Evidence for glutathione-S-transferase activity in human blood platelets.
Data will be presented pointing to the presence of glutathione-S-transferase activity in human blood platelets and the possible involvement of this enzyme in the process of platelet activation. Using 1-chloro-2,4-dinitrobenzene as a synthetic substrate of the glutathione-S-transferase a rapid dose-dependent depletion of platelet glutathione was measured. The formed GSH-CDNB conjugate was separated by thin-layer chromatography. Hints to the formation of leukotriene-like substances by glutathione-S-transferase catalysed reaction were obtained using the specific leukotriene C antagonist FPL 55 712 in aggregation studies.
D016718:Arachidonic Acid; D001095:Arachidonic Acids / Q000037:antagonists & inhibitors; D001792:Blood Platelets / Q000201:enzymology*; D002867:Chromones / Q000494:pharmacology; D004137:Dinitrochlorobenzene / Q000097:blood; D005982:Glutathione Transferase / Q000097:blood*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D010974:Platelet Aggregation / Q000187:drug effects; D013189:SRS-A / Q000037:antagonists & inhibitors
D001095:Arachidonic Acids; D002867:Chromones; D004137:Dinitrochlorobenzene; D013189:SRS-A; D016718:Arachidonic Acid; C006312:FPL 55712; D005982:Glutathione Transferase