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Oxidative priming of neutrophils by interferon-gamma

S D Tennenberg1, D E Fey, M J Lieser

  • 1Department of Surgery, Wayne State University School of Medicine, Allen Park Veterans Affairs Medical Center, Detroit, Michigan 48101.

Insights

Interferon-gamma (IFN-gamma) selectively primes neutrophil superoxide anion release in response to specific stimuli. This priming requires new protein synthesis and impacts early signaling pathways in host defense.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Neutrophil (PMN) oxidative responses are crucial for host defense and inflammation.
  • Dysregulated oxidative responses can contribute to tissue injury.

Purpose of the Study:

  • To investigate the mechanisms of interferon-gamma (IFN-gamma)-induced oxidative priming of human neutrophils (PMNs) in vitro.
  • To determine the signaling pathways affected by IFN-gamma priming.

Main Methods:

  • Human PMNs were pretreated with recombinant IFN-gamma.
  