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Fluid Shear Stress Activates Proline-Rich Tyrosine Kinase via Reactive Oxygen Species-Dependent Pathway

Fluid Shear Stress Activates Proline-Rich Tyrosine Kinase via Reactive Oxygen Species-Dependent Pathway

Lung-Kuo Tai, Masanori Okuda, Jun-ichi Abe, Chen Yan, Bradford C Berk

Arterioscler Thromb Vasc Biol. 2002 Nov 1;22(11):1790-6.

PMID: 12426206

Abstract:

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 H(2)O(2) 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP126150978-A	BAPTA/AM - CAS 126150-97-8		126150-97-8	Price

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