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Am J Physiol Gastrointest Liver Physiol 279: G332-G340, 2000;
0193-1857/00 $5.00
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Vol. 279, Issue 2, G332-G340, August 2000

Glutathione oxidation and PTPase inhibition by hydrogen peroxide in Caco-2 cell monolayer

R. K. Rao, L. Li, R. D. Baker, S. S. Baker, and A. Gupta

Department of Pediatrics, Medical University of South Carolina, Charleston, South Carolina 29425

The role of H2O2 and protein thiol oxidation in oxidative stress-induced epithelial paracellular permeability was investigated in Caco-2 cell monolayers. Treatment with a H2O2 generating system (xanthine oxidase + xanthine) or H2O2 (20 µM) increased the paracellular permeability. Xanthine oxidase-induced permeability was potentiated by superoxide dismutase and prevented by catalase. H2O2-induced permeability was prevented by ferrous sulfate and potentiated by deferoxamine and 1,10-phenanthroline. GSH, N-acetyl-L-cysteine, dithiothreitol, mercaptosuccinate, and diethylmaleate inhibited H2O2-induced permeability, but it was potentiated by 1,3-bis(2-chloroethyl)-1-nitrosourea. H2O2 reduced cellular GSH and protein thiols and increased GSSG. H2O2-mediated reduction of GSH-to-GSSG ratio was prevented by ferrous sulfate, GSH, N-acetyl-L-cysteine, diethylmaleate, and mercaptosuccinate and potentiated by 1,10-phenanthroline and 1,3-bis(2-chloroethyl)-1-nitrosourea. Incubation of soluble fraction of cells with GSSG reduced protein tyrosine phosphatase (PTPase) activity, which was prevented by coincubation with GSH. PTPase activity was also lower in H2O2-treated cells. This study indicates that H2O2, but not O2-· or ·OH, increases paracellular permeability of Caco-2 cell monolayer by a mechanism that involves oxidation of GSH and inhibition of PTPases.

intestine; tight junction; protein tyrosine phosphatase; signal transduction; tyrosine kinase


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