© 1997 American Heart Association, Inc.
Articles |
Thrombin Receptor-Mediated Increase of Two Matrix Metalloproteinases, MMP-1 and MMP-3, in Human Endothelial Cells
From INSERM U. 311, Etablissement de Transfusion Sanguine de Strasbourg, Strasbourg Cédex, France (E.D.-C., F.L., J.-P.C., C.K.-S.); and Laboratoire d'Oncologie Moléculaire, Institut de Recherche contre les Cancers de l'Appareil Digestif, Hôpitaux Universitaires de Strasbourg, Strasbourg, France (C.O.).
Correspondence to Claudine Klein-Soyer, Etablissement de Transfusion Sanguine, INSERM U. 311, 10, rue Spielmann, B.P. 36, 67065 Strasbourg Cédex, France. E-mail claudine.soyer{at}etss.u-strasbg.fr
Abstract Matrix metalloproteinases (MMPs) are responsible for
the degradation of extracellular matrix components and are secreted by
a variety of cells including human endothelial cells.
Because 
-thrombin is known to interact with matrix components and
has been shown to activate latent MMP-2 in human umbilical vein
endothelial cells, we investigated whether human
-thrombin could also regulate other MMPs secreted by the human
saphenous vein or mammary artery endothelial cells
(EC). After treatment of EC with increasing concentrations of thrombin
for different periods of time, a significantly higher
gelatinolytic activity of both MMP-1 and MMP-3 was
observed in addition to MMP-2 activation. The effect of thrombin was
time and dose-dependent, reaching a maximum at 24 hours. After
treatment with 5 NIH U/ml thrombin for 24 hours, Western blotting
revealed 9.5- and 4.4-fold increases over control values for MMP-3 and
MMP-1, respectively. The synthetic thrombin receptor agonist peptide
SFLLRNPNDKYEPF fully reproduced the action of thrombin, whereas
chemical inactivation of the catalytic site of thrombin abolished its
effect on MMP-1 and MMP-3. Thrombin and SFLLRNPNDKYEPF both induced
MMP-3 mRNA synthesis but had no significant influence on constitutive
MMP-1 mRNA levels. These results demonstrate that thrombin not only
activates latent MMP-2 but also modulates MMP-1 and MMP-3
production in EC, this latter effect being mediated by the
G-protein-coupled thrombin receptor. Hence, our present data
provide evidence to support the suspected role of thrombin in tissue
remodeling and angiogenesis.
Key Words: interstitial collagenase • stromelysin-1 • angiogenesis • -thrombin • thrombin receptor agonist peptide
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