Epoprostenol (prostacyclin, PGI2) binding and activation of adenylate cyclase in platelets of diabetic and control subjects.
1 The binding of epoprostenol (prostacyclin, PGI2) to isolated fractured human platelets has been studied using tritiated PGI2. 2 High and low affinity binding sites for PGI2 have been identified (Kd values = 16 and 382 nM). 3 Analysis of the prostacyclin-dependent activation of adenylate cyclase suggests that enzyme activation is mediated by the high affinity binding site. 4 Platelet PGI2 receptor binding and adenylate cyclase activation by PGI2 are unchanged in diabetic and normal human platelets. 5 This work suggests that hyperaggregability of diabetic platelets is not due to any alteration of platelet prostacyclin receptor numbers or their activation.
D000262:Adenylyl Cyclases / Q000097:blood*; D000293:Adolescent; D000328:Adult; D001792:Blood Platelets / Q000378:metabolism*; D003920:Diabetes Mellitus / Q000097:blood*; D003930:Diabetic Retinopathy / Q000097:blood; D004789:Enzyme Activation; D011464:Epoprostenol / Q000097:blood*; D006801:Humans; D008297:Male; D010974:Platelet Aggregation; D011453:Prostaglandins / Q000097:blood*
D011453:Prostaglandins; D011464:Epoprostenol; D000262:Adenylyl Cyclases