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J. Biol. Chem., Vol. 278, Issue 14, 11916-11924, April 4, 2003
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From the Department of Physiology, University of Tennessee Health
Sciences Center, Memphis, Tennessee, 38163
The activity of Src kinases appears to play a
role in both assembly and disassembly of tight junction. However, the
role of a specific isoform of Src kinase in regulation of tight
junction is not known. In the present study the role of c-Src in
regulation of epithelial tight junction was investigated in Caco-2 cell
monolayers. Oxidative stress (xanthine oxidase + xanthine) induced an
activation and membrane translocation of c-Src. The oxidative
stress-induced decrease in transepithelial electrical resistance,
increase in inulin permeability, and redistribution of occludin and
ZO-1 from the intercellular junctions were prevented by PP2. The rates
of oxidative stress-induced activation of c-Src, tyrosine
phosphorylation of ZO-1 and
Expression of Kinase-inactive c-Src Delays Oxidative
Stress-induced Disassembly and Accelerates Calcium-mediated Reassembly
of Tight Junctions in the Caco-2 Cell Monolayer*
-catenin, decrease in resistance,
increase in permeability to inulin, and redistribution of occludin and
ZO-1 were significantly greater in cells transfected with wild type
c-Src, whereas it was low in cells transfected with
kinase-inactive c-SrcK297R mutant, when compared with those
in empty vector-transfected cells. The rates of recovery of resistance,
increase in barrier to inulin, and reorganization of occludin and ZO-1
into the intercellular junctions during the calcium-induced reassembly
of tight junction were much greater in Caco-2 cells transfected with
c-SrcK297R as compared with those in cells transfected with
empty vector or wild type c-Src. These results show that
the dominant-negative expression of kinase-inactive c-Src
delays the oxidative stress-induced disruption of tight junction and
accelerates calcium-induced assembly of tight junction in Caco-2 cells
and demonstrate that oxidative stress-induced disruption of
tight junction is mediated by the activation of c-Src.
*
This study was supported by National Institutes of Health
Grants R01-DK55532 and R01-AA12307 (to R. K. R.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Physiology,
University of Tennessee Health Sciences Center, 894 Union Ave., Rm.
426, Memphis, TN 38163. Tel.: 901-448-3235; Fax: 901-448-7126; E-mail: rkrao@physio1.utmem.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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