Studies of in vivo phosphorylated proteins in BC3H‐1 myocytes suggest that protein kinase C is involved in insulin action

FEBS Letters

Farese, Robert V.¹  Davis, John S.¹  Vila, María del C.¹  Cooper, Denise R.¹  Standaert, Mary L.¹ 

[1] Veterans Administration Hospital and Departments of Internal Medicine and Biochemistry, University of South Florida, College of Medicine, Tampa, FL 33612, USA

关键词: Insulin;    Phorbol ester;    Protein phosphorylation;    Protein kinase C;    Myocyte;    Diacylglycerol;    Phospholipid;    TPA;    12-O-tetradecanoyl phorbol-13-acetate;    PMSF;    phenylmethylsulfonyl fluoride;    PS;    phosphatidylserine;    PKC;    protein kinase C;    DMSO;    dimethyl sulfoxide;   

DOI  :  10.1016/0014-5793(89)81187-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Insulin (10 and 100 nM) and phorbol esters increased the phosphorylation of several proteins, including 40, 47 and 80 kDa proteins, which are markers for protein kinase C activation. Insulin effects were evident at 2 min and increased over 20 min. These findings suggest that insulin activates protein kinase C in BC3H-1 myocytes.

【 授权许可】

Unknown