglycosylated vitellogenin but not by lipophorin (the major hemolymph lipoprotein), microvitellogenin, a female-specific protein (Mr ∼ 31,000) found in both hemolymph and eggs, and the smaller vitellogenin subunit, apovitellogenin-II (Mr ∼ 45,000). These results suggest that selective uptake of M. sexta VG from the hemolymph involves binding to specific receptors located on the follicle membranes.
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    Sterols of phytophagous and omnivorous species of Hymenoptera (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 13-18 
    Details
    ISSN: 0739-4462
    Keywords: Hymenoptera ; sterols ; phytophagous ; omnivorous ; Apidae ; Megachilidae ; Vespidae ; Formicidae ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The sterols of six species of Hymenoptera including two phytophagous species (Apis mellifera and Megachile rotundata) and four omnivorous species (Dolichovespula maculata, Vespula maculifrons, Formica exsectoides, and Solenopsis invicta) were isolated and identified. The two phytophagous species of bees have in common relatively high levels of 24-methylenecholesterol and very low levels of cholesterol (〈1% of total sterols). The isofucosterol content (40.7%) of M. rotundata was nearly three times that of A. mellifera, but overall utilization of dietary sterols in the two species is similar in that neither is able to convert C28 and C29 phytosterols to cholesterol. All four omnivorous species are predatory to some extent, and the fact that their usual dietary sterols include high levels of chlosterol is reflected in the sterols isolated from these species, which contain 45-81% cholesterol. All six hymenopteran species appear to utilize dietary sterols for structural needs with little or no metabolic modification of the steroid structure.
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    Comparison of some properties of the high-affinity juvenile hormone binding protein from the larval hemolymph of pyralid moths (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 61-73 
    Details
    ISSN: 0739-4462
    Keywords: high-affinity juvenile hormone binding protein ; hemolymph ; Pyralidae ; larval diapause ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The properties of the high-affinity low molecular weight juvenile hormone (JH) binding protein present in the hemolymph of larvae of five species of pyralid moths, a noctuid moth, and a sphingid moth were compared. The pyralid moths exhibit a facultative diapause as last-instar larvae. The species employed were the southwestern corn borer, Diatraea grandiosella, the southern cornstalk borer, Diatraea crambidoides, the sugarcane borer, Diatraea saccharalis, the European corn borer, Ostrinia nubilalis, the sunflower moth, Homoeosoma electellum, the cabbage looper, Trichoplusia ni, and the tobacco hornworm, Manduca sexta. The binding characteristics of the proteins were determined using saturation binding assays and competitive binding assays. The dissociation constants of JH I, JH II, and JH III for the binding protein of all the species varied from 0.8 x 10-7 M to 2.8 x 10-7 M. Calibrated gel filtration showed that the binding protein of all the species had apparent molecular weights ranging from 29,000 to 31,000. Electrophoresis in 7% acrylamide gels revealed that the relative mobilities of the binding proteins ranged from 0.33 to 0.43. Isoelectric focusing showed that the binding proteins had isoelectric points between 4.4 and 5.0.
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    Feedback inhibition of ecdysone production by 20-hydroxyecdysone during pupal - adult metamorphosis of Mamestra configurata wlk (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 53-60 
    Details
    ISSN: 0739-4462
    Keywords: development ; ecdysteroids ; ecdysone ; feedback inhibition ; 20-hydroxyecdysone ; metamorphosis ; pupa ; Mamestra configurata ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Large peaks of ecdysone (E, 2,875 ng/g live wt) and 20-hydroxyecdysone (20-HE, 2,150 ng/g live wt) occur on days 8 and 12, respectively, of postdiapause pupal-adult metamorphosis at 20°C in the bertha armyworm, Mamestra configurata, and then decline to low levels (〈 100 ng/g live wt) prior to eclosion of the moth (50% eclosion at day 31.8). These peaks of E and 20-HE can be suppressed by treating the developing pupae with a physiological dose (2,500 ng/g live wt) of 20-HE. Suppression of E and 20-HE by 20-HE treatment was dose dependent, rapid (within 24 h of treatment) and permanent. The peaks of E and 20-HE were suppressed by 20-HE treatment on days 1, 3, 5, and 7 but the 20-HE peak was not suppressed by treatment on days 9 or 11.It is proposed that the mechanism by which 20-HE suppresses the production of E and thereby its own production forms a negative feedback loop that operates during the first 0.4 units of pupal-adult development in M. configurata. The function of the transitory peaks of E and 20-HE that form this feedback loop is currently unknown. Since most adults from pupae that had their ecdysteroid levels experimentally suppressed by 20-HE treatment were morphologically normal, it seems that the peaks of E and 20-HE have little or no function in controlling morphological development in pupae of M. configurata.
