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(Received for publication, June 7, 1996, and in revised form, July 12, 1996)
From the Departments of The binding and assembly of the coagulation
proteases on the endothelial cell surface are important steps not only
in the generation of thrombin and thrombogenesis, but also in vascular
cell signaling. Effector cell protease receptor (EPR-1) was identified
as a novel leukocyte cell surface receptor recognizing the coagulation
serine protease Factor Xa but not the precursor Factor X. We now
demonstrate that EPR-1 is expressed on vascular endothelial cells and
smooth muscle cells. Northern blots of endothelial and smooth muscle
cells demonstrated three abundant mRNA bands of 3.0, 1.8, and 1.3
kDa. 125I-Labeled Factor Xa bound to endothelial cells in a
dose-dependent saturable manner, and the binding was
inhibited by antibody to EPR-1. No specific binding was observed with a
recombinant mutant Factor X in which the activation site was
substituted by Arg196
Volume 271, Number 45,
Issue of November 8, 1996
pp. 28407-28413
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Biochemistry,
Pathology, and § Medicine, Cornell University
Medical College, New York, New York 10021, the ** Department of
Immunology, The Scripps Research Institute, La Jolla, California 92037,
and the ¶ Department of Pathology, Yale University School of
Medicine, New Haven, Connecticut 06536
Gln to prevent the proteolytic
conversion to Xa. EPR-1 was identified immunohistochemically on
microvascular endothelial and smooth muscle cells. Functionally,
exposure of smooth muscle cells or endothelial cells to Factor Xa
induced a 3-fold and a 2-fold increase in [3H]thymidine
uptake, respectively. However, receptor occupancy alone is insufficient
for mitogenic signaling because the active site of the enzyme is
required for mitogenesis. Thus, EPR-1 represents a site of specific
protease-receptor complex assembly, which during local initiation of
the coagulation cascade could mediate cellular signaling and responses
of the vessel wall.
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