An investigation into the role of coagulation factor XIII in ADP- induced
aggregation and fibrinogen binding with rabbit platelets
EJ Harfenist, G Raychaudhuri, MA Packham and JF Mustard
Because there was a possibility that activated factor XIII (factor XIIIa)
might stabilize a platelet-fibrinogen aggregate through its crosslinking
action, we have isolated plasma factor XIII, activated it, and studied the
effect of factor XIIIa at a concentration of 3.3 micrograms/ml on
aggregation and 125I-fibrinogen binding of rabbit platelets stimulated with
9 microM ADP. Factor XIIIa did not cause aggregation in the absence of ADP,
nor did it enhance ADP-induced aggregation or substantially stabilize the
platelet aggregate. The presence of factor XIIIa did not affect the amount
of fibrinogen bound to platelets immediately after stimulation with ADP,
but it appeared to cause a slow specific binding of 125I-fibrinogen to
platelets whether or not they were stimulated with ADP. This binding, which
was not inhibited by prostaglandin E1, did not lead to aggregation and was
accompanied by crosslinking of fibrinogen through its A alpha and gamma
chains, either to other fibrinogen molecules or to a platelet protein or
proteins.
Volume 60,
Issue 4,
pp. 905-911,
10/01/1982
Copyright © 1982 by The American Society of Hematology
