Calcium‐activated, phospholipid‐dependent protein kinase activity and protein phosphorylation in HL60 cells induced to differentiate by retinoic acid

FEBS Letters

Butcher, Fred R.¹  Emler, Carol A.¹  Fontana, Joseph A.¹  Durham, John P.¹ 

[1] Departments of Biochemistry, West Virginia University, Morgantown, WV 26506, USA

关键词: Protein kinase;    Leukemia;    Differentiation;    Retinoic acid;    Ca2+;    PL protein kinase;    calciumactivated phospholipid-dependent protein kinase;    TPA;    12-O-tetradecanoyl phorbol-13-acetate;    RA;    retinoic acid;    NSE;    non-specific esterase;   

DOI  :  10.1016/0014-5793(85)80761-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Treatment of human promyelocytic (HL60) cells with retinoic acid for at least 48 h causes differentiation to more mature myeloid forms. Prior to commitment of cells to the myeloid pathway there is a marked increase in cytosolic calcium-activated, phospholipid-dependent protein kinase activity. This increase does not result from an intracellular redistribution of the enzyme. Concomitant with the increased enzyme activity there is enhanced phospholipid-dependent phosphorylation of proteins of 29, 49, 52, 58, 68, 69, 120, 170, 200 and 245 kDa.

【 授权许可】

Unknown