Enhanced prothrombin-converting activity and factor Xa binding of platelets activated by the alternative complement pathway.
Platelet prothrombin-converting activity and factor Xa binding were studied after exposure of human platelet rich plasma (PRP) to various conditions leading to platelet activation. Zymosan resulted in increased platelet-bound C3, enhanced prothrombin-converting activity and increased factor Xa binding. Similar findings were observed with normal platelets resuspended in factor XII-deficient plasma. The combined use of zymosan and thrombin to activate platelets resulted in synergistic prothrombin-converting activity and factor Xa binding. In contrast, no synergism was obtained with the concomitant use of zymosan and collagen, suggesting that collagen and zymosan share the same pathway for platelet activation. Heterologous antibody to factor V completely inhibited the platelet prothrombin-converting activity for all modes of platelet activation, indicating that this activity is mediated by factor V.
D001792:Blood Platelets / Q000187:drug effects* / Q000276:immunology; D003094:Collagen / Q000494:pharmacology; D003176:Complement C3 / Q000032:analysis; D015933:Complement C3d; D003170:Complement Pathway, Alternative; D005170:Factor X / Q000378:metabolism*; D015951:Factor Xa; D006801:Humans; D007700:Kinetics; D011516:Prothrombin / Q000378:metabolism*; D013917:Thrombin / Q000494:pharmacology; D015054:Zymosan / Q000494:pharmacology*
D003176:Complement C3; D015933:Complement C3d; D011516:Prothrombin; D005170:Factor X; D003094:Collagen; D015054:Zymosan; D013917:Thrombin; D015951:Factor Xa