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Am J Physiol Cell Physiol 283: C1501-C1510, 2002. First published July 17, 2002; doi:10.1152/ajpcell.00162.2002
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Vol. 283, Issue 5, C1501-C1510, November 2002

On the mechanism of thrombin-induced angiogenesis: involvement of alpha vbeta 3-integrin

Nikos E. Tsopanoglou, Paraskevi Andriopoulou, and Michael E. Maragoudakis

Department of Pharmacology, Medical School, University of Patras, 25110 Patras, Greece

Thrombin has been 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 vbeta 3-integrin. This thrombin-mediated effect is specific, dose dependent, and requires the catalytic site of thrombin. In addition, thrombin interacts with alpha vbeta 3 as demonstrated by direct binding of alpha vbeta 3 protein to immobilized thrombin. This interaction of thrombin with alpha vbeta 3-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 vbeta 3 or a specific peptide antagonist to alpha vbeta 3 can abolish all these alpha vbeta 3-mediated effects. Furthermore, in the chick chorioallantoic membrane system, the antagonist peptide to alpha vbeta 3 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.

attachment; migration; apoptosis; reverse transcription-polymerase chain reaction


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