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PMID |
Sentence |
1 |
1312492
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To study the role of membrane lipids in signal transduction by the insulin receptor, we have studied the effect of phospholipase C (Clostridium perfringens) and a phosphatidylinositol-specific phospholipase (Staphylococcus aureus) on insulin binding, a function of the alpha-subunit, and tyrosine kinase activity, a function of the beta-subunit in IM-9 lymphocytes and NIH 3T3 fibroblasts transfected with the human insulin receptor.
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2 |
1312492
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Treatment of the cells with phospholipase C at concentrations up to 3.4 U/ml did not affect specific insulin binding, but reduced insulin-stimulated receptor phosphorylation by 50%.
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3 |
1312492
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Insulin-stimulated phosphorylation of pp 185, the presumed endogenous substrate for the insulin receptor kinase, was also reduced following phospholipase C treatment, with an almost complete loss of insulin stimulation after exposure of cells to enzyme at concentrations as low as 0.6 U/ml.
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4 |
1312492
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In contrast to these effects of phospholipase C on intact cells, receptor autophosphorylation was not affected in insulin receptors purified on wheat germ agglutinin-agarose from phospholipase C treated cells.
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5 |
1312492
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Treatment of cells with the phosphatidylinositol-specific phospholipase C did not affect any of the parameters studied.
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6 |
1848407
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Diabetes reduces heparin- and phospholipase C-releasable lipoprotein lipase from cardiomyocytes.
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7 |
1848407
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Incubation of isolated cardiac myocytes from rat hearts with heparin or phosphatidylinositol-specific phospholipase C (PLC) resulted in the release of lipoprotein lipase (LPL) into the medium.
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8 |
1848407
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The release of LPL by the combination of heparin and PLC was not additive, and preincubation of cardiac myocytes with heparin eliminated the release of LPL in a subsequent incubation with PLC.
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9 |
1848407
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This evidence suggests that LPL may be bound ionically to heparan sulfate proteoglycans that are covalently linked to the cell surface of cardiac myocytes by a phosphatidylinositol-glycan membrane anchor; a second pool of LPL may also be bound to proteoglycans attached directly to the myocardial cell surface.
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10 |
1848407
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The intravenous administration of insulin (5 U for 1 h) in diabetic rats reversed the effects of diabetes on cellular and heparin-releasable LPL activities.
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11 |
1848407
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Diabetes also reduced the PLC-induced release of LPL.
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12 |
2173562
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Isolation of insulin-sensitive phosphatidylinositol-glycan from rat adipocytes.
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13 |
2173562
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A material that activated pyruvate dehydrogenase was extracted from rat adipocyte membrane supernatants.
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14 |
2173562
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Its release was stimulated by insulin and phosphatidylinositol-specific-phospholipase C and its activity was destroyed by nitrous acid deamination.
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15 |
2173562
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Digestion of the purified molecule with phosphatidylinositol-specific phospholipase C generated a material that activated both pyruvate dehydrogenase and low-Km cyclic AMP phosphodiesterase.
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16 |
2173562
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Impairment in insulin-stimulated breakdown of the molecule in adipocytes of streptozotocin-diabetic rats was found, consistent with the impaired insulin activation of pyruvate dehydrogenase and glucose utilization seen in this model.
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17 |
2173562
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Isolation of insulin-sensitive phosphatidylinositol-glycan from rat adipocytes.
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18 |
2173562
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A material that activated pyruvate dehydrogenase was extracted from rat adipocyte membrane supernatants.
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19 |
2173562
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Its release was stimulated by insulin and phosphatidylinositol-specific-phospholipase C and its activity was destroyed by nitrous acid deamination.
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20 |
2173562
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Digestion of the purified molecule with phosphatidylinositol-specific phospholipase C generated a material that activated both pyruvate dehydrogenase and low-Km cyclic AMP phosphodiesterase.
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21 |
2173562
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Impairment in insulin-stimulated breakdown of the molecule in adipocytes of streptozotocin-diabetic rats was found, consistent with the impaired insulin activation of pyruvate dehydrogenase and glucose utilization seen in this model.
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22 |
2257956
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In in vitro experimental systems, ALPase was readily released from the duodenal plasma membrane by bacterial phosphatidylinositol-specific-phospholipase C (PI-PLase C) but little if any was released from the ileal membrane. 4.