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    Cuticular lipids for species recognition of mole crickets (Orthoptera: Gryllotalpidae): II. Scapteriscus abbreviatus, S. acletus, S. vicinus, S. sp., and Neocurtilla hexadactyla (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 127-134 
    Details
    ISSN: 0739-4462
    Keywords: Scapteriscus ; cuticular lipids ; hydrocarbons ; gas chromatography ; mole cricket ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Qualitative analyses were made from whole-body cuticular extracts of Scapteriscus abbreviatus, Scapteriscus acletus, Scapteriscus vicinus, and Neocurtilla hexadactyla by isothermal and temperature-programmed gas chromatography. Adults of both sexes and nymphs of each species were collected in Florida. The chromatographic profiles of peaks were distinct and easily recognizable for each species, regardless of sex or developmental stage. Distinct sexual differences were found in S. acletus and S. abbreviatus. Specimens of S. abbreviatus from Puerto Rico and S. vicinus from Bolivia produced gas chromatography (GC) traces very similar to those of conspecifics collected in Florida. Evidence is presented to illustrate the potential importance of volatile cuticular lipid analysis as a tool for mole cricket identification. Cuticular extracts of an undescribed short-winged species of Scapteriscus from Bolivia were also examined and produced GC traces unlike those of any other species analyzed to date.
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    Ecdysteroids in testis sheaths of Heliothis virescens larvae: An immunocytological study (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 173-180 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroid ; testis ; Heliothis ; immunocytology ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Testes of last-instar larvae of the lepidopteran, Heliothis virescens, were examined by an immunocytological technique to locate tissues associated with ecdysteroids. Antiecdysteroid antibody, prepared in rabbits, was incubated with sections of testis. Sections were then exposed to antirabbit antibody coupled to horseradish peroxidase. Oxidized 3,3-diaminobenzidine allowed visualization. Ecdysteroid was detected in tissues of the inner layer of the testis sheath and its extensions that form the follicle walls.
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    Announcements (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 215-215 
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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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    URL: http://dx.doi.org/10.1002/arch.940030211
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    Ecdysteroids in Developing ovarian follicles of Hyalophora cecropia (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 253-263 
    Details
    ISSN: 0739-4462
    Keywords: ecdysteroids ; oogenesis ; silkworm ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Developing ovarian follicles of the silkmoth Hyalophora cecropia accumulate large amounts of ecdysteroids during oogenesis. As measured by an ecdysteroid radioimmunoassay (RIA), this accumulation begins near the end of vitellogenesis, just prior to nurse cell collapse, and continues through the beginning of chorion formation. Analysis of ovarian ecdysteroids by a combination of high-performance liquid chromatography and RIA demonstrates that the major proportion of these are present in a highly polar form, most likely as conjugates; ecdysone and 20-hydroxyecdysone were present as well, in much lower proportions. Light microscopic autoradiographs of photoactivated follicles after in vivo incubation with [3H]ecdysone indicate that within the oocyte ecdysteroids are associated with the yolk sphere membranes.
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    Qualitative and quantitative changes in hemolymph proteins during an ovarian cycle and after insemination in Thermobia domestica (packard) (thysanura, lepismatidae) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 277-291 
    Details
    ISSN: 0739-4462
    Keywords: Thermobia domestica ; vitellogenins ; ovarian cycle ; insemination ; electrophoresis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Qualitative and quantitative investigations on the hemolymph proteins in the adult firebrat Thermobia domestica were performed during an ovarian cycle in inseminated and noninseminated females. Variations of hemolymph protein concentration were determined by Lowry's method. In addition, the proteins were studied by gradient slab gel electrophoresis using nondenaturing conditions and microdensitometry. Besides five major protein fractions, which are present in both sexes, three female-specific protein bands (vitellogenins) are found in the hemolymph and in maturing oocytes. These vitellogenins have molecular masses of 430, 300 and 240 kiloDalton. In fact, associated with the main 300-kD band, there were two smaller bands (320 and 280 kD) indistinguishable by densitometric measurement. Quantitative changes of vitellogenins are linked to oocyte maturation. These proteins appeared in the hemolymph before ecdysis, at the same time as the first yolk granules in the basal oocytes. They increased after ecdysis during the intense vitellogenic phase and decreased during chorion formation. In noninseminated females, in which all maturing oocytes are resorbed before chorion formation, the level of the 300 kD vitellogenins remained lower than in inseminated females. The quantity of vitellogenins fell only after complete oosorption. Thus insemination caused changes in the relative quantities of the different vitellogenic proteins.
