A phospholipase A2 hydrolyzing arachidonoyl‐phospholipids in mouse peritonea macrophages

FEBS Letters

Wijkander, Jonny¹  Sundler, Roger¹ 

[1] Department of Physiological Chemistry, University of Lund, PO Box 94, S-221 00 Lund, Sweden

关键词: Phospholipase A2;    Arachidonic acid;    Phorbol myristate acetate;    Quercetin;    Nordihydroguaiaretic acid;    (Mouse macrophage);    PMA;    4-β-phorbol 12-myristate 13-acetate;    PLA2;    phospholipase A2;   

DOI  :  10.1016/0014-5793(89)81160-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A calcium-dependent phospholipase A₂ with half-maximal activity at approx. 0.7 μM free Ca²⁺ has been identified in the cytosolic fraction from macrophages. The enzyme eluted as a 70 kDA protein upon gel chromatography and showed increased activity after 10 min pretreatment of the cells with 10 nM phorbol myristate acetate. No significant activity could be detected in the membrane fraction. The enzyme hydrolyzed arachidonic acid-containing phosphatidylcholine and -ethanolamine as well as phosphatidylinositol. The release of arachidonic acid in the vitro assay was inhibited in a dose-dependent manner by nordihydroguaiaretic acid and quercetin that are also potent inhibitors of the mobilization of arachidonic acid in intact macrophages.

【 授权许可】

Unknown