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23 |
8144525
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Cells transformed with the RT6.2 gene expressed NAD glycohydrolase activity that was released from intact cells by phosphatidylinositol-specific phospholipase C, consistent with its presence on the cell surface.
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24 |
8144525
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The molecular weight of the phosphatidylinositol-specific phospholipase C-released NAD glycohydrolase, determined by SDS-polyacrylamide gel electrophoresis, was 22,000-24,000, in good agreement with that of native RT6.2.
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25 |
8144525
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Cells transformed with the RT6.2 gene expressed NAD glycohydrolase activity that was released from intact cells by phosphatidylinositol-specific phospholipase C, consistent with its presence on the cell surface.
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26 |
8144525
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The molecular weight of the phosphatidylinositol-specific phospholipase C-released NAD glycohydrolase, determined by SDS-polyacrylamide gel electrophoresis, was 22,000-24,000, in good agreement with that of native RT6.2.
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27 |
8349037
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Glycosyl phosphatidylinositol molecules from fetal and adult cells were sensitive to hydrolysis by a phosphatidylinositol-specific phospholipase C from B. cereus.
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28 |
8349037
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However, in fetal hepatocytes insulin failed to reduce the glycosyl-phosphatidylinositol content when labeled either with [1-14C]isethionyl acetimidate or [3H]glucosamine, whereas insulin-like growth factor I produced a significant hydrolysis of glycosyl phosphatidylinositol.
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29 |
8349037
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Fetal and adult hepatocytes were incubated with insulin or inositol phosphoglycan after which glycogen phosphorylase activities were determined.
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30 |
8349037
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Inositol phosphoglycan mimicked the action of insulin on both forms of the enzyme from adult hepatocytes, whereas in fetal cells insulin did not change, and purified inositol phosphoglycan reduced the activities of glycogen phosphorylase.
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31 |
8390376
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Insulin stimulates hydrolysis of plasmanylinositol-glycan and phosphatidylinositol-glycan in rat adipocytes.
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32 |
8390376
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Insulin binding to its receptor has been known to induce hydrolysis of phosphatidylinositol-glycan and release inositol-glycan and diacylglycerol, two putative second messengers of insulin actions.
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33 |
8390376
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The treatment of [3H]glycerol-labeled PIG with phosphatidylinositol-specific phospholipase C released [3H]glycerol-labeled DAG and [3H]glycerol-labeled 1-alkyl,2-acyl-glycerol, suggesting that PIG has not only PIG but also plasmanylinositol-glycan moiety.
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34 |
8390376
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Insulin induced hydrolysis of PIG/PMIG and generation of IG, DAG, and AAG in a dose-dependent manner.
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35 |
8390376
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These results provide evidence that insulin-induced generation of IG, DAG, and AAG might be early events in the insulin-signaling mechanism in rat adipocytes, and insulin-releasable AAG seems to mediate some actions of insulin.
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36 |
8529504
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The studies on the molecular mechanism of extrapancreatic activity with rat adipocytes and diaphragm suggest that these direct insulin-mimetic effects rely on the induction of GLUT4 translocation from internal stores to the plasma membrane and on the activation of the key metabolic enzymes, glycogen synthase and glycerol-3-phosphate acyltransferase.
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37 |
8529504
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The direct effects of sulfonylureas may ultimately be regulated by a glycosyl-phosphatidylinositol-specific phospholipase C, shown to be activated by glimepiride in rat adipocytes.
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38 |
8650189
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Supernatant CD4-GPI also attached to human red blood cells and could be cleaved with phosphatidylinositol-specific phospholipase C.
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39 |
11139580
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Depolarization-induced [Ca(2+)](i) response was not altered by, an inhibitor of phosphatidylinositol-specific phospholipase C, suggesting that stimulation of the enzyme by Ca(2+) is not essential for amplification of Ca(2+) signaling.
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40 |
11489987
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Treatment of T cells with phosphatidylinositol-specific phospholipase C removed much of the NADase activity, consistent with at least one NADase having a GPI anchor; ART2- T cell subsets contained NADase activity that was not releasable by phosphatidylinositol-specific phospholipase C treatment.
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41 |
23826075
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Mll2 has been shown to regulate a small subset of genes, a number of which Neurod1, Enpp1, Slc27a2, and Plcxd1 are downregulated in adult mutant mice.
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