Susceptibility of protein kinase C to oxidative inactivation: Loss of both phosphotransferase activity and phorbol diester binding

FEBS Letters

Gopalakrishna, Rayudu¹  Anderson, Wayne B.² 

[1] Department of Pathology, School of Medicine, University of California at Los Angeles, Los Angeles, CA 90024, USA;Division of Cancer Biology and Diagnosis, National Cancer Institute, Bethesda, MD 20892, USA

关键词: Protein kinase C;    Oxidative inactivation;    Oxygen radical;    Phorbol ester;    Membrane binding;    PDBu;    phorbol 12;    13-dibutyrate;    TPA;    12-O-tetradecanoylphorbol-13-acetate;    PYS;    parietal yolk sac;   

DOI  :  10.1016/0014-5793(87)81164-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Exposure of protein kinase C to low concentrations of either N-chlorosuccinimide or H₂O₂ resulted in rapid and parallel loss of phosphotransferase activity and phorbol ester binding. This oxidative inactivation of protein kinase C also occurred in intact cells exposed to a low concentration of H₂O₂. With H₂O₂ treatment the rate of inactivation of protein kinase C in the cytosol of MCF-7 cells was rather slower than that which occurred in the cytosol of PYS cells. However, in both cell types, the oxidative inactivation of membrane-associated protein kinase C occurred rapidly in comparison to the enzyme in the cytosol. Prior treatment of cells with phorbol ester to induce membrane association (stabilization) of protein kinase C, followed by exposure to H₂O₂, resulted in increased inactivation of protein kinase C, suggesting that membrane association of protein kinase C increases its susceptibility to oxidative inactivation

【 授权许可】

Unknown