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Next Article 
Surface-dependent reactions of the vitamin K-dependent enzyme complexes
KG Mann, ME Nesheim, WR Church, P Haley and S Krishnaswamy
Department of Biochemistry, University of Vermont, Burlington 05405.
During the past 20 years contributions from many laboratories have led to
the development of isolation procedures, delineation of primary structures,
and more recently, to the expression of recombinant proteins associated
with the coagulation cascade. In general, studies of coagulation proteins
under defined conditions have demonstrated the prescience of Davie and
Ratnoff and MacFarlane in their proposals of the coagulation cascade. The
more recent discovery of thrombomodulin by Esmon et al has led to the
identification and characterization of components of the vitamin
K-dependent anticoagulant pathway. In this review we have attempted to
analyze and compare the functional properties of each of the vitamin
K-dependent enzyme complexes associated with the procoagulant and
anticoagulant phases of blood clotting. Although dissimilarities exist, the
vitamin K-dependent complexes have analogous requirements and appear to
function with a common general mode of organization. Membrane-bound
cofactors serve as anchoring sites for the appropriate membrane-binding
enzymes. This process localizes the complex on the membrane surface and
increases the catalytic efficiency for substrate utilization. Complex
formation provides extraordinary improvements in the catalytic efficiency
for the complexes as compared with their soluble enzyme components.
Membrane- bound complexes provide a mechanism that can be regulated at a
site by membrane presentation, zymogen activation, and cofactor activation
or presentation. The kinetic constants obtained for the various coagulation
reactions determined in vitro provide some insights into how these pathways
may function in vivo. The catalytic efficiency (kcat/Km) for factor X
activation by factor VIIIa/factor IXa is far in excess of the catalytic
efficiency of activation of factor X by tissue factor/factor VIIa (Table
3). This may provide a rational interpretation for the observation that
patients with hemophilia A and B bleed even though they appear to have an
alternative pathway to factor X activation. In addition, tissue factor is
not ordinarily presented by the vascular tissue that has direct access to
blood. However, it appears that extravascular constitutive tissue factor is
available once the blood vessel becomes disrupted. The efforts to identify
the initiating reactions of the blood coagulation process have not been
unambiguously successful. We conclude that factor VII is most likely a
zymogen, just as are the other proenzymes of the blood clotting process. In
addition, it is difficult to rationalize the importance of the intrinsic
pathway of coagulation involving factor XII, prekallikrein, and high
molecular weight kininogen since the congenital absence of any one of these
factors does not result in abnormal bleeding.(ABSTRACT TRUNCATED AT 400
WORDS)
Volume 76,
Issue 1,
pp. 1-16,
07/01/1990
Copyright © 1990 by The American Society of Hematology
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R. M. Camire
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