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Activation of p38 in stimulated human neutrophils: Phosphorylation of the oxidase component p47(phox) by p38 and erk but not by jnk

Academic Article
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Overview

authors

  • ElBenna, J.
  • Han, Jiahuai
  • Park, J. W.
  • Schmid, E.
  • Ulevitch, Richard
  • Babior, Bernard Macy

publication date

  • October 1996

journal

  • Archives of Biochemistry and Biophysics  Journal

abstract

  • Incubation of human neutrophils with FMLP, a chemotactic peptide, or PMA, a stimulator of protein kinase C, resulted in the activation of p38, a proline-directed kinase. Previous studies had shown that extracellular signal-regulated kinase (ERK), another proline-directed kinase, was activated with similar kinetics in neutrophils stimulated with FMLP and PMA (1, 2). Because one possible target for these proline-directed kinases is p47phox, a component of the respiratory burst oxidase, we examined the phosphorylation of this protein by p38 and ERK, as well as JNK, another proline-directed kinase present in neutrophils. We found that both p38 and ERK phosphorylated p47phox at the same site and at similar rates, but that p47phox was not a substrate for JNK. These data show that p38, like ERK, can be activated in neutrophils exposed to an appropriate stimulus, and that some but not all proline-directed kinases are able to participate in the phosphorylation of a protein essential for normal neutrophil function.

subject areas

  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cell Membrane
  • Enzyme Activation
  • Humans
  • JNK Mitogen-Activated Protein Kinases
  • Kinetics
  • Mitogen-Activated Protein Kinases
  • N-Formylmethionine Leucyl-Phenylalanine
  • NADPH Dehydrogenase
  • NADPH Oxidase
  • Nerve Tissue Proteins
  • Neutrophils
  • Peptide Fragments
  • Peptide Mapping
  • Phosphopeptides
  • Phosphoproteins
  • Phosphorylation
  • Protein Kinases
  • Receptor Protein-Tyrosine Kinases
  • Receptor, EphA8
  • Tetradecanoylphorbol Acetate
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Identity

International Standard Serial Number (ISSN)

  • 0003-9861

PubMed ID

  • 8900416
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Additional Document Info

start page

  • 395

end page

  • 400

volume

  • 334

issue

  • 2

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