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Enhanced prothrombin‐converting activity and factor Xa binding of platelets activated by the alternative complement pathway
Author(s) -
Ö ZgeAnwar Ayşle H.,
Freedman John J.,
Senyi Andrew F.,
Cerskus Andrew L.,
Blajchman Morris A.
Publication year - 1984
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1984.tb02890.x
Subject(s) - platelet , zymosan , chemistry , thrombin , platelet activation , platelet factor 4 , platelet rich plasma , prothrombinase , alternative complement pathway , factor vii , opsonin , complement system , biochemistry , coagulation , immunology , medicine , antibody , biology , in vitro
S ummary. 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.