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  • Life and Medical Sciences  (21)
  • 550 - Earth sciences  (13)
  • l-canavanine  (6)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Phytochemistry 30 (1991), S. 1055-1058 
    ISSN: 0031-9422
    Keywords: Canavalia ensiformis ; Leguminosae ; canavanyl proteins ; insects. ; l-canavanine ; non-protein amino acid ; toxicity
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part A: Physiology 52 (1975), S. 105-108 
    ISSN: 0300-9629
    Keywords: Leguminosae ; Manduca sexta ; O-ureido-l-homoserine ; Plant-insect interactions ; amino acid toxicity ; canaline-urea cycle ; l-canaline ; l-canavanine ; l-canavaninosuccinate ; ornithine-urea cycle ; tobacco hornworm
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part A: Physiology 52 (1975), S. 105-108 
    ISSN: 0300-9629
    Keywords: Leguminosae ; Manduca sexta ; O-ureido-l-homoserine ; Plant-insect interactions ; amino acid toxicity ; canaline-urea cycle ; l-canaline ; l-canavanine ; l-canavaninosuccinate ; ornithine-urea cycle ; tobacco hornworm
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical Systematics and Ecology 9 (1981), S. 219-220 
    ISSN: 0305-1978
    Keywords: Bruchidae ; Caryedes brasiliensis ; Dioclea megacarpa ; Leguminosae ; insect nitrogen excretion ; l-canavanine ; plant-insect interaction
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical Systematics and Ecology 17 (1989), S. 203-206 
    ISSN: 0305-1978
    Keywords: Canavalia ensiformis ; Leguminosae ; allelochemical detoxification ; l-canaline ; l-canavanine ; oxime formation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of chemical ecology 9 (1983), S. 803-815 
    ISSN: 1573-1561
    Keywords: Caryedes brasiliensis ; Coleoptera ; Bruchidae ; l-canavanine ; l-canaline ; Dioclea megacarpa (Leguminosae) ; allelochemicals ; detoxification ; adaptation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract This communication reviews recent biochemical studies ofl-canavanine that have provided significant understanding of the interaction between the seed ofDioclea megacarpa (Leguminosae) and the bruchid beetleCaryedes brasiliensis (Bruchidae). The principal biochemical bases are proposed for: canavanine toxicity, the ability of the beetle larvae to adapt to its presence, the metabolic sequestration and detoxification of ammonia, and the potential amplification by microbial symbionts of the beetle's abilities to adapt to toxic components of the host.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 0730-2312
    Keywords: IGF-I receptor ; T-cells ; OKT-3 ; PHA ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The biological effects of the IGFs are mediated through interaction with specific cell surface receptors. It has been previously reported that mitogenic activation of T-lymphocytes by phytohemagglutinin (PHA) is associated with increased IGF-I receptor content. However, the mechanisms which regulate IGF-I receptor expression during T-lymphocyte activation are unknown. To explore further the regulation of IGF-I receptor expression in T-cells, we investigated IGF-I receptor content and mRNA abundance in T-lymphocytes after stimulation either by PHA or OKT-3, the latter being a monoclonal antibody directed against the CD-3 antigen of the T-cell receptor IGF-I binding in T-cells demonstrated increased IGF-I receptor content after stimulation by both PHA and OKT-3. Peak binding was induced after 72 h of treatment with PHA and 48 h of treatment with OKT-3. Affinity cross-linking of 125I-IGF-I to T-cell membranes demonstrated a single ∼ 130 kDa band which was increased after treatment with PHA or OKT-3. This band was inhibited by the addition of α-IR3, a monoclonal antibody to the IGF-I receptor. Both PHA and OKT-3 increased IGF-I receptor mRNA abundance with peak increases at 20 h and 60 h, respectively. Parallel increases in IGF-I receptor and β-actin mRNA abundance were observed, consistent with previous studies demonstrating increased actin gene expression after T-cell activation. Thus, the increase in IGF-I receptor mRNA abundance markedly preceded the increase in IGF-I receptor content after PHA stimulation, but the increase in IGF-I receptor mRNA abundance followed the increase in IGF-I receptor content after OKT-3. These studies suggest, therefore, that IGF-I receptor content in both of these activated cells is not regulated primarily at the level of steady state mRNA.
    Additional Material: 3 Ill.
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  • 8
    ISSN: 0730-2312
    Keywords: mouse sarcoma 180 cells ; tissue inhibitor of metalloproteinases ; angiogenesis ; endothelial cells ; metalloproteinases ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: We have previously shown that mouse sarcoma 180 cells produce vascular endothelial growth factor [VGEF; Rosenthal et al., 1990, Growth Factors, 4: 53-59], endothelial mitogen that stimulates angiogeneis. Recent reports have implicated metallaproteinases and their inhibitors in the regulation of vascular morphogeneis, tumor invasion, and metastasis. We report here that mouse sarcoma 180 cells produce two collagenase inhibitors. These inhibitors were purified by heparin-Sepharose affinity chromatography, gel filtration, and C4 reverse phase h.p.l.c. Analytical gel electrophoresis of the purified inhibitors (MS-22 and MS-31) revealed molecular masses of 22,000 and 32,000 Da under reducing conditions, and 20,000 and 30,000 Da under nonreducing conditions, respectively. The NH2-terminal amino acid sequence of MS-22 was identical to that of tissue inhibitor of metalloproiteinases type 2 (TIMP-2) produced by human melanoma cells (Stetler-Stevenson et al., 1989, J. Biol. Chem. 264: 17374-17378) over the first 30 amino acids. The NH2-terminal amino acid sequence of MS-31 was identical to that of murine TIMP-1 [Gewert et al., 1989 EMBO J 6:651-657]. Statistical analysis of the amino acid composition data of these two mouse sarcoma 180-derived collagenase inhibitors confirms the identificationof MS-22 as TIMP-2 and MS-31 as TIMP-1.
