Nonsteroidal anti-inflammatory drugs suppress T-cell activation by inhibiting p38 MAPK induction

J Biol Chem. 2002 Jan 11;277(2):1509-13. doi: 10.1074/jbc.M110676200. Epub 2001 Nov 7.

Abstract

In addition to antagonizing inflammation by inhibiting the activity of cyclooxygenases (COX), nonsteroidal anti-inflammatory drugs (NSAID) block T-cell activation. The immunosuppressant activity of NSAID correlates with their ability to block transcription factors required for the expression of inducible response genes triggered by T-cell antigen receptor (TCR) engagement. Whereas the inhibition of nuclear factor-kappaB by aspirin and sodium salicylate can be partly accounted for by their binding to IkappaB kinase-beta, the broad range of transcriptional targets of NSAID suggests that the products of COX activity might affect one or more among the early steps in the TCR-signaling cascade. Here we show that the inhibition of NF-AT activation by NSAID correlates with a selective inhibition of p38 MAP kinase induction. The suppression of TCR-dependent p38 activation by NSAID can be fully overcome by prostaglandin E(2), underlining the requirement for COX activity in p38 activation. Furthermore, the inhibition of COX-1 results in defective induction of the COX-2 gene, which behaves as an early TCR responsive gene. The data identify COX-1 and COX-2 as integral and sequential components of TCR signaling to p38 and contribute to elucidate the molecular basis of immunosuppression by NSAID.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Inflammatory Agents, Non-Steroidal / pharmacology*
  • Cell Line
  • Cyclooxygenase 1
  • Cyclooxygenase 2
  • DNA-Binding Proteins / metabolism*
  • Enzyme Activation
  • Enzyme Induction
  • Genes, Reporter
  • Humans
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Lymphocyte Activation / drug effects*
  • MAP Kinase Signaling System / physiology*
  • Membrane Proteins
  • Mitogen-Activated Protein Kinases / antagonists & inhibitors
  • Mitogen-Activated Protein Kinases / metabolism*
  • NFATC Transcription Factors
  • Nuclear Proteins*
  • Prostaglandin-Endoperoxide Synthases / genetics
  • Prostaglandin-Endoperoxide Synthases / metabolism
  • Recombinant Fusion Proteins / metabolism
  • T-Lymphocytes / drug effects*
  • T-Lymphocytes / metabolism
  • Transcription Factors / metabolism*
  • p38 Mitogen-Activated Protein Kinases

Substances

  • Anti-Inflammatory Agents, Non-Steroidal
  • DNA-Binding Proteins
  • Isoenzymes
  • Membrane Proteins
  • NFATC Transcription Factors
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Transcription Factors
  • Cyclooxygenase 1
  • Cyclooxygenase 2
  • PTGS1 protein, human
  • PTGS2 protein, human
  • Prostaglandin-Endoperoxide Synthases
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases