Anastasiadis PZ

Bacallao R

Diviya Sinha

Downing JR

Gumbiner B

Ilic D

John H. Schwartz

Mandel LJ

Nieset JE

Schwartz JH

Valerie R. Price

Wilfred Lieberthal

Zhiyong Wang

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 β-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 β-catenin and p120. Our findings suggest that these events contribute to the loss of the epithelial barrier function associated with chemical anoxia.</jats:p

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AJP Renal Physiology

Chemical anoxia of tubular cells induces activation of c-Src and its translocation to the zonula adherens

Chemical anoxia of tubular cells induces activation  of c-Src and its translocation to the zonula adherens

Chemical anoxia of tubular cells induces activation of c-Src and its translocation to the zonula adherens

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