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    Change in corpus allatum function during metamorphosis of the tobacco hornworm Manduca sexta: Regulation at the terminal step in juvenile hormone biosynthesis (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 321-338 
    Details
    ISSN: 0739-4462
    Keywords: corpora allata ; juvenile hormone ; JH acid ; JH acid methyltransferase ; HMGCoA reductase ; Manduca sexta ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Changes in activity of the corpora allata (CA) during larval-pupal-adult development of the tobacco hornworm Manduca sexta were studied by transplantation assays, measurements of in vitro juvenile hormone (JH) and JH acid synthesis, and determination of JH acid methyltransferase (JHAMT) and 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase activities. The data from these assays demonstrate that the CA cease to secrete JH by day 4 of the last larval instar (wandering stage). With regard to JH synthesis, they remain inactive throughout the prepupal, pupal, and most of the pharate adult periods. CA of females, but not of males, resume JH synthesis shortly before eclosion. The biochemical basis of the inactivation process is the loss of JHAMT activity. However, prepupal CA produce JH acids, as shown by enzyme and in vitro assays. Pupal and pharate adult CA do not synthesize JH acids although levels of HMG-CoA reductase activity seem to remain relatively high. Radiolabeled JH was recovered from hemolymph of allatectomized prepupae that had been injected with radiolabeled JH acid. These results provide further evidence that certain peripheral tissues (eg, imaginal discs) convert JH acid secreted by the prepupal CA to JH and, thus, that JH acid is a prohormone in the prepupal period. The CA change from hormone secretion to prohormone secretion during larval-prepupal transformation, a unique functional alteration in an endocrine gland.
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    Mitochondrial biogenesis during spermatogenesis in Heliothis virescens, H. subflexa, and their male-sterile backcross hybrids (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 363-380 
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    ISSN: 0739-4462
    Keywords: Heliothis ; hybrid male sterility ; mitochondria ; protein synthesis ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The mitochondrial proteins synthesized by spermatogenic cells from Heliothis virescens, H. subflexa, and their male-sterile backcross progeny were analyzed by using two-dimensional gel electrophoresis. This subset of total cellular proteins was defined by using a combination of cellular fractionation techniques and pulse-labeling in the presence of antibiotics. Mitochondrial morphology was also evaluated in cells from fertile and sterile testes by using the laser dye rhodamine 123. These studies revealed that while abnormal mitochondrial structures are apparent in sperm from backcross moths, neither protein synthesis nor import into the organelle was affected in these individuals. Two mitochondrial proteins exhibiting charge variation between the two parental hybridizing species have been identified, and these results are discussed within the context of a hypothesis developed to account for the sterility phenomenon.
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    Cuticular hydrocarbons from six species of tephritid fruit flies (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 397-412 
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    ISSN: 0739-4462
    Keywords: cuticular hydrocarbons ; alkanes ; Tephritidae ; fruit flies ; larvae ; adults ; mass spectra ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cuticular alkanes obtained from larvae and adults of six species of tephritid fruit flies, Anastrepha ludens, A. suspensa, Ceratitis capitata, C. rosa, Dacus cucurbitae, and D. dorsalis were analyzed by gas chromatography. The same four major alkanes were shown to be present by capillary GC-mass spectra in all Anastrepha and Ceratitis larvae. Profiles were obtained from individual larvae and adult specimens that showed statistical differences between species, whereas profiles of conspecific life forms including pupae of A. suspensa from different locations showed some similarities. Sexual dimorphism was not observed in alkanes extracted from adults. A novel series of alkadienes was found in all Anastrepha and Ceratitis but not in Dacus.
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    Biochemical effects of sublethal doses of cypermethrin on the sixth-instar larvae of Tribolium castaneum (Herbst.) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 447-455 
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    ISSN: 0739-4462
    Keywords: Tribolium castaneum larvae ; cypermethrin ; biochemical effect of synthetic pyrethroid ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Effects of sublethal doses ie, 2, 4, 10, and 20 ppm of cypermethrin, were studied on the sixth-instar larvae of Tribolium castaneum (Herbst.). Of all the biochemical parameters tested, the free amino acids and cholesterol content and the activity of amylase were found to be the most sensitive components. Glutamate pyruvate transaminase activity was elevated at all doses except 2 ppm. The activities of alkaline phosphatase and glutamate oxaloacetate transaminase and glucose content were raised significantly at doses of 10 and 20 ppm. Acid phosphatase activity and the soluble protein content increased at a dose of 20 ppm. Total lipid and triglycerides, however, decreased significantly at this sublethal dose. Other biochemical parameters, such as cholinesterase and lactate dehydrogenase activities and the total protein, urea, glycogen, DNA, and RNA contents, were not significantly affected by exposure to different doses of cypermethrin.
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    Disinhibition of oocyte growth in adult, virgin Periplaneta americana by corpus allatum denervation: Age dependency and relatedness to mating (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 471-483 
    Details
    ISSN: 0739-4462
    Keywords: oogenesis ; neuroendocrine regulation ; juvenile hormone production ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Unilateral section of the nervi corporis allati I (NCA-1) of isolated, starved, adult, virgin Periplaneta americana disinhibited oocyte growth during a specific period following their adult emergence. The effect required that the corpus allatum (CA) be free of NCA-1 innervation for 4 days beyond the time the females were 7-8 days old. The onset of this sensitive period corresponds to when most isolated, starved virgins become sexually receptive. The results suggest that NCA-1 inhibition of CA activity, initiated about 7 days, is relieved by mating. When done on sexually receptive, starved virgins, unilateral NCA-1 section was as effective as insemination for stimulating growth and chorionation of the first generation of oocytes. Neural inhibition of juvenile hormone (JH) secretion by the CA may also explain diminished production of oocytes by isolated, fed virgins, for during 30 days following unilateral NCA-1 section they produced 2.6 to 5 times more oothecae than did controls with a single CA removed or after the sham operation. The number of oothecae deposited by fed virgins was similarly increased after bilateral NCA-1 section, but to a lesser extent than when the operation was done on fed, inseminated females of the same age.Specificity of the response of the CA to denervation was substantiated by experiments in which the CA were extirpated and reimplanted, by topically applying C16JH, and by experiments in which the nervus corporis cardiaci 1 and 2 on the right or left side were severed.
