PMID: 2105213Jan 12, 1990Paper

Primary stimuli of icosanoid release inhibit arachidonoyl-CoA synthetase and lysophospholipid acyltransferase. Mechanism of action of hydrogen peroxide and methyl mercury in platelets

European Journal of Biochemistry
W Hornberger, H Patscheke

Abstract

Icosanoid formation in platelets depends on the concentration of free arachidonate that is mainly liberated from membrane phospholipids by phospholipase A2. The concentration of free arachidonate is also controlled by the activities of the reacylating enzymes arachidonoyl-CoA synthetase and lysophospholipid acyltransferase. In human platelet microsomes we determined the high enzyme activities of 5.9 nmol.min-1.(10(9) platelets)-1 for the arachidonoyl-CoA synthetase and 37 nmol.min-1.(10(9) platelets)-1 for the lysophospholipid acyltransferase. The activities of these reacylating enzymes were strongly reduced by hydrogen peroxide (H2O2) and methyl mercury that are primary stimuli of arachidonate release in intact platelets. H2O2 inhibited the arachidonoyl-CoA synthetase with an IC50 of 3.3 mmol/l without affecting the lysophospholipid acyltransferase. Sulfhydryl group protection by 3-mercapto-1,2-propanediol did not overcome the inhibition but glutathione prevented the inhibition of the arachidonoyl-CoA synthetase by H2O2. This suggests that glutathione by virtue of the glutathione peroxidase reduces H2O2 rather than that it protects free sulfhydryl groups of the arachidonoyl-CoA synthetase. Methyl mercury left the arachidonoyl-...Continue Reading

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Citations

Oct 20, 1998·Prostaglandins & Other Lipid Mediators·M M Mahfouz, F A Kummerow
Jan 1, 1997·Free Radical Biology & Medicine·L IulianoF Violi
Mar 13, 1999·Biochemical Pharmacology·G Leoncini, M G Signorello
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Aug 15, 1991·Archives of Biochemistry and Biophysics·L IulianoF Violi
Aug 1, 1995·Arteriosclerosis, Thrombosis, and Vascular Biology·A WeidtmannW Siess

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