L-Glutamine ameliorates acetaldehyde-induced increase in paracellular permeability in Caco-2 cell monolayer

Am J Physiol Gastrointest Liver Physiol. 2004 Sep;287(3):G510-7. doi: 10.1152/ajpgi.00058.2004.

Abstract

Role of L-glutamine in the protection of intestinal epithelium from acetaldehyde-induced disruption of barrier function was evaluated in Caco-2 cell monolayer. L-Glutamine reduced the acetaldehyde-induced decrease in transepithelilal electrical resistance and increase in permeability to inulin and lipopolysaccharide in a time- and dose-dependent manner; d-glutamine, L-aspargine, L-arginine, L-lysine, or L-alanine produced no significant protection. The glutaminase inhibitor 6-diazo-5-oxo-L-norleucine failed to affect the L-glutamine-mediated protection of barrier function. L-Glutamine reduced the acetaldehyde-induced redistribution of occludin, zonula occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions. Acetaldehyde dissociates occludin, ZO-1, E-cadherin, and beta-catenin from the actin cytoskeleton, and this effect was reduced by L-glutamine. L-Glutamine induced a rapid increase in the tyrosine phosphorylation of EGF receptor, and the protective effect of L-glutamine was prevented by AG1478, the EGF-receptor tyrosine kinase inhibitor. These results indicate that L-glutamine prevents acetaldehyde-induced disruption of the tight junction and increase in the paracellular permeability in Caco-2 cell monolayer by an EGF receptor-dependent mechanism.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetaldehyde / antagonists & inhibitors*
  • Acetaldehyde / pharmacology*
  • Actins / metabolism
  • Adherens Junctions / drug effects
  • Caco-2 Cells
  • Cell Membrane Permeability / drug effects*
  • Cytoskeletal Proteins / metabolism
  • Dose-Response Relationship, Drug
  • Egtazic Acid / pharmacology
  • Endotoxins / pharmacology
  • ErbB Receptors / antagonists & inhibitors
  • Glutamine / pharmacology*
  • Humans
  • Lipopolysaccharides / pharmacology
  • Mannitol / pharmacology
  • Membrane Proteins / metabolism
  • Occludin
  • Phosphorylation
  • Quinazolines
  • Tight Junctions / drug effects
  • Tyrosine / metabolism
  • Tyrphostins / pharmacology

Substances

  • Actins
  • Cytoskeletal Proteins
  • Endotoxins
  • Lipopolysaccharides
  • Membrane Proteins
  • OCLN protein, human
  • Occludin
  • Quinazolines
  • Tyrphostins
  • Glutamine
  • RTKI cpd
  • Mannitol
  • Tyrosine
  • Egtazic Acid
  • ErbB Receptors
  • Acetaldehyde