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    Masthead (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986) 
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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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    Proteolytic enzymes and blood digestion in the mosquito, Culex nigripalpus (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 147-160 
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    ISSN: 0739-4462
    Keywords: trypsin ; proteases ; Culex nigripalpus ; blood digestion ; peritrophic membrane ; radioimmunoassay ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The synthesis of proteolytic enzymes in the fat body and midgut of female Culex nigripalpus was followed. The effects of brain factor(s) and RNA levels in the fat body were correlated with the synthesis of proteolytic enzymes. Trypsinlike activity in the midgut of C. nigripalpus accounted for 80% of total proteolytic activity, whereas chymotrypsinlike activity accounted for 5-7% of total proteolytic activity. Synthesis of porteases in the midgut and fat body reached a peak at 35 h and 22 h after the blood meal, respectively. In the fat body, proteolytic enzyme activity fell to a low level 30 h after the blood meal, but activity in the midgut reached a low level 58 h after the blood meal. The presence of low protease activity in the fat body at the time of peak vitellogenin synthesis indicated that processing of vitellogenin was not done in this tissue.Fat bodies incubated in vitro in the presence of [14C]valine synthesized a [14C]labeled trypsinlike molecule identified as such with antitrypsin antibodies and specific substrate p-toluene-sulphonyl-L-arginine methylester (TAME) and on disc gel electrophoresis in the presence of dodecyl sulfate. The sizes of the proteins found inside and outside the peritrophic membrane were determined by gel-chromatography and disc gel electrophoresis in the presence of dodecyl sulfate. The molecular weight (± SEM) of the largest polypeptide that migrated through the peritrophic membrane into the ectoperitrophic space was found to be 23,000 ± 2,000 daltons. Based on these results, a model is proposed to account for blood digestion in the mosquito midgut, along with the role of the peritrophic membrane.
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    Linoleic acid biosynthesis in the pea aphid, Acyrthosiphon pisum (Harris) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 193-203 
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    ISSN: 0739-4462
    Keywords: Linoleic acid biosynthesis ; A. pisum ; polyunsaturated fatty acids ; symbiotes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The pea aphid Acyrthosiphon pisum (Harris) incorporated [1-14C]acetate into a phospholipid dienoic fatty acid in a time-dependent manner. In 2-h incubations, the incorporation of radioactivity into the 18:2 fraction was minimal, whereas after 45 h 18:2 was the major fatty acid labeled. Ozonolysis of the isolated dienoic fatty acid methyl ester followed by radio-gas-liquid chromatography showed that radioactivity was associated with fragments containing carbons 1-9 and 13-18. These data established the location of the double bonds in the 9,12 positions and indicated that the entire molecule was labeled from [1-14C]acetate. Tetracycline-treated aphids synthesized linoleic acid in the same proportions as untreated controls. Scanning electron microscopy showed that over 50% of the treated insects had greatly reduced numbers of intracellular symbiotes or lacked them or most of the existing symbiotes had an abnormal appearance. Therefore, we conclude that intracellular symbiotes are not involved in the biosynthesis of linoleic acid in the pea aphid.
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    Identification of male-specific exocrine secretions from predatory stink bugs (Hemiptera, pentatomidae) (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 1-12 
    Details
    ISSN: 0739-4462
    Keywords: semiochemical ; isovalerate ; trimethyltetradecanol ; Heteroptera ; Hemiptera ; predator ; exocrine ; Perillus ; Stiretrus ; Oplomus ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the nearctic predaceous stink bugs (Asopinae), Perillus bioculatus and Stiretrus anchorago, and the neotropical asopine, Oplomus severus, males possess conspicuous sternal glands that are absent in females. In each of these species, the male sternal gland secretion contains predominantly a single compound; 6,10,13-trimethyltetradecyl isovalerate in the allopatric species, P. bioculatus and O. severus, and 6,10,13-trimethyltetradecanol in S. anchorago, a species sympatric with P. bioculatus. The function of the sternal gland secretions from asopine hemipterans is unknown.
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    Properties of the Δ11-desaturase enzyme used in cabbage looper moth sex pheromone biosynthesis (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 45-52 
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    ISSN: 0739-4462
    Keywords: cabbage looper ; Trichoplusia ni ; sex pheromone biosynthesis ; desaturase ; microsomes ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The biosynthesis of a large number of sex pheromone components of various moth species can be explained by invoking a Δ 11-desaturation of common fatty acids. A Δ11-desaturase system from Trichoplusia ni, the cabbage looper moth, is identified and partially purified. Some of its properties are defined and compared with those of the ubiquitous Δ-9 desaturase enzyme. Similarities between the two systems include subcellular location (microsomal), substrate specificity (16- and 18-carbon acids), and lack of sensitivity to carbon monoxide, while differences include cofactor preference (NADH rather than NADPH), sensitivity to cyanide ion, pH optimum (7.4-7.8 vs 6.8-7.2), and location in the organism (in the pheromone gland compared to generally distributed). The effects of insect age were also investigated.
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    Binding of insecticides to lipophorin and arylphorin, two hemolymph proteins of Heliothis zea (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 87-96 
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    ISSN: 0739-4462
    Keywords: insecticide binding proteins ; lipophorin ; arylphorin ; storage protein ; Heliothis zea ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The binding of different insecticides to hemolymph proteins of the corn earworm, Heliothis zea, was studied by an analytical isoelectric focusing technique. Two proteins capable of binding hydrophobic substrates were discovered and identified as lipophorin and arylphorin. Lipophorin, the major lipoprotein of Heliothis zea, demonstrated rather unspecific binding of xenobiotics of different hydrophobicities. Arylphorin, a putative storage protein, revealed strong affinity for compounds of medium polarity, binding only weakly to insecticides of higher or lower polarity.
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    Isolation and characterization of Brush border fragments from mosquito mesenterons (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 135-146 
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    ISSN: 0739-4462
    Keywords: mosquito ; mesenteron ; brush border ; enzymes ; electrophoresis ; electron microscopy ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Brush border fragments were isolated from homogenates of mesenterons from the mosquito, Culex tarsalis, by a combination of Ca2+ precipitation and differential centrifugation. These preparations were routinely enriched seven- to eightfold for the brush border marker enzyme, leucine aminopeptidase. Alkaline phosphatase, a putative brush border marker for both vertebrate and invertebrate brush borders, was found to be unsuitable for Cx. tarsalis. Isoelectric focusing electrophoresis coupled with histochemical enzyme detection was used to enumerate isozymic species of nonspecific esterases [3], leucine aminopeptidase [1], and alkaline phosphatase [1] in isolated brush border fragments. Leucine aminopeptidase activity was solubilized by papain digestion, suggesting an extrinsic active site for this membrane-bound enzyme. The predominant nonspecific esterase isozyme remained membrane-bound. Conventional staining (ie, Coomassie Blue and silver) of proteins separated by isoelectric focusing, sodium dodecylsulfate, and two-dimensional electrophoresis indicated a simple pattern for brush border fragments, with two proteins predominating among the 11-14 routinely detected.
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    Modulatory effects of octopamine and serotonin on male sensitivity and periodicity of response to sex pheromone in the cabbage looper moth, Trichoplusia ni (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 161-171 
    Details
    ISSN: 0739-4462
    Keywords: sex pheromone ; sustained-flight tunnel ; Trichoplusia ni ; octopamine ; serotonin ; 5-hydroxytryptamine ; biogenic amines ; circadian rhythms ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The pheromone-mediated flight behavior of male cabbage looper moths in a sustained-flight tunnel and random activity exhibited during scotophase were observed after males were treated with octopamine or serotonin (5 hydroxytryptamine). Octopamine induced a hypersensitivity to the olfactory signal, resulting in a significant lowering of the pheromone dose that elicited peak levels of response. Octopamine, however, did not affect the circadian rhythmicity of response to pheromone. In contrast, serotonin disrupted the circadian rhythmicity of response, resulting in a high percentage of males exhibiting random activity and response to pheromone throughout the entire 8 h scotophase instead of during the normal peak period during the latter part of the scotophase. Serotonin did not effect a decrease in the dose of pheromone eliciting peak response. In addition, at the highest dosages tested octopamine and serotonin induced opposite postures associated with a paralysis that occurred when males attempted to take flight to the pheromone.
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    Partial characterization of a major gut thiol proteinase from larvae of Callosobruchus maculatus F. (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 561-575 
    Details
    ISSN: 0739-4462
    Keywords: Callosobruchus maculatus ; proteinase inhibitors ; thiol digestive proteinase ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Much of the proteolytic activity in the digestive tract of Callosobruchus maculatus larvae can be attributed to a thiol proteinase(s) that hydrolyzes [3H]methemoglobin optimally at pH 5.0. Maximal hydrolysis of [3H]methemoglobin, [3H]alpha-casein, and N-benzoyl-DL-arginine napthylamide-(BANA) required the presence of thiol reducing agents. Larval gut proteinase activity was strongly inhibited by p-hydroxymercuribenzoic acid (pHMB), Nethylmaleimide (NEM), and iodoacetic acid (IAA) but was unaffected by the Bowman-Birk and Kunitz proteinase inhibitors from soybeans or by lima bean trypsin inhibitor. L-Trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (E-64), a specific inhibitor of thiol proteinases, potently inhibited proteolysis of [3H]methemoglobin by larval gut homogenates. Proteolytic activity in the larval gut was located in the lumen contents and thus appears to play a major role in extracellular digestion. The pH of the larval midgut is slightly acidic, and midgut contents exhibit a negative redox potential, conditions supporting the activity of a thiol proteinase. The significance of these findings is discussed with reference to the vulnerability of this digestive proteinase as a target for existing or genetically engineered plant chemical defenses.
