Inhibition of oxidant-induced nuclear factor-kappaB activation and inhibitory-kappaBalpha degradation and instability of F-actin cytoskeletal dynamics and barrier function by epidermal growth factor: key role of phospholipase-gamma isoform

J Pharmacol Exp Ther. 2004 Apr;309(1):356-68. doi: 10.1124/jpet.103.062232. Epub 2004 Jan 14.

Abstract

Using monolayers of intestinal (Caco-2) cells as a model for studying inflammatory bowel disease (IBD), we previously showed that nuclear factor-kappaB (NF-kappaB) activation is required for oxidant-induced disruption of cytoskeletal and barrier integrity. Epidermal growth factor (EGF) stabilizes the F-actin cytoskeleton and protects against oxidant damage, but the mechanism remains unclear. We hypothesized that the mechanism involves activation of phospholipase C-gamma (PLC-gamma), which prevents NF-kappaB activation and the consequences of this activation, namely, cytoskeletal and barrier disruption. We studied wild-type and transfected cells. The latter were transfected with varying levels (1-5 microg) of cDNA to either stably overexpress PLC-gamma or to inhibit its activation. Cells were pretreated with EGF before exposure to oxidant (H(2)O(2)). Stably overexpressing PLC-gamma (+2.0-fold) or preincubating with EGF protected against oxidant injury as indicated by 1) decreases in several NF-kappaB-related variables [NF-kappaB (p50/p65 subunit) nuclear translocation, NF-kappaB subunit activity, inhibitory-kappaBalpha (I-kappaBalpha) phosphorylation and degradation]; 2) increases in F-actin and decreases in G-actin; 3) stabilization of the actin cytoskeletal architecture; and 4) enhancement of barrier function. Overexpression induced inactivation of NF-kappaB was potentiated by EGF. PLC-gamma was found mostly in membrane and cytoskeletal fractions (<9% in the cytosolic fractions), indicating its activation. Dominant negative inhibition of endogenous PLC-gamma (-99%) substantially prevented all measures of EGF protection against NF-kappaB activation. We concluded 1) EGF protects against oxidant-induced barrier disruption through PLC-gamma activation, which inactivates NF-kappaB; 2) Activation of PLC-gamma by itself is protective against NF-kappaB activation; 3) the ability to modulate the dynamics of NF-kappaB/I-kappa Balpha is a novel mechanism not previously attributed to the PLC family of isoforms in cells; and 4) development of PLC-gamma mimetics represents a possible new therapeutic strategy for IBD.

Publication types

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

MeSH terms

  • Actins / metabolism*
  • Caco-2 Cells
  • Cell Nucleus / drug effects
  • Cell Nucleus / metabolism
  • Cytoskeleton / drug effects
  • Cytoskeleton / metabolism
  • Cytosol / drug effects
  • Enzyme Stability
  • Epidermal Growth Factor / pharmacology*
  • Humans
  • I-kappa B Proteins / metabolism*
  • NF-kappa B / metabolism*
  • NF-kappa B / physiology
  • Oxidants / pharmacology
  • Phospholipase C gamma
  • Phosphorylation
  • Protein Isoforms
  • Protein Subunits
  • Subcellular Fractions
  • Transfection
  • Type C Phospholipases / metabolism*

Substances

  • Actins
  • I-kappa B Proteins
  • NF-kappa B
  • Oxidants
  • Protein Isoforms
  • Protein Subunits
  • Epidermal Growth Factor
  • Type C Phospholipases
  • Phospholipase C gamma