| 10915642 |
Rao RK, Li L, Baker RD, Baker SS, Gupta A: Glutathione oxidation and PTPase inhibition by hydrogen peroxide in Caco-2 cell monolayer. Am J Physiol Gastrointest Liver Physiol. 2000 Aug;279(2):G332-40.
The role of H (2) O (2) and protein thiol oxidation in oxidative stress-induced epithelial paracellular permeability was investigated in Caco-2 cell monolayers. Treatment with a H (2) O (2) generating system (xanthine oxidase + xanthine) or H (2) O (2) (20 microM) increased the paracellular permeability. Xanthine oxidase-induced permeability was potentiated by superoxide dismutase and prevented by catalase. H (2) O (2)-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 H (2) O (2)-induced permeability, but it was potentiated by 1,3-bis (2-chloroethyl)-1-nitrosourea. H (2) O (2) reduced cellular GSH and protein thiols and increased GSSG. H (2) O (2)-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 H (2) O (2)-treated cells. This study indicates that H (2) O (2), but not O (2)(-). or.OH, increases paracellular permeability of Caco-2 cell monolayer by a mechanism that involves oxidation of GSH and inhibition of PTPases. |
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