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Renal Section, Evans Biomedical Research Center, Department of Medicine, Boston Medical Center and Boston University School of Medicine, Boston, Massachusetts 02118
Cyanide
(CN)-induced chemical anoxia of cultured mouse proximal tubular (MPT)
cells increased the kinase activity of c-Src by approximately
threefold.
4-Amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP2), a specific inhibitor of c-Src, prevented Src activation. CN also
increased the permeability of MPT cell monolayers, an event ameliorated
by PP2. During CN treatment, the proteins of the zonula adherens (ZA;
E-cadherin and the catenins) disappeared from their normal location at
cell-cell borders and appeared within the cytosol. CN also resulted in
the appearance of c-Src at cell-cell borders. PP2 prevented these
CN-induced alterations in the distribution of ZA proteins and c-Src. CN
also increased the association of c-Src with 
-catenin and p120 and
induced a substantial increase in tyrosine phosphorylation of both
catenins. PP2 prevented the CN-induced phosphorylation of these
catenins. In summary, we show that CN-induced chemical anoxia activates
c-Src and induces its translocation to cell-cell junctions where it
binds to and phosphorylates -catenin and p120. Our findings suggest
that these events contribute to the loss of the epithelial barrier
function associated with chemical anoxia.
ischemia; tight junction; Src kinase; E-cadherin; catenins; p120ctn; renal tubular cells
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