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Extracellular matrix of cultured bovine aortic endothelial cells contains
functionally active type 1 plasminogen activator inhibitor
J Mimuro, RR Schleef and DJ Loskutoff
The extracellular matrix (ECM) of cultured bovine aortic endothelial cells
(BAEs) was analyzed by immunoblotting and reverse fibrin autography and
shown to contain type 1 plasminogen activator inhibitor (PAI-1). Most PAI-1
in the ECM formed complexes with exogenously added tissue-type plasminogen
activator (tPA), demonstrating that this PAI-1 was functionally active. The
resulting tPA/PAI-1 complexes were recovered in the reaction solution,
indicating that the PAI-1 in such complexes no longer bound to ECM. The
PAI-1 could not be removed by incubating ECM in high salt (2 mol/L NaCl),
sugars (1 mol/L galactose, 1 mol/L mannose), glycosaminoglycans (10 mmol/L
heparin, 10 mmol/L dermatan sulfate), or epsilon-aminocaproic acid (0.1
mol/L). However, PAI-1 could be extracted from ECM by treatment with either
arginine (0.5 mol/L) or potassium thiocyanate (2 mol/L), or by incubation
under acidic conditions (pH 2.5). ECM depleted of PAI-1 by acid extraction
was able to bind both the active and latent forms of PAI-1. In this
instance, most of the bound PAI-1 did not form complexes with tPA,
indicating that the latent form was not activated as a consequence of
binding to ECM. Although the PAI-1 activity in conditioned medium decayed
with a half-life (t 1/2) of less than 3 hours, the t 1/2 of ECM- associated
PAI-1 was greater than 24 hours. These data suggest that PAI- 1 is produced
by cultured BAEs in an active form and is then either released into the
medium where it is rapidly inactivated or into the subendothelium where it
binds to ECM. The specific binding of PAI-1 to ECM protects it from this
inactivation.
Volume 70,
Issue 3,
pp. 721-728,
09/01/1987
Copyright © 1987 by The American Society of Hematology
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