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Proteolytic degradation of von Willebrand factor after DDAVP administration
in normal individuals
J Batlle, MF Lopez-Fernandez, A Lopez-Borrasca, C Lopez-Berges, JA Dent, SD Berkowitz, ZM Ruggeri and TS Zimmerman
The infusion of 1-deamino-8-D-arginine vasopressin (DDAVP) in normal
individuals is followed by an increase in factor VIII/von Willebrand factor
(vWF) in plasma, by an increase in intensity of all sizes of multimers, and
by the appearance of larger multimers of vWF than those seen in the resting
state. Since the larger multimers are rapidly cleared and proteolysis is
known to cause disaggregation of large multimers, we evaluated the degree
of vWF proteolysis after DDAVP administration. DDAVP was infused into eight
normal adult volunteers, and the relative proportions of the intact 225
kilodalton (kDa) subunit and the 189, 176, and 140 kDa vWF fragments were
compared before and at different times after DDAVP infusion. The relative
proportion of the 176 kDa fragment was increased, whereas that of the other
species was decreased, thereby indicating that proteolytic fragmentation
had occurred. However, plasmin did not appear to be responsible because the
vWF fragments characteristically produced by this enzyme could not be
detected. Concomitant analysis of vWF multimeric structure showed that
these changes were accompanied by an increase in the relative proportion of
the satellite bands, which suggests that they were proteolytically
generated. Proteolysis may explain, at least in part, rapid clearance of
larger vWF multimers released by DDAVP.
Volume 70,
Issue 1,
pp. 173-176,
07/01/1987
Copyright © 1987 by The American Society of Hematology
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