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Phospholipase D is involved in cytosolic phospholipase A 2 ‐dependent selective release of arachidonic acid by fMLP‐stimulated rat neutrophils
Author(s) -
Fujita Ken-ichi,
Murakami Makoto,
Yamashita Fumio,
Amemiya Kouji,
Kudo Ichiro
Publication year - 1996
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(96)01056-3
Subject(s) - arachidonic acid , phosphatidic acid , phospholipase a2 , phospholipase d , diacylglycerol lipase , phospholipase , chemistry , diacylglycerol kinase , biochemistry , phosphatidate , cytosol , phospholipase c , enzyme , protein kinase c , phospholipid , membrane
When rat polymorphonuclear neutrophils (PMN) were treated with N ‐formyl‐Met‐Leu‐Phe (fMLP), the release of arachidonic acid in preference to other fatty acids was observed. Levels of arachidonic acid reached a plateau within 5 min, and were accompanied by an ∼ 4‐fold increase in in vitro phospholipase (PL) A 2 and PLD activities in PMN lysates. Treatment of PMN with ethanol (an inhibitor of PLD‐mediated phosphatidic acid formation), propranolol (a phosphatidic acid phosphatase inhibitor), or 4‐bromophenacylbromide (a PLA 2 inhibitor), each suppressed fMLP‐stimulated arachidonate release. Treatment with RHC‐80267 (a diacylglycerol lipase inhibitor), however, had no such effect. The cytosolic PLA 2 (cPLA 2 ) inhibitor, arachidonoyl trifluoromethyl ketone, suppressed PLA 2 activity in PMN homogenates and arachidonate release by fMLP‐treated PMN. These results suggest that fMLP‐elicited arachidonate release is mediated by cPLA 2 but not diacylglycerol lipase, and that the activation of cPLA 2 is downstream of the PLD‐dependent signaling pathway.