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  • Articles: DFG German National Licenses  (2)
  • Cell & Developmental Biology  (1)
  • insolin action  (1)
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  • Articles: DFG German National Licenses  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 69 (1985), S. 83-90 
    ISSN: 1573-4919
    Keywords: Insulin receptor ; phosphorylation ; indomethacin ; insolin action
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Insulin stimulated phosphorylation of tyrosine residues by the insulin receptor kinase may be part of a signalling mechanism associated with insulin's action. We report that indomethacin inhibited the phosphorylation of the β-subunit of the solubilized adipocyte insulin receptor. Indomethacin also inhibited several insulin-sensitive processes in intact rat adipocytes. Indomethacin (1 mM) inhibited basal phosphorylation of the β-subunit of the solubilized insulin receptor by 6007o and insulin-stimulated phosphorylation by 30%. In adipocytes, indomethacin inhibited basal 3-0-[methyl-14C]-methyl-D glucose transport by 50070 (P 〈 0.01), D-[6-14C]-glucose oxidation by 5007o (P 〈 0.01), D-[6-14C]-glucose conversion to lipid by 30010 (P 〈 0.01), and D-[1-14C]-glucose conversion to lipid by 6007o (P〈0.01). Similarly, indomethacin inhibited insulin-stimulated 3-0-[methyl-14C]-methyl-D-glucose transport by 75070 (P〈0.01), D-[6-14C]-glucose oxidation by 20% (P〈0.05), D-[1-14C]-glucose oxidation by 35070 (P〈0.01), D-[6-14C] glucose conversion to lipid by 25010 (P〈0.01), and D-[1-14C] glucose conversion to lipid by 4501o (P〈0.01). In contrast, insulin binding to its receptor, basal D-[1-14C]-glucose oxidation and both basal and insulin-stimulated activation of glycogen synthase were unaffected by indomethacin. Thus, indomethacin partially inhibited autophosphorylation of the solubilized insulin receptor on tyrosine and partially inhibited some but not all of insulin's actions. This supports the hypothesis that insulin's metabolic effects are linked to activation of the insulin receptor protein kinase and indicates that there may be heterogeneity in the mechanisms of intracellular metabolic control by insulin.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 177 (1973), S. 23-37 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Male rats were maintained on a controlled feeding schedule and groups of animals sacrificed at 2, 15, 21, 36, 48 and 72 hours of fasting. Chemical determinations of glycogen showed that livers of rats fasted two hours contained 8.7% glycogen; 15 hours, 6.2%; 21 hours, 0.7%; 36 hours, 0.7%; 48 hours, 0.8%; and 72 hours, 0.4%. After PA/S procedures, glycogen appeared in hepatocytes of rats fasted 2 and 15 hours as large masses intensely stained. At these time-periods, almost all cells contained significant quantities of glycogen but hepatocytes located toward portal tracts showed larger and more intensely stained masses of glycogen than found in cells near central veins. After longer periods of fasting, glycogen masses decreased in size, number, and staining intensity. The fine structure of hepatocytes from rats fasted 2 or 15 hours showed abundant α and β particles of glycogen in the form of large masses throughout the cytosome. These correlated in position and shape to the masses of glycogen seen in the light microscope. As glycogen depletion occurred (fasted 21 hours and longer) the number of glycogen particles decreased in hepatocytes. It is concluded from this study that a good correlation exists between chemical determinations of hepatic glycogen, cytochemistry of glycogen in hepatocytes, fine structure of liver cells, and the fasting state of the animal.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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