Literature DB >> 8031124

Insulin-like effects of sodium orthovanadate on diacylglycerol-protein kinase C signaling in BC3H-1 myocytes.

K Yamada1, M L Standaert, B Yu, H Mischak, D R Cooper, R V Farese.   

Abstract

In this paper we examine whether sodium orthovanadate activates diacylglycerol (DAG)/protein kinase C (PKC) signaling systems that are activated by insulin in BC3H-1 myocytes. Like insulin, sodium orthovanadate provoked increases in membrane DAG, PKC enzyme activity, and immunoreactive PKC-beta. Concomitantly, both PKC enzyme activity and immunoreactive PKC-beta decreased in the cytosol, suggesting that sodium orthovanadate, like insulin, stimulated the translocation of PKC-beta from the cytosol to the membrane fraction. Sodium orthovanadate was also found to activate phospholipid signaling pathways that were previously reported to be activated by insulin, viz., inositol-lipid synthesis/turnover; phosphatidylcholine hydrolysis; and de novo phospholipid synthesis by activation of glycerol-3-PO4 acyltransferase. Our findings suggest that vanadate mimics insulin in the activation of specific phospholipid/DAG/PKC signaling pathways.

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Year:  1994        PMID: 8031124     DOI: 10.1006/abbi.1994.1295

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  2 in total

1.  Effects of insulin on the translocation of protein kinase C-theta and other protein kinase C isoforms in rat skeletal muscles.

Authors:  K Yamada; A Avignon; M L Standaert; D R Cooper; B Spencer; R V Farese
Journal:  Biochem J       Date:  1995-05-15       Impact factor: 3.857

Review 2.  Glycerol-3-phosphate acyltransferases: rate limiting enzymes of triacylglycerol biosynthesis.

Authors:  Angela A Wendel; Tal M Lewin; Rosalind A Coleman
Journal:  Biochim Biophys Acta       Date:  2008-11-07
  2 in total

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