Cooperative interactions of protein kinase C and cAMP‐dependent protein kinase systems in human promyelocytic leukemia HL60 cells

FEBS Letters

Kuo, J.F.¹  Deli, Eva¹  Kiss, Zoltan¹ 

[1] Department of Pharmacology, Emory University School of Medicine, Atlanta, GA 30322, USA

关键词: 12-O-Tetradecanoylphorbol-13-acetate;    cAMP;    Differentiation;    Protein kinase C;    PKC;    protein kinase C;    PKA;    cAMP-dependent protein kinase;    TPA;    12-O-tetradecanoylphorbol-13-acetate;    dbcAMP;    dibutyryl cAMP;    PGE2;    prostaglandin E2;   

DOI  :  10.1016/0014-5793(88)80860-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Interactions of protein kinase C (PKC) and cAMP-dependent protein kinase (PKA) systems were investigated in HL60 cells. It was found that the differentiating effects of 12-O-tetradecanoylphorbol-13-acetate (TPA) were potentiated by dibutyryl cAMP (dbcAMP) or prostaglandin E₂ (PGE₂). In addition, dbcAMP or PGE₂ inhibited TPA-induced binding of PKC to plasma membrane, leading to decreased protein phosphorylation, and promoted subsequent redistribution of enzyme to the nuclear membrane region. The findings are consistent with the hypothesis that PKC and PKA systems regulate cooperatively the phenotypical differentiation of leukemic cells.

【 授权许可】

Unknown