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    Regulation of insect gene expression July 18-20, 1985 (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 3-5 
    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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    Juvenile hormone-regulated locust vitellogenin genes: Lack of expression after transfer into Drosophila (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 35-46 
    Details
    ISSN: 0739-4462
    Keywords: locust ; vitellogenin ; juvenile hormone ; P element ; Drosophila ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In Locusta migratoria, vitellogenin (Vg) is normally produced only in adult female fat body under stimulation by juvenile hormone (JH). This permits study of (a) programming of genes for expression and (b) modulation of expression by JH. From L. migratoria genomic libraries, two Vg genes (A and B) have been cloned. Coding regions encompass 10-12 kbases of DNA, contain introns, and hybridize with 6,300 nucleotide mRNAs. Although the 5'-exons, coding for signal peptides, are similar in sequence, the remaining coding sequences have distinct restriction maps and show no crosshybridization. Upstream DNA from the two genes has some sequence similarity, corresponding to potential regulatory regions. Dot hybridization assays of mRNAs A and B in locust fat body after induction by methoprene show coordinate expression of the two Vg genes and also a third, unidentified JH-regulated gene. In the hope of providing a system for identification of control sequences, P element-mediated transformation has been used to transfer locust DNA into Drosophila. From Vg gene B, a central block was deleted, to give a mini-Vg gene comprising 5' and 3' terminal coding sequences plus upstream flanking DNA. This was incorporated into the P element vector Carnegie 20 and injected into Drosophila embryos. Three transformed fly lines were obtained in which the locust mini-Vg gene was integrated at different chromosomal sites. On Northern blots of fly RNA, however, no expression of the locust sequences could be detected, even though the accompanying rosy gene was expressed. This suggests that the locust regulatory sequences were not recognized in Drosophila, and current effort is directed toward developing a homologous locust transformation system for expression assay of cloned JH-regulated genes.
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    Stage-specific mechanisms regulate the expression of the dopa decarboxylase gene during Drosophila development (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 97-104 
    Details
    ISSN: 0739-4462
    Keywords: enzyme induction ; Drosophila ; steroid hormone ; 20-hydroxyecdysone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Transcripts of the dopa decarboxylase (Ddc) gene accumulate within 4 h of the administration of 20-OH-ecdysone to mature larvae of Drosophila. The increase can be explained as the sum of a direct steroid effect, independent of protein synthesis, and an indirect effect, dependent on proteins synthesized after an increase in the hormone titer. By contrast, the peaks of DDC activity in embryos, and perhaps in the first two larval instars and in imaginal discs as well, cannot be ascribed to any direct steroid effects. In fact, a decreasing hormone titer might be required before the Ddc gene can be expressed at these stages. The stage-specific differences in the molecular mechanisms regulating Ddc gene activity may be reflected in the phenotype of an activity variant, Ddc+4. Molecular studies now underway on the variant Ddc gene might help us to understand the complex multifunctional region that we believe lies upstream of the gene and regulates its expression during development.
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    Announcements (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 600-600 
    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.940030609
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    The polypeptide structure of Vitellogenin and Vitellin from the cockroach, Leucophaea maderae (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 577-591 
    Details
    ISSN: 0739-4462
    Keywords: Leucophaea maderae ; polypeptide structure ; protein processing ; yolk proteins ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Vitellogenin (Vg) synthesized by the fat body of Leucophaea maderaeis made up of four polypeptides with molecular weights of 160,000, 105,000, 98,000, and 57,000. Other polypeptides previously reported as part of Vg are associated with other proteins. Vitellin (Vt), the yolk protein (YP) isolated from mature oocytes and from newly formed oothecae, is a protein with a sedimentation coefficient of 28s and consists of three polypeptides with molecular weights of 105,000, 85,000, and 57,000. During vitellogenesis, the YP of developing oocytes contains both Vt and a 14s component. The 14s component is made up of four polypeptides with molecular weights of 105,000, 90,000, 85,000, and 57,000. The data suggest that 14s may not be a discrete protein but rather a form in transition between Vg and Vt in which the 98,000 dalton polypeptide is converted to the 85,000 dalton polypeptide of Vt through a 90,000 dalton intermediate. The 160,000 dalton peptide of Vg does not appear to be a part of Vt. Under alkaline conditions, both the 14s component and Vt are reduced to a polypeptide with a lower sedimentation rate in sucrose gradients. When acid conditions are restored, a protein resembling 14s is obtained. This suggests that the YP is a loosely held aggregate of similar or identical proteins with a molecular weight of about 250,000.
