Toxicological Sciences, Vol 51, 80-86, Copyright © 1999 by Society of Toxicology
AR Parrish, JM Catania, J Orozco and AJ Gandolfi
The impact of xenobiotics on intercellular adhesion, a fundamental
biological process regulating most, if not all, cellular pathways, has been
sparsely investigated. Cell-cell adhesion is regulated in the epithelium
primarily by the E-cadherin/catenin complex. To characterize the impact of
oxidative stress on the E-cadherin/catenin complex, precision-cut mouse
liver slices were challenged with two model compounds for the generation of
oxidative stress, diamide (DA; 25-250 microM) or t-butylhydroperoxide
(tBHP; 5-50 microM), for 6 h. At the concentrations used, neither compound
elicited cytotoxicity, as assessed by intracellular K+ content and leakage
of lactate dehydrogenase into the culture media. However, a 25% reduction
in non- protein sulfhydryl levels, an indication of oxidative perturbation,
was seen in liver slices treated with DA or tBHP. Total protein expression
of E-cadherin, beta-, or alpha-catenin was not affected by challenge with
DA or tBHP. A decrease of beta-catenin in the SDS-soluble fraction of
slices, an indicator of the formation of the adhesion complex, was
observed. Additionally, a decrease in beta-catenin interactions with E-
cadherin and alpha-catenin, as assessed by immunoprecipitation and Western
blot analysis, was seen. Disruption of the E-cadherin/catenin complex by
tBHP, but not DA, correlated with enhanced tyrosine phosphorylation of
beta-catenin. These results suggest that noncytotoxic oxidative stress
disrupts the E-cadherin/catenin cell adhesion complex in precision-cut
mouse liver slices.
ARTICLES
Chemically induced oxidative stress disrupts the E-cadherin/catenin cell adhesion complex
Department of Anesthesiology, College of Medicine, Southwest Environmental Health Sciences Center. University of Arizona, Tucson, USA. parrish@medicine.tamu.edu
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