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MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils

Patricia Y Coxon1, Madhavi J Rane, Silvia Uriarte

  • 1Department of Medicine, University of Louisville Health Sciences Center, Louisville, KY 40202, USA.

Cellular Signalling
|September 23, 2003
PubMed

Insights

MAPK-activated protein kinase-2 (MK2) mediates key human neutrophil functions, including chemotaxis and respiratory burst. MK2 activation is dependent on both p38 MAPK and extracellular signal-regulated kinase (ERK), highlighting its central role in neutrophil signaling.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • p38 Mitogen-Activated Protein Kinase (MAPK) regulates critical neutrophil functions.
  • MAPK-activated protein kinase-2 (MK2) is activated by p38 MAPK in neutrophils.

Purpose of the Study:

  • To investigate if MK2 mediates p38 MAPK-dependent neutrophil responses.
  • To compare the effects of p38 MAPK and MK2 inhibition on neutrophil functions.

Main Methods:

  • Utilized p38 MAPK inhibitor (SB203580) and an MK2 inhibitory peptide.
  • Assessed respiratory burst activity, exocytosis, chemotaxis, and IL-8 production.
  • Investigated extracellular signal-regulated kinase (ERK) involvement using PD98059.

Main Results:

  • Both SB203580 and MK2 peptide inhibited respiratory burst, exocytosis, and chemotaxis.
  • SB203580, but not MK2 peptide, inhibited LPS-induced IL-8 production.
  • ERK phosphorylated MK2 in vitro and activated it in stimulated neutrophils, suggesting dual kinase involvement.

Conclusions:

  • MK2 mediates p38 MAPK-dependent neutrophil responses.
  • MK2 also plays a role in ERK-dependent neutrophil signaling pathways.
  • These findings elucidate MK2's crucial role in integrating signals from both p38 MAPK and ERK in neutrophils.

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