The effect of fibrin polymers on thrombin-catalyzed plasma factor XIIIa formation.
The effect of fibrin polymers on thrombin-catalyzed factor XIIIa formation was studied in afibrinogenemic plasma. Fibrin polymers derived from des A fibrinogen and des A,B fibrinogen increased sixfold the rate of thrombin-catalyzed factor XIIIa formation in the presence of EDTA. Calcium chloride accelerated factor XIIIa formation 14-fold in the presence of des A,B fibrinogen without increasing the rate of thrombin formation. Fibrinopeptides A and B had no effect on factor XIIIa formation in afibrinogenemic plasma. Des A,B fibrinogen reduced by 20- to 40-fold the thrombin concentration required to activate factor XIII. Glycyl-L-prolyl-L-arginyl-L-proline (gly-pro-arg-pro), a fibrin polymerization inhibitor, inhibited des A and des A,B fibrinogen from enhancing thrombin-catalyzed factor XIIIa formation. Gly-pro-arg-pro did not modify factor XIIIa formation in afibrinogenemic plasma and did not inhibit thrombin cleavage of the chromogenic substrate S-2238. These results demonstrate that fibrin polymers accelerate thrombin-catalyzed plasma factor XIIIa formation.
Greenberg
C S
CS
Miraglia
C C
CC
D000347:Afibrinogenemia / Q000097:blood; D002118:Calcium / Q000378:metabolism; D004492:Edetic Acid; D005176:Factor XIII / Q000378:metabolism*; D005337:Fibrin / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D009842:Oligopeptides / Q000494:pharmacology; D013917:Thrombin / Q000378:metabolism*; D011503:Transglutaminases
D009842:Oligopeptides; C034585:glycyl-prolyl-arginyl-proline; D005337:Fibrin; D005340:Fibrinogen; D005176:Factor XIII; D004492:Edetic Acid; D011503:Transglutaminases; D013917:Thrombin; D002118:Calcium