Phosphorylation of a 16‐kDa protein by diacylglycerol‐activated protein kinase C in vitro and by vasopressin in intact hepatocytes

FEBS Letters

Cooper, Ronald H.¹  Kobayashi, Koichi¹  Williamson, John R.¹ 

[1] Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA

关键词: Protein phosphorylation;    Diacylglycerol-activated protein kinase C;    Vasopressin;    Hepatocyte;    Hormone action;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(84)80057-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A 16-kDa protein present in a purified rat liver plasma membrane fraction and also in cytosol can be phosphorylated by endogenous diacylglycerol-activated protein kinase C. In intact hepatocytes prelabeled with ³²P, vasopressin causes a rapid increase in the phosphorylation of a 16-kDa protein having a similar pI value to that observed in in vitro studies. These findings suggest that vasopressin-induced phosphorylation of the 16-kDa in the intact hepatocyte may reflect increased activity of protein kinase C, secondary to membrane polyphosphoinositide breakdown. Phosphorylation of the 16-kDa protein may thus be part of the coordinated mechanism associated with hormonal regulation of cellular Ca²⁺ fluxes.

【 授权许可】

Unknown