Phorbol ester and 1,2‐diolein are not fully equivalent activators of protein kinase C in respect to phosphorylation of membrane proteins in vitro

FEBS Letters

Luo, Yuan¹  Kiss, Zoltan¹ 

[1]Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Odesszai krt 62, 6701 Szeged, Hungary

关键词: 12-O-Tetradecanoylphorbol 13-acetate;    1;    2-Diolein;    Protein kinase C;    PS;    phosphatidylserine;    TPA;    12-O-tetradecanoylphorbol 13-acetate;    1;    2-DG;    1;    2-diacylglycerol;   

DOI  :  10.1016/0014-5793(86)80405-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphorylation of liver plasma membrane proteins by protein kinase C was studied by using the two best known activators of the enzyme, 12-O-tetradecanoylphorbol-13-acetate (TPA) and 1,2-diolein. While the effects of TPA and diolein were almost identical on two proteins and similar in magnitude on four proteins, the phosphorylation of an additional four proteins was increased only by TPA. We conclude that in respect to phosphorylation of membrane proteins, TPA and diglycerides are not fully equivalent activators of kinase C.

【 授权许可】

Unknown