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    Masthead (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986) 
    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.940030101
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    Major hemolymph proteins from larvae of the black swallowtail butterfly, Papilio polyxenes (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 539-550 
    Details
    ISSN: 0739-4462
    Keywords: lipophorin ; arylphorin ; storage protein ; hemolymph ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Three major hemolymph proteins of Papilio polyxenes larvae were isolated and characterized. Density gradient ultracentrifugation of hemolymph resulted in flotation of the major lipoprotein, lipophorin. P. polyxenes larval lipophorin is composed of two apoproteins, apolipophorin-I and apolipophorin-II, plus a mixture of lipids, to give a density of 1.13 g/ml. Immunoblotting experiments using antisera directed against Manduca sexta apolipophorin-I and apolipophorin-II, respectively, revealed cross-reactivity of apoLp-I with Manduca sexta apoLp-I, and apoLp-II with M. sexta apoLp-II.Gel permeation chromatography of the subnatant obtained following density gradient ultracentrifugation revealed the presence of a major protein peak which was shown to contain three major serum proteins, two of which were isolated and characterized. One of these proteins was purified by lectin affinity chromatography. Both proteins have native molecular weights in the range of 450,000 and appear to be hexamers of a single subunit type. Major serum protein-1 is nonglycosylated and has a subunit molecular weight of 75,000. Major serum protein-2 is glycosylated and has a subunit molecular weight of 74,000. Amino acid analysis of this protein revealed a tyrosine plus phenylalanine content of 20 mole percent, characteristic of the arylphorin class of insect storage proteins. Using antibodies against M. sexta larval hemolymph proteins, both the P. polyxenes major serum proteins were shown to be immunologically related to serum proteins of other lepidopteran species.
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    Masthead (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986) 
    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.940030701
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    Alternative ligands for measurement and purification of ecdysteroid receptors in Drosophila Kc cells (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 25-33 
    Details
    ISSN: 0739-4462
    Keywords: photoaffinity labeling ; kaladasterone ; muristerone A ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: An ecdysteroid-binding protein has been demonstrated in nuclear and cytosolic extracts of cultured Drosophila cells (Kc cells). Attempts to purify the binding moiety have been hampered because of the small number of binding sites (ca 1,000/cell) and sensitivity of the ecdysteroid binding moiety toward salt (dissociation at 150 mM). Recently 3α[3H]kaladasterone and 3α[3H]muristerone A have been synthesized. The binding kinetics of these two ecdysteroids are similar to ponasterone A. Photoaffinity labeling of the ecdysteroid receptor in Kc cells was attempted using the 3α[3H]kaladasterone, and standard protein chromatographic techniques have been used to examine the 3α[3H]muristerone A-receptor complex, which is less sensitive to salt dissociation. Attempts to characterize the protein to which these ligands have been attached will be discussed.
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    The paradigm of stage-specific gene sets in insect metamorphosis: Time for revision! (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 47-57 
    Details
    ISSN: 0739-4462
    Keywords: metamorphosis ; cuticular proteins ; juvenile hormone ; alcohol dehydrogenase ; Drosophila melanogaster ; gene sets ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Students of insect metamorphosis have in the past accepted the paradigm that the structures of different metamorphic stages are built from molecules coded for by different sets of genes. A substantial body of evidence, based on cuticular proteins, has now accumulated that casts doubt on that paradigm. This paper summarizes the evidence and provides a new framework for viewing the activities of genes during metamorphosis.Studies on promoter utilization for alcohol dehydrogenase in Drosophila melanogaster reveal that cells change promoters at the onset of metamorphosis. These data suggest that modifications of regulatory elements rather than duplications of structural genes may have occurred to permit the evolution of metamorphosis.
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    Regulation of cockroach oothecin synthesis by juvenile hormone (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 59-73 
    Details
    ISSN: 0739-4462
    Keywords: gene expression ; chorion ; homology ; cockroach ; oothecin ; juvenile hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Control of specific protein synthesis by juvenile hormone during sexual maturation and reproduction is being studied in the left colleterial gland of the cockroach Periplaneta americana. Rates of specific oothecin synthesis and oothecin mRNA concentrations have been measured during sexual maturation and the effects of allatectomy and administration of juvenile hormone determined. The heterogeneity of the oothecins has been characterized and found to be due probably to a multiplicity of structural genes. The complete primary structure of the major oothecin has been deduced from the sequences of cloned cDNAS. It can be divided into a central region and two flanking arms that share sequence features. The structures of the oothecins show strong homologies with the silkmoth chorion proteins.
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    Activation of storage protein receptor by 20-hydroxyecdysone (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 105-118 
    Details
    ISSN: 0739-4462
    Keywords: Sarcophaga ; fat body ; membrane ; pupation ; cycloheximide ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A storage protein receptor was shown to be present in membranes of the pupal fat body of Sarcophaga peregrina, whereas membranes of the larval fat body contained a cryptic receptor. The molting hormone, 20-hydroxyecdysone, was essential for activation of the cryptic receptor to bind and incorporate the storage protein. The active receptor in the pupal fat body membrane was a protein with a molecular mass of 120-kdaltons. It was found that a 125-kdalton protein, a cryptic receptor for storage protein, present in the larval fat body membrane was converted to an active receptor in the presence of 20-hydroxyecdysone, without accompanying appreciable new protein synthesis.
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    Hormonal regulation of sequential larval cuticular gene expression (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 75-86 
    Details
    ISSN: 0739-4462
    Keywords: Manduca sexta ; 20-hydroxyecdysone ; cuticle ; genes ; gene regulation ; juvenile hormone ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: As the tobacco hornworm (Manduca sexta) larva feeds and grows, the abdominal epidermis synthesizes larval endocuticular proteins. During a molt this synthesis temporarily ceases while the cells deposit a new epicuticle; then these proteins reappear in a sequential manner, some before ecdysis, others after ecdysis. At the time of metamorphosis, the epidermis becomes pupally committed and ceases synthesizing these endocuticular proteins. Northern and dot blot hybridization analysis using cDNA clones for three different low-molecular-weight larval cuticular proteins showed that RNA transcription of all three ceased by the time of head cap slippage during the molt, then begins again just before ecdysis, one showing a different time course from the other two. All responded to the commitment peak of ecdysteroid in the absence of juvenile hormone (JH) by a permanent cessation of transcription.During the final day of feeding (day 3) of the 5th instar the cuticular lamellae become 5-10 times thinner coincidentally with a change in cuticular protein synthesis involving a cessation of synthesis of many of the endocuticular proteins and the appearance of at least three new proteins  -  14.5, 15, and 27 kd (kilodaltons). Incubation of day 15th instar epidermis with 10-100 ng/ml 20-hydroxyecdysone (20HE) induced the synthesis of the 27-kd protein and the transcription of the mRNAs for the 14.5- and 15-kd proteins. Incubation in the absence of hormones or with 20HE in the presence of JH prevented the appearance of these new proteins and the deposition of thin lamellae. The mRNAs for three endocuticular proteins whose synthesis ceases on day 3 showed differing responses to 20HE and JH. Thus, the sequential program of larval endocuticular gene expression is controlled primarily by hormonal titers in both the molt and the intermolt periods.
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    Developmental and ecdysteroid regulation of gene expression in the larval fat body of Drosophila melanogaster (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 133-141 
    Details
    ISSN: 0739-4462
    Keywords: P element transformation ; gene regulation ; larval serum proteins ; Drosophila ; ecdysteroids ; fat body ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Six major transcripts encoding the α, β, and γ subunits of the larval serum protein LSP-1, the single subunit of the LSP-2, and the P1 and P6 polypeptides appear sequentially in the fat body tissue during the third larval stage of Drosophila melanogaster. Northern blot analysis shows that the transcription of the LSP-2 and P1 mRNAs is restricted temporally to the third instar and the early phase of pupal development and spatially to the fat body tissue. The synthesis and/or accumulation of the LSP-2 and P1 transcripts are differentially affected by mutations of the dor and occ loci of the 2B5 complex of genes involved in the trans-regulation of the activity of ecdysteroid-responsive genes. Application of the P element-mediated germ line transformation to the P1 gene shows that correct developmental expression of this gene requires no more than 1.5 kb of DNA sequences upstream from the mRNA start site.
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    Ecdysone regulation of cuticle protein gene expression in Drosophila (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 3 (1986), S. 119-132 
    Details
    ISSN: 0739-4462
    Keywords: Ecdysone ; cuticle proteins ; gene expression ; Drosophila ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The deposition and apolysis of insect cuticles have long been known to be regulated by ecdysone. Unsclerotized, chitin-containing procuticles contain evolutionarily conserved, hydrophobic proteins that are soluble in solutions of denaturing agents. The pupal procuticle of Drosophila is deposited by larval and imaginal epidermis starting 9 h after puparium formation when the ecdysone titer is low. Initially, a set of low molecular weight proteins (less than 25,000 daltons; low molecular weight pupal cuticle proteins = S-PCPs) is synthesized. However, about the time of pupation, synthesis of S-PCPs ceases, and high molecular weight proteins (greater than 50,000 daltons; H-PCPs) are synthesized. In vitro experiments indicate that the initial formation of the procuticle with synthesis of the S-PCPs requires a pulse of hormone followed by withdrawal (6 h with 20-hydroxyecdysone, 1 μg/ml). The switch from synthesis of S-PCPs to H-PCPs is facilitated by a second, short pulse of 20-hydroxyecdysone (0.1 μg/ml, 3 h). Ultrastructural localization demonstrates that the S-PCPs are located only in the external lamellae of the procuticle, while the H-PCPs are present only in internal lamellae. Developmental analyses with cloned genes indicate that cuticle protein genes are expressed during only one stage of Drosophila development. Some of the genes encoding S-PCPs are limited in their expression to larval (posterior) or imaginal (anterior) epidermis. Preliminary molecular analyses of the larval and pupal cuticle protein genes indicate that they are organized in different ways. For example, four larval genes exist in a cluster with divergent transcription, and one PCP gene, PCP-GART, is located within an intron of a “housekeeping” gene.
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    URL: http://dx.doi.org/10.1002/arch.940030713
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