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Staurosporine stimulates phospholipase D activation in human polymorphonuclear leukocytes
Author(s) -
Périanin Axel,
Combadière Christophe,
Pedruzzi Eric,
Djerdjouri Bahia,
Hakim Jacques
Publication year - 1993
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(93)81127-l
Subject(s) - staurosporine , phosphatidylethanol , phospholipase d , phosphatidic acid , protein kinase c , chemistry , biochemistry , phospholipase , enzyme , phospholipid , membrane
Treatment of 1‐ O ‐[ 3 H]alkyl‐2‐acyl‐phosphatidylcholine‐prelabeled human polymorphonuclear leukocytes (PMNs) with Staurosporine (50 nM to 1 μM) induced a time‐ and concentration‐dependent generation of tritiated phosphatidic acid (PA), reaching approximately 225% of the control value at 15–20 min. In the presence of ethanol, Staurosporine induced a production of phosphatidylethanol (PEt) reaching, 250% of control values, and partial inhibition of PA production, consistent with PLD activation. The amount of ether‐linked acylglycerol (EAG) was weakly enhanced (29%) after 5 min of PMN treatment; longer treatment resulted in no significant EAG production, suggesting a possible late inhibition of PA hydrolase activity. Staurosporine concentrations that induced an elevation in PA completely depressed protein kinase C (PKC) activity in both soluble and particulate cell fractions, suggesting that PLD activation may occur independently from PKC activation. PLD may thus represent a potential cellular target for Staurosporine action.