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Am J Physiol Cell Physiol (July 24, 2002). doi:10.1152/ajpcell.00230.2002
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Articles in PresS, published online ahead of print July 24, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00230.2002
Submitted on May 20, 2002
Accepted on July 17, 2002

Src-dependent, neutrophil-mediated vascular hyperpermeability and ß-catenin modification

John H Tinsley1*, Elena E Ustinova1, Wenjuan Xu1, and Sarah Y Yuan1

1 Medical Physiology, Texas A&M University System Health Science Center, Temple, TX, USA

* To whom correspondence should be addressed. E-mail: jht{at}tamu.edu.

The hyperpermeability response of microvessels in inflammation involves complex signaling reactions and structural modifications in the endothelium. Our goal was to determine the role of Src-family kinases in neutrophil-mediated venular hyperpermeability and possible interactions between Src and endothelial barrier components. We found that inhibition of Src abolished the increases in albumin permeability caused by C5a-activated neutrophils in intact, perfused coronary venules as well as in cultured endothelial monolayers. Activated neutrophils increased Src phosphorylation at Tyr416, which is located in the catalytic domain, and decreased phosphorylation at Tyr527 near the carboxyl terminus; events consistent with reports that phosphorylating and transforming activities of Src are upregulated by Tyr416 phosphorylation and negatively regulated by Tyr527 phosphorylation. Furthermore, neutrophil stimulation resulted in association of Src with the endothelial junction protein ß-catenin and ß-catenin tyrosine phosphorylation. These phenomena were abolished by blockage of Src activity. Taken together, our studies for the first time link neutrophil-induced hyperpermeability to a pathway involving Src kinase activation, Src/ß-catenin association, and ß-catenin tyrosine phosphorylation in the microvascular endothelium.




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