on August 22, 2002
Published online before print August 22, 2002, doi: 10.1161/01.ATV.0000034475.40227.40
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Submitted on June 19, 2002
Accepted on August 6, 2002
Fluid Shear Stress Activates Proline-Rich Tyrosine Kinase via Reactive Oxygen Species-Dependent Pathway
Lung-Kuo Tai ;
From the Center for Cardiovascular Research (L.-K.T., J.A., C.Y., B.C.B.), University of Rochester, Rochester, NY, and the Division of Cardiovascular and Respiratory Medicine (M.O.), Kobe University Graduate School of Medicine, Kobe, Japan.
* To whom correspondence should be addressed. E-mail: bradford_berk{at}urmc.rochester.edu.
Objective—Fluid shear stress (flow) modulates endothelial cell (EC) function via specific signal transduction events. Previously, we showed that flow-mediated tyrosine phosphorylation of p130 Crk-associated substrate (Cas) required calcium-dependent c-Src activation. Because flow increases reactive oxygen species (ROS) production in ECs and because H2O2 increases tyrosine phosphorylation of proline-rich tyrosine kinase (PYK2), we hypothesized that flow may activate PYK2 via ROS.
Methods and Results—Exposure of bovine aortic ECs to flow stimulated PYK2 phosphorylation rapidly, with a peak at 2 minutes. The activation of PYK2 and phosphorylation of Cas induced by flow were inhibited by pretreatment with the antioxidant N-acetylcysteine. Flow-induced PYK2 phosphorylation was inhibited by BAPTA-AM, an intracellular calcium chelator. Bovine aortic ECs transfected with kinase-inactive PYK2 showed attenuated flow-stimulated Cas tyrosine phosphorylation. Although flow-induced Cas phosphorylation was inhibited by kinase-inactive Src, PYK2 activation induced by flow was not inhibited by overexpression of kinase-inactive Src.
Conclusions—These results show a redox-sensitive pathway for flow-mediated activation of nonreceptor tyrosine kinase activity that requires ROS and intracellular calcium, but not Src kinase.
Key words: proline-rich tyrosine kinase • calcium • reactive oxygen species • shear stress
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