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Plasminogen receptors, urokinase receptors, and their modulation on human
endothelial cells
LA Miles, EG Levin, J Plescia, D Collen and EF Plow
Department of Immunology, Research Institute of Scripps Clinic, La Jolla,
CA 92037.
Endothelial cells are centrally involved in regulation of fibrinolysis, and
receptors for plasminogen and urokinase provide a mechanism by which cells
can regulate their fibrinolytic function. Therefore, the existence and
characteristics of receptors for these fibrinolytic components on cultured
human umbilical vein endothelial cells were examined. We verified the
presence of plasminogen receptors on these cells (Kd = 2.1 +/- 1.3 mumol/L,
and 1.8 +/- 1.3 x 10(7) binding sites/cell). These binding parameters and
other characteristics indicate that these receptors are closely related to
the plasminogen receptors on many circulating and adherent cells. Specific
binding sites that interact with two-chain urokinase of mol wt 55,000 with
a dissociation constant of 2.1 +/- 1.7 nmol/L, with 2.9 +/- 2.9 x 10(5)
sites/cell were also identified. Single-chain urokinase of mol wt 55,000,
but not the two-chain degradation product of mol wt 33,000 bound to the
cells, implicating the amino-terminal aspects of the ligand in receptor
recognition. When endothelial cells were stimulated with thrombin, an agent
that modulates their fibrinolytic potential, both receptor types were
modestly affected; urokinase binding increased 17%, whereas plasminogen
binding decreased 19%. The presence and modulation of plasminogen and
urokinase receptors provide a potentially important additional mechanism by
which endothelial cells may regulate fibrinolysis.
Volume 72,
Issue 2,
pp. 628-635,
08/01/1988
Copyright © 1988 by The American Society of Hematology
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