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The conversion of fibrinogen to fibrin: recombinant fibrinogen typifies
plasma fibrinogen
OV Gorkun, YI Veklich, JW Weisel and ST Lord
Department of Pathology and Laboratory Medicine, University of North
Carolina, Chapel Hill 27599-7525, USA.
Plasma fibrinogen is a mixture of multiple molecular forms arising mainly
through alternative mRNA processing and subsequent posttranslational
modification. Recombinant fibrinogen is synthesized without alternative
mRNA processing in a cultured cell system that may generate novel
posttranslational modifications. Thus, to show that recombinant fibrinogen
can serve as a functional model for plasma fibrinogen, we have examined the
conversion of fibrinogen to fibrin, comparing the recombinant with the
plasma protein. We examined the kinetics of (1) thrombin-catalyzed
fibrinopeptide release, (2) thrombin- catalyzed polymerization of
fibrinogen, (3) the polymerization of fibrin monomers, and (4)
FXIIIa-catalyzed cross-link formation. We saw small differences in
polymerization, suggesting that the ordered assembly of protofibrils and
fibers was not identical. In all other analyses, we found that plasma
fibrinogen and recombinant fibrinogen were remarkably similar. Using
electron microscopy, we examined the structures of individual fibrinogen
molecules and fibrin clots. Individual fibrinogen molecules were
predominantly three nodule structures for both recombinant and plasma
proteins. Both samples also displayed four nodule structures, but fewer
four nodule structures were found with recombinant fibrinogen. Fibrin clot
structures were essentially indistinguishable. We concluded that
recombinant fibrinogen can serve as a accurate model for plasma fibrinogen.
Volume 89,
Issue 12,
pp. 4407-4414,
06/15/1997
Copyright © 1997 by The American Society of Hematology
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