Regulation of arachidonate‐mobilizing phospholipase A2 by phosphorylation via protein kinase C in macrophages

FEBS Letters

Wijkander, Jonny¹  Sundler, Roger¹ 

[1] Department of Medical and Physiological Chemistry, Lund University, Lund, Sweden

关键词: Arachidonic acid;    Phospholipase A2 (intracellular);    Protein phosphorylation;    Protein kinase C;    PLA2-85;    85 kDa phospholipase A2;    PKC;    protein kinase C;    PMA;    4β-phorbol 12-myristate 13-acetate;   

DOI  :  10.1016/0014-5793(92)81124-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Stimulation of ³²P-labeled macrophages with phorbol ester caused an increase in phosphorylation of the intracellular, high molecular weight phospholipase A₂. This increase in phosphorylation was accompanied by an increase in enzyme activity, but led to no detectable shift in the concentration dependence for Ca²⁺-induced activation. The phosphorylated phospholipase A₂ could be dephosphorylated by treatment with acid phosphatase, and such treatment also reduced its catalytic activity. Together with previous data, these results indicate that the arachidonate-mobilizing phospholipase A₂ is dually regulated by Ca^2'+ (membrane interaction) and by phosphorylation (catalytic activity).

【 授权许可】

Unknown