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Increased resistance to plasmic degradation of fibrin with highly
crosslinked alpha-polymer chains formed at high factor XIII concentrations
CW Francis and VJ Marder
Department of Medicine, University of Rochester School of Medicine and
Dentistry, NY 14642.
We have previously demonstrated that increasing factor XIII concentrations
above that present in plasma (1 U/mL) results in the formation of very high
molecular weight alpha fate polyacrylamide and agarose gel electrophoresis
(SDS-PAGE). In this report, we have examined the effect of such
crosslinking on plasmic susceptibility of fibrin prepared from purified
fibrinogen and from plasma in the presence of factor XIII concentrations
between 0 and 10 U/mL. The crosslinking achieved with purified fibrinogen
at 1 U/mL factor XIII increased resistance to plasmic degradation by 32% as
measured in a radiolabeled clot lysis system. However, further increases in
plasmic resistance occurred at factor XIII concentrations of 2 and 10 U/mL,
the latter decreasing the lysis rate to 45% of that which occurred in the
absence of factor XIII. To achieve the same rate of clot lysis with fibrin
formed using 10 U/mL rather than 1 U/mL of factor XIII, an increase in
plasmin concentration of up to 4.2-fold was required. Similar results were
obtained using clots prepared from plasma in the presence of factor XIII
concentrations greater than 1 U/mL. Since the alpha 2-plasmin inhibitor
content was the same for fibrin at 1 or 10 U/mL factor XIII, the increasing
plasmic resistance could not be attributed to increased binding of the
inhibitor. We conclude that fibrin prepared in the presence of factor XIII
at concentrations exceeding that in plasma shows increased resistance to
plasmic degradation, which is likely explained by the formation of very
high molecular weight alpha polymer chains.
Volume 71,
Issue 5,
pp. 1361-1365,
05/01/1988
Copyright © 1988 by The American Society of Hematology
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