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Am J Physiol Cell Physiol (July 17, 2002). doi:10.1152/ajpcell.00162.2002
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Articles in PresS, published online ahead of print July 17, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00162.2002
Submitted on April 10, 2002
Accepted on July 11, 2002

On the mechanism of thrombin-induced angiogenesis: Involvement of {alpha}vß3 integrin

Nikos E. Tsopanoglou1, Paraskevi Andriopoulou1, and Michael E. Maragoudakis1*

1 Pharmacology, University of Patras, Patras, Greece

* To whom correspondence should be addressed. E-mail: maragoud{at}med.upatras.gr.

Thrombin was reported to be a potent angiogenic factor both in vitro and in vivo and many of the cellular effects of thrombin may contribute to activation of angiogenesis. In this report we show that thrombin-treatment of human endothelial cells increases mRNA and protein levels of {alpha}vß3 integrin. This thrombin-mediated effect is specific, dose dependent and requires the catalytic site of thrombin. In addition thrombin interacts with {alpha}vß3 as demonstrated by direct binding of {alpha}vß3 protein to immobilized thrombin. This interaction of thrombin with {alpha}vß3 integrin, which is an angiogenic marker in vascular tissue, is of functional significance. Immobilized thrombin promotes endothelial cells attachment, migration and survival. Antibody to {alpha}vß3 or a specific peptide antagonist to {alpha}vß3 can abolish all these {alpha}vß3-mediated effects. Furthermore, in chick chorioallantoic membrane system the antagonist peptide to {alpha}vß3 diminishes both basal and the thrombin-induced angiogenesis. These results support the pivotal role of thrombin in activation of endothelial cells and angiogenesis and may be related to the clinical observation of neovascularization within thrombi.




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