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  • 11
    Digitale Medien
    Digitale Medien
    Springer
    Diabetologia 29 (1986), S. 888-892 
    ISSN: 1432-0428
    Schlagwort(e): casein kinase II ; calmodulin-dependent protein kinase ; cyclic AMP-dependent protein kinase ; polyamines ; pancreatic islets
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The occurrence of polyamine-stimulated protein kinase (casein kinase II) in cytosol of mouse pancreatic islets was investigated. Islet protein phosphorylation was enhanced by spermidine, spermine, lysine-rich histone and polylysine; the major endogenous substrates in the cytosol were three proteins of Mr 50000, 55000 and 100000. Cadaverine and putrescine were without effects. A Mr 100 000 protein is a major substrate for Ca2+-calmodulin-dependent protein kinase, and Mr 50 000 and 55 000 proteins are substrates for cyclic adenosine 3′,5′-cyclic monophosphate (AMP) dependent protein kinase in mouse islets. However, neither cyclic-AMP-dependent protein kinase inhibitor nor trifluoperazine inhibited polyamine-enhanced protein phosphorylation. Both basal and polyamine-enhanced protein phosphorylation patterns were identical when either [γ-32P] adenosine 5′-triphosphate (ATP) or [γ-32P] guanosine 5′-triphosphate (GTP) was used as phosphate donors, indicative of the presence of a polyaminestimulated casein kinase 11 in pancreatic islets. It is suggested that polyamines and polyamine-enhanced casein kinase II activity may have an important role in regulation of protein phosphorylation in pancreatic islets.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 12
    Digitale Medien
    Digitale Medien
    Springer
    Diabetologia 26 (1984), S. 375-378 
    ISSN: 1432-0428
    Schlagwort(e): Adenylate cyclase ; cytosol ; pancreatic islets ; mouse
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The role of cytosolic components in the regulation of mouse pancreatic islet adenylate cyclase activity was studied. Addition of mouse islet cytosol (27000 g supernatant of mouse islet sonicate), devoid of adenylate cyclase activity itself, increased adenylate cyclase activity by 93±17% (n = 9) in the 27000 g total particulate fraction of mouse islets. Addition of GTP stimulated adenylate cyclase activity by 91±11% (n = 13) or to the same degree as cytosol. Like GTP, the substance causing the enhancing activity of the cytosol was found to be dialysable, resistant to heat, sensitive to charcoal treatment and alkaline phosphatase and insensitive to digestion with trypsin. However, in contrast to the stimulation by GTP, the stimulation by cytosol was not inhibited by guanosine 5′-0-(2-thiodiphosphate), and furthermore, the effects of cytosol and GTP were additive. Neither NAD nor phosphoenolpyruvate stimulated adenylate cyclase activity. The cytosolic factor did not confer sensitivity towards glucose, Ca2+ or Ca2+-calmodulin on adenylate cyclase. The results demonstrate that mouse pancreatic islets contain a phosphocompound (or several compounds) distinct from GTP and capable of markedly stimulating adenylate cyclase. The identity of the compound and its physiological significance remain to be established.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 13
    ISSN: 1432-0428
    Schlagwort(e): Pancreatic islets ; glucose metabolism ; diacylglycerol ; diacylglycerol lipase inhibitor
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The effect of interference with diacylglycerol metabolism was investigated in pancreatic mouse islets. In the presence of the diacylglycerol lipase inhibitor RHC 80267, glucose-induced insulin secretion was reduced 50–60%; whereas carbacholin-induced insulin secretion was unaffected. Addition of the diacylglycerol kinase inhibitor R 59022 did not change glucose-stimulated insulin secretion but abolished the inhibition seen in the presence of RHC 80267. RHC 80267 increased islet glucose utilisation, measured as formation of tritiated water from 5-[3H]-glucose, 3-fold but did not affect glucose oxidation to CO2, lactate production or islet ATP levels. Glucose utilisation in leucocytes and hepatocytes was not increased by addition of RHC 80267. Islet lipid production from glucose was augmented 4-fold in the presence of RHC 80267 but only accounted for about 5% of the increase in glucose utilisation. The activity of adenylate cyclase and phosphoinositide-specific phospholipase C was unaffected by RHC 80267. Concentrations of RHC 80267 below 35 μmol/l did not alter the activity of phospholipase A2; whereas higher concentrations of the drug inhibited phospholipase A2 activity approx 25%. The data support the hypothesis that production of arachidonic acid from diacylglycerol may be involved in regulation of insulin secretion.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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