The protein phosphatase inhibitor, okadaic acid, potentiates the stimulatory effect of phorbol ester on phosphatidylcholine synthesis, but not on phospholipid hydrolysis, in fibroblasts

FEBS Letters

Kiss, Zoltan¹ 

[1] The Hormel Institute, University of Minnesota, Austin, MN, USA

关键词: Okadaic acid;    Phorbol ester;    Phosphatidylcholine synthesis;    PtdCho;    phosphatidylcholine;    PMA;    phorbol 12-myristate 13-acetate;    PLC;    phospholipase D;    PKC;    protein kinase c;    1;    2-DAG;    1;    2-diacylglycerol;    DMEM;    Dulbeccos modified Eagle's medium;   

DOI  :  10.1016/0014-5793(92)81295-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The potent protein phosphatase inhibitor, okadaic acid, was used to determine the possible role of protein phosphorylation reaction(s) in phorbol ester-induced synthesis and hydrolysis of phosphatidylcholine (PtdCho) in NIH 3T3 fibroblasts. Okadaic acid (2μM) was found to enhance the stimulatory effects of lower concentrations (2.5–25 nM) of phorbol 12-myristate 13-acetate (PMA) on PtdCho synthesis, but not an PtdCho hydrolysis, after treatments for 30–60 min. These data support a view that in fibroblasts PMA simulates only PtdCho synthesis, and not PtdCho hydrolysis, by a protein phosphorylation-dependent mechanism.

【 授权许可】

Unknown