Abstract
The role of superoxide dismutase (SOD) on human platelet was investigated by utilizing diethyldithiocarbamate (DDC); chelator of copper ion and inhibitor of SOD. DDC inhibited the activity of platelet SOD in a does dependent manner after two hrs incubation at 37°C. Since cytochrome oxydase was not inhibited at low concentrations of the drug, SOD might be inhibited specifically among copper containing enzymes. The platelet aggregations induced by ADP, collagen or arachidonic acid were enhanced at low concentrations of DDC. The N-ethylmaleimide or thrombin-induced MDA production was also enhanced at low concentrations of the drug. These results suggest that SOD plays a stimulatory role on platelet function by affecting the prostaglandin synthesis.
