Protein kinase C negatively modulated by phorbol ester

FEBS Letters

Hagiwara, Masatoshi¹  Hidaka, Hiroyoshi¹  Saitoh, Masahiro¹  Inagaki, Masaki¹ 

[1] Department of Pharmacology, Mie University School of Medicine, Edobashi, Tsu, Mie 514, Japan

关键词: Protein kinase C;    Phorbol ester;    Enzyme inhibitor;    Negative modulation;    Nucleotide-binding site;   

DOI  :  10.1016/0014-5793(86)80701-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Pretreatment of protein kinase C with 12-O-tetradecanoylphorbol-13-acetate (TPA) and phospholipid resulted in complete inhibition of ATP/phosphotransferase activity, irreversibly. The inactivation by TPA required the phospholipid, and TPA alone did not cause inactivation. Ca²⁺ and diacylglycerol mimicked TPA. This action of TPA was not general for all protein kinases as it did not accelerate the inactivation of the catalytic subunit of cAMP-dependent protein kinase by phospholipid. The addition of MgATP to the reaction mixture completely protected protein kinase C from being inactivated by TPA, in the presence of phospholipid. The nucleotide-binding site of the enzyme was probably influenced by the binding of TPA and phospholipid.

【 授权许可】

Unknown