Dexamethasone causes sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38

Mol Cell Biol. 2002 Nov;22(22):7802-11. doi: 10.1128/MCB.22.22.7802-7811.2002.

Abstract

The stress-activated protein kinase p38 stabilizes a number of mRNAs encoding inflammatory mediators, such as cyclooxygenase 2 (Cox-2). In HeLa cells the anti-inflammatory glucocorticoid dexamethasone destabilizes Cox-2 mRNA by inhibiting p38 function. Here we demonstrate that this effect is phosphatase dependent. Furthermore, in HeLa cells dexamethasone induced the sustained expression of mitogen-activated protein kinase phosphatase 1 (MKP-1), a potent inhibitor of p38 function. The inhibition of p38 and the induction of MKP-1 by dexamethasone occurred with similar dose dependence and kinetics. No other known p38 phosphatases were induced by dexamethasone, and other cell types which failed to express MKP-1 also failed to inhibit p38 in response to dexamethasone. The proinflammatory cytokine interleukin 1 (IL-1) induced MKP-1 expression in a p38-dependent manner and acted synergistically with dexamethasone to induce MKP-1 expression. In HeLa cells treated with IL-1 or IL-1 and dexamethasone, the dynamics of p38 activation mirrored the expression of MKP-1. These observations suggest that MKP-1 participates in a negative-feedback loop which regulates p38 function and that dexamethasone may inhibit proinflammatory gene expression in part by inducing MKP-1 expression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins*
  • Cyclooxygenase 2
  • Dexamethasone / pharmacology*
  • Dose-Response Relationship, Drug
  • Dual Specificity Phosphatase 1
  • Enzyme Inhibitors / pharmacology
  • Gene Expression Regulation, Enzymologic / drug effects*
  • Glucocorticoids / pharmacology
  • HeLa Cells
  • Humans
  • Imidazoles / pharmacology
  • Immediate-Early Proteins / genetics
  • Immediate-Early Proteins / metabolism*
  • Interleukin-1 / metabolism
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Membrane Proteins
  • Mitogen-Activated Protein Kinases / antagonists & inhibitors
  • Mitogen-Activated Protein Kinases / metabolism*
  • Oligonucleotide Array Sequence Analysis
  • Phosphoprotein Phosphatases*
  • Prostaglandin-Endoperoxide Synthases / genetics
  • Prostaglandin-Endoperoxide Synthases / metabolism
  • Protein Phosphatase 1
  • Protein Tyrosine Phosphatases / genetics
  • Protein Tyrosine Phosphatases / metabolism*
  • Pyridines / pharmacology
  • RNA Stability
  • Time Factors
  • p38 Mitogen-Activated Protein Kinases

Substances

  • Cell Cycle Proteins
  • Enzyme Inhibitors
  • Glucocorticoids
  • Imidazoles
  • Immediate-Early Proteins
  • Interleukin-1
  • Isoenzymes
  • Membrane Proteins
  • Pyridines
  • Dexamethasone
  • Cyclooxygenase 2
  • PTGS2 protein, human
  • Prostaglandin-Endoperoxide Synthases
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 1
  • DUSP1 protein, human
  • Dual Specificity Phosphatase 1
  • Protein Tyrosine Phosphatases
  • SB 203580