    Additional Material: 1 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 60 (1996), S. 529-537 
    ISSN: 0730-2312
    Keywords: phospholipids ; phosphatidylserine ; sphingosine ; sphingosine-1-phosphate ; sphingosine kinase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Sphingosine-1-phosphate (SPP) is a unique sphingolipid metabolite involved in cell growth regulation and signal transduction. SPP is formed from sphingosine in cells by the action of sphingosine kinase, an enzyme whose activity can be stimulated by growth factors. Little is known of the mechanisms by which sphingosine kinase is regulated. We found that acidic phospholipids, particularly phosphatidylserine, induced a dose-dependent increase in sphingosine kinase activity due to an increase in the apparent Vmax of the enzyme. Other acidic phospholipids, such as phosphatidylinositol, phosphatidic acid, phosphatidylinositol bisphosphate, and cardiolipin stimulated sphingosine kinase activity to a lesser extent than phosphatidylserine, whereas neutral phospholipids had no effect. Diacylglycerol, a structurally similar molecule which differs from phosphatidic acid in the absence of the phosphate group, failed to induce any changes in sphingosine kinase activity. Our results suggest that the presence of negative charges on the lipid molecules is important for the potentiation of sphingosine kinase activity, but the effect does not directly correlate with the number of negative charges. These results also support the notion that the polar group confers specificity in the stimulation of sphingosine kinase by acidic glycerophospholipids. The presence of a fatty acid chain in position 2 of the glycerol backbone was not critical since lysophosphatidylserine also stimulated sphingosine kinase, although it was somewhat less potent. Dioleoylphosphatidylserine was the most potent species, including a fourfold stimulation, whereas distearoyl phosphatidylserine was completely inactive. Thus, the degree of saturation of the fatty acid chain of the phospholipids may also play a role in the activation of sphingosine kinase. © 1996 Wiley-Liss, Inc.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 41 (1995), S. 287-299 
    ISSN: 1040-452X
    Keywords: SGP-1 ; SGP-2 ; Postnatal development ; Nonciliated cells ; Efferent ducts ; Rats ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Sulfated glycoprotein (SGP) -1 and -2, secretory products of Sertoli cells, are secreted into the lumen of seminiferous tubules where they bind to late spermatids. Once released, the spermatozoa traverse the efferent ducts where these proteins detach from their surface and are endocytosed by the nonciliated cells. In adult animals, SGP-1 and SGP-2 are also synthesized by nonciliated cells and targeted from the Golgi apparatus to lysosomes. The purpose of the present study was to determine the pattern of expression of SGP-1 and SGP-2 within nonciliated cells during postnatal development. The efferent ducts of animals at different postnatal ages were prepared for an electron microscopic immunocytochemical quantitative analysis as well as for Northern blot analysis. The data expressed as labeling content (no. gold particles/μm2 and taking into account the volume of the endocytic or-ganelles and the cell) revealed that anti-SGP-1 labeling in endosomes of nonciliated cells was minimal at 15, 21, and 29 days of age. On the other hand, the lysosomal labeling content showed a significant increase by day 29 compared to 15 and 21-day-old animals indicating that an endogenous form of SGP-1 was being synthesized by nonciliated cells and targeted to lysosomes. By day 39 a significant increase in endosomal labeling occurred; this was attributed to the endocytosis of Sertoli-derived SGP-1 which coincided with the entry of spermatozoa into the lumen of these ducts at this age. Lysosomal labeling showed further significant increases at days 39, 49, and then again at day 90. Northern blot analysis detected SGP-1 mRNA transcripts at all postnatal ages examined. While decreases or increases in transcripts could not be determined due to the greater amount of tissue present with increasing age, these data taken together support the idea of an endogenous form of SGP-1 being synthesized by nonciliated cells and targeted to lysosomes during postnatal development.In the case of SGP-2, endosomal labeling was minimal at 15, 21, and 29 days of age but was significantly increased by day 39, with similar values at all subsequent ages. The high value at day 39 was attributed to the endocytosis of SGP-2 which coincided with the entry of spermatozoa into the lumen at this age. Lysosomal labeling, on the other hand, was low at days 15 and 21 but peaked at day 29 at a time when endosomal labeling was minimal. These results suggested the synthesis of an endogenous form of SGP-2 which was being targeted to lysosomes. Similar values for SGP-2 lysosomal labeling comparable to that at day 29 were obtained at all other ages. Since SGP-2 endosomal labeling was significantly increased at day 39 and maintained thereafter, it is suggested that labeling in lysosomes at this and subsequent ages could also be due to the endocytosis of Sertoli-derived SGP-2. However, Northern blot analysis confirmed the presence of mRNA transcripts for SGP-2 at all postnatal ages examined, although increases or decreases in their amount were not determined. These results thus consolidate the hypothesis of an endogenous form of SGP-2 being synthesized by nonciliated cells and targeted to lysosomes. Finally, since the amounts of endogenous SGP-1 and SGP-2 peak at different ages, it is suggested that different factors are involved in regulation of these two proteins during postnatal development. © 1995 Wiley-Liss, Inc.
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