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Articles in PresS, published online ahead of print November 5, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00172.2002
Submitted on May 1, 2002
Accepted on October 23, 2002
1 Department of Medicine, Boston Medical Center and Boston University School of Medicine, Boston, MA, USA
* To whom correspondence should be addressed. E-mail: wliebert{at}bu.edu.
When mouse proximal tubular cells in culture were subjected to cyanide (CN)-induced chemical anoxia, the activity of c-Src kinase increased 3 fold. PP2, a specific inhibitor of Src kinase completely prevented Src activation. CN also caused an increase in the permeability of the MPT cell monolayer which was partly prevented by PP2. In response to chemical anoxia, the proteins that constitute the ZA (E-cadherin and the catenins) disappeared from their normal location at cell-cell borders and appeared within the cytosol. In addition, CN resulted in the appearance of c-
Src at cell-cell borders. PP2 ameliorated the structural alterations in the ZA as well as the appearance of Src at cell borders induce by chemical anoxia. Co-immunoprecipitation studies demonstrated that CN increased the association of c-Src with 
- catenin and p120 and that this association was blocked by PP2. Finally, we show that tyrosine phosphorylation of both - catenin and p120 increased substantially during chemical anoxia, and that these events were also prevented by PP2. In summary, we show that chemical anoxia induces activation of c-Src and its translocation to cell-cell junctions where it binds to and phosphorylates -catenin and p120. Our findings also suggests that these events contribute to the loss of the epithelial barrier function associated with chemical anoxia.
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