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A phospholipase A 2 hydrolyzing arachidonoyl‐phospholipids in mouse peritonea macrophages
Author(s) -
Wijkander Jonny,
Sundler Roger
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81160-3
Subject(s) - arachidonic acid , phosphatidylinositol , nordihydroguaiaretic acid , biochemistry , phosphatidylcholine , phospholipase a2 , chemistry , phospholipase c , phospholipase a , phospholipase , cytosol , phorbol , enzyme , ethanolamine , phospholipid , microbiology and biotechnology , protein kinase c , biology , membrane , kinase
A calcium‐dependent phospholipase A 2 with half‐maximal activity at approx. 0.7 μM free Ca 2+ 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.