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Clearance of human native, proteinase-complexed, and proteolytically
inactivated C1-inhibitor in rats
BJ de Smet, JP de Boer, J Agterberg, G Rigter, WK Bleeker and CE Hack
Central Laboratory of the Netherlands Red Cross Blood Transfusion Service,
Amsterdam.
C1-inhibitor is the only known inhibitor of the classical pathway of
complement and the major inhibitor of the contact pathway of coagulation.
Like other serine proteinase inhibitors, C1-inhibitor can exist in three
conformations, ie, the native, the proteinase-complexed, and the
proteolytically inactivated form. Here we studied the plasma elimination
kinetics of these three forms of human C1-inhibitor in rats. The clearance
of the complexed form of C1-inhibitor appeared to be the most rapid and
depended in part on the proteinase involved (observed plasma t1/2 was 20
minutes for C1s-C1-inhibitor, 32 minutes for kallikrein-C1-inhibitor, and
47 minutes for beta XIIa-C1- inhibitor), whereas that of native
C1-inhibitor was the slowest (observed plasma t1/2 4.5 hours). Inactivated
C1-inhibitor was cleared with an apparent plasma t1/2 of 1.6 hours. Thus,
the short plasma t1/2 of complexed relative to native C1-inhibitor explains
why in patients only low concentrations of C1-inhibitor complexes may be
observed despite activation of the contact and/or complement systems.
Volume 81,
Issue 1,
pp. 56-61,
01/01/1993
Copyright © 1993 by The American Society of Hematology
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