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A series of functional parameters, including the aggregability triggered by various agents, the in vitro malondialdehyde production and the glutathio ne peroxidase activity, has been investigated in platelets from normal blood donors.  Glutathione peroxidase activity assays showed a significant inverse correlation with malondialdehyde induced by arachidonic acid but not with aggregation data and malondialdehyde induced by thrombin. Moreover, arachidonic acid generates in human platelets lysates large amounts of hydrogen acceptor substrate(s) for the glutathione peroxidase with peculiar kinetic features. These are related to ma londialdehyde production and to partial inhibition by acetyl-salicilic acid and are likely connected with prostaglandin metabolism.  Our data suggest that physiological variations in glutathione peroxidase activity are important in human platelet arachidonic acid metabolism, because they modulate the biosynthesis of key end-products, as thromboxane A2, whose malondialdehyde is an inde.

Glutathione Peroxidase And Malondialdehyde Production In The Arachidonic Acid Metabolism Of Human Platelets