Key role of PLC-gamma in EGF protection of epithelial barrier against iNOS upregulation and F-actin nitration and disassembly

Am J Physiol Cell Physiol. 2003 Oct;285(4):C977-93. doi: 10.1152/ajpcell.00121.2003. Epub 2003 Jun 4.

Abstract

Upregulation of inducible nitric oxide synthase (iNOS) is key to oxidant-induced disruption of intestinal (Caco-2) monolayer barrier, and EGF protects against this disruption by stabilizing the cytoskeleton. PLC-gamma appears to be essential for monolayer integrity. We thus hypothesized that PLC-gamma activation is essential in EGF protection against iNOS upregulation and the consequent cytoskeletal oxidation and disarray and monolayer disruption. Intestinal cells were transfected to stably overexpress PLC-gamma or to inhibit its activation and were then pretreated with EGF +/- oxidant (H2O2). Wild-type (WT) intestinal cells were treated similarly. Relative to WT monolayers exposed to oxidant, pretreatment with EGF protected monolayers by: increasing native PLC-gamma activity; decreasing six iNOS-related variables (iNOS activity/protein, NO levels, oxidative stress, actin oxidation/nitration); increasing stable F-actin; maintaining actin stability; and enhancing barrier integrity. Relative to WT cells exposed to oxidant, transfected monolayers overexpressing PLC-gamma (+2.3-fold) were protected, as indicated by decreases in all measures of iNOS-driven pathway and enhanced actin and barrier integrity. Overexpression-induced inhibition of iNOS was potentiated by low doses of EGF. Stable inhibition of PLC-gamma prevented all measures of EGF protection against iNOS upregulation. We conclude that 1) EGF protects against oxidative stress disruption of intestinal barrier by stabilizing F-Actin, largely through the activation of PLC-gamma and downregulation of iNOS pathway; 2) activation of PLC-gamma is by itself essential for cellular protection against oxidative stress of iNOS; and 3) the ability to suppress iNOS-driven reactions and cytoskeletal oxidation and disassembly is a novel mechanism not previously attributed to the PLC family of isoforms.

Publication types

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

MeSH terms

  • Actin Cytoskeleton / physiology
  • Actins / metabolism*
  • Caco-2 Cells
  • Cytoskeleton / drug effects
  • Epidermal Growth Factor / physiology*
  • Humans
  • Hydrogen Peroxide / pharmacology
  • Intestinal Mucosa / metabolism*
  • Intracellular Membranes / metabolism
  • Nitrates / metabolism*
  • Nitric Oxide Synthase / metabolism*
  • Nitric Oxide Synthase Type II
  • Oxidants / pharmacology
  • Oxidation-Reduction / drug effects
  • Peptide Fragments / pharmacology
  • Permeability
  • Phosphoinositide Phospholipase C
  • Phospholipase C gamma
  • Protein Processing, Post-Translational
  • Tissue Distribution
  • Type C Phospholipases / antagonists & inhibitors
  • Type C Phospholipases / chemistry
  • Type C Phospholipases / pharmacology
  • Type C Phospholipases / physiology*
  • Up-Regulation / drug effects

Substances

  • Actins
  • Nitrates
  • Oxidants
  • Peptide Fragments
  • Epidermal Growth Factor
  • Hydrogen Peroxide
  • NOS2 protein, human
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type II
  • Type C Phospholipases
  • PLCZ1 protein, human
  • Phosphoinositide Phospholipase C
  • Phospholipase C gamma