Temporal control of NF-kappaB activation by ERK differentially regulates interleukin-1beta-induced gene expression

J Biol Chem. 2004 Jan 9;279(2):1323-9. doi: 10.1074/jbc.M307521200. Epub 2003 Oct 27.

Abstract

In cultured rat vascular smooth muscle cells, sustained activation of ERK is required for interleukin-1beta to persistently activate NF-kappaB. Without ERK activation, interleukin-1beta induces only acute and transient NF-kappaB activation. The present study examined whether the temporal control of NF-kappaB activation by ERK could differentially regulate the expression of NF-kappaB-dependent genes, including inducible nitric oxide synthase (iNOS), cyclooxygenase-2 (COX-2), vascular cell adhesion molecule-1 (VCAM-1), and manganese-containing superoxide dismutase (Mn-SOD). Treatment of vascular smooth muscle cells with interleukin-1beta induced the expression of iNOS, COX-2, VCAM-1, and Mn-SOD in a time-dependent manner, but with different patterns. Either PD98059 or U0126, selective inhibitors of MEK, or overexpression of a dominant negative MEK-1 inhibited interleukin-1beta- induced ERK activation and the expression of iNOS and COX-2 but had essentially no effect on the expression of VCAM-1 and Mn-SOD. The expression of these genes was inhibited when NF-kappaB activation was down-regulated by MG132, a proteasome inhibitor, or by overexpression of an I-kappaBalpha mutant that prevented both the transient and the persistent activation of NF-kappaB. Inhibition of ERK did not affect interleukin-1beta-induced I-kappaBalpha phosphorylation and degradation but attenuated I-kappaBbeta degradation. Thus, although NF-kappaB activation was essential for interleukin-1beta induction of each of the proteins studied, gene expression was differentially regulated by ERK and by the duration of NF-kappaB activation. These results reveal a novel functional role for ERK as an important temporal regulator of NF-kappaB activation and NF-kappaB-dependent gene expression.

Publication types

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

MeSH terms

  • Animals
  • Blotting, Western
  • Butadienes / pharmacology
  • Cells, Cultured
  • Cyclooxygenase 2
  • Cysteine Endopeptidases
  • Cysteine Proteinase Inhibitors / pharmacology
  • Dose-Response Relationship, Drug
  • Enzyme Inhibitors / pharmacology
  • Flavonoids / pharmacology
  • Gene Expression Regulation*
  • Genes, Dominant
  • I-kappa B Proteins / metabolism
  • Interleukin-1 / metabolism*
  • Isoenzymes / metabolism
  • Leupeptins / pharmacology
  • Mitogen-Activated Protein Kinases / metabolism*
  • Multienzyme Complexes / antagonists & inhibitors
  • Mutation
  • Myocytes, Smooth Muscle / cytology
  • NF-KappaB Inhibitor alpha
  • NF-kappa B / metabolism*
  • Nitric Oxide Synthase / metabolism
  • Nitric Oxide Synthase Type II
  • Nitriles / pharmacology
  • Phosphorylation
  • Prostaglandin-Endoperoxide Synthases / metabolism
  • Proteasome Endopeptidase Complex
  • RNA, Messenger / metabolism
  • Rats
  • Reverse Transcriptase Polymerase Chain Reaction
  • Superoxide Dismutase / metabolism
  • Time Factors
  • Vascular Cell Adhesion Molecule-1 / metabolism

Substances

  • Butadienes
  • Cysteine Proteinase Inhibitors
  • Enzyme Inhibitors
  • Flavonoids
  • I-kappa B Proteins
  • Interleukin-1
  • Isoenzymes
  • Leupeptins
  • Multienzyme Complexes
  • NF-kappa B
  • Nfkbia protein, rat
  • Nitriles
  • RNA, Messenger
  • U 0126
  • Vascular Cell Adhesion Molecule-1
  • NF-KappaB Inhibitor alpha
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type II
  • Nos2 protein, rat
  • Cyclooxygenase 2
  • Prostaglandin-Endoperoxide Synthases
  • Superoxide Dismutase
  • Mitogen-Activated Protein Kinases
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde
  • 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one