Role of A alpha chain of fibrinogen in coagulation and platelet interaction investigated with a monoclonal antibody.
A murine monoclonal antibody (anti-C2G7), reactive with fibrinogen, was used to analyse the structure and function of the fibrinogen epitope C2G7. Anti-C2G7 was found to be reactive with fibrinogen but not with fibronectin, Factor VIII-von Willebrand Factor (FVIII-vWF), beta-thromboglobulin (beta TG), platelet factor 4 (PF4) nor with a range of normal cells and cell lines. Biochemical and plasmin digestion studies of fibrinogen revealed that C2G7 is present on the carboxy-terminal end of the alpha chain on a fragment with a Mr approximately 30-40 K. Functional studies, on the role of fibrinogen in coagulation and platelet function, demonstrated the importance of C2G7 (or a closely associated region) for thrombin-associated fibrin polymerization and collagen induced fibrinogen binding to platelets.
Thurlow
P J
PJ
Department of Haematology, Austin Hospital, Heidelberg, Victoria, Australia.
Connellan
J M
JM
Kenneally
D A
DA
D000818:Animals; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D001777:Blood Coagulation; D001792:Blood Platelets / Q000378:metabolism / Q000502:physiology*; D055598:Chemical Phenomena; D002621:Chemistry; D005337:Fibrin / Q000096:biosynthesis; D005340:Fibrinogen / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D007158:Immunologic Techniques; D051379:Mice; D011863:Radioimmunoassay; D013917:Thrombin / Q000502:physiology
D000911:Antibodies, Monoclonal; D005337:Fibrin; D005340:Fibrinogen; D013917:Thrombin