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Articles in PresS, published online ahead of print July 24, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00222.2002
Submitted on May 16, 2002
Accepted on July 17, 2002
1 Bioengineering, University of California, San Diego, La Jolla, CA, USA
* To whom correspondence should be addressed. E-mail: schien{at}bioeng.ucsd.edu.
Blood flow can modulate vascular cell functions. We studied interactions between integrins and Flk-1 in transducing the mechanical shear stress due to flow. This application of a step shear stress caused Flk-1[[bull1]]Cbl activation (Flk-1[[bull1]]Cbl association, tyrosine phosphorylation of the Cbl-bound Flk-1, and tyrosine phosphorylation of Cbl) in bovine aortic endothelial cells (BAECs). The activation of integrins by plating BAECs on vitronectin or fibronectin also induced this Flk-1[[bull1]]Cbl activation. The shear-induced Flk-1[[bull1]]Cbl activation was blocked by inhibitory antibodies for 
vß3 or ß1 integrin, suggesting that it is mediated by integrins. Inhibition of Flk-1 by SU1498 also abolished this shear-induced Flk-1[[bull1]]Cbl activation. In contrast to the requirement of integrins for Flk-1[[bull1]]Cbl activation, the Flk-1 blocker SU1498 had no detectable effect on the shear-induced integrin activation, suggesting that integrins and Flk-1 play sequential roles in the signal transduction hierarchy induced by shear stress. Integrins are essential for the mechanical activation of Flk-1 by shear stress, but not for the chemical activation of Flk-1 by VEGF.
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