The effect of platelet surface protein phosphorylation on collagen-platelet interaction.
Phosphorylation of the surface proteins of human platelets by treatment with human plasma kinase and exogenous ATP enhances their aggregation response to collagen. This effect can be reversed by treatment of the phosphorylated platelets with acid phosphatase. Moreover, acid phosphatase treatment of normal human platelets results in a decreased aggregation response to collagen. The increased responsiveness of phosphorylated platelets to collagen is associated with a concomitant increase in Thromboxane A2 formation. These results suggest that the platelet surface protein phosphorylation/dephosphorylation plays an important role in modulating platelet function.
D000135:Acid Phosphatase / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D001792:Blood Platelets / Q000187:drug effects* / Q000378:metabolism; D003094:Collagen / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D008565:Membrane Proteins / Q000097:blood*; D010766:Phosphorylation; D010974:Platelet Aggregation / Q000187:drug effects*; D011494:Protein Kinases / Q000097:blood; D013929:Thromboxane B2 / Q000378:metabolism
D008565:Membrane Proteins; D013929:Thromboxane B2; D000255:Adenosine Triphosphate; D003094:Collagen; D011494:Protein Kinases; D000135:Acid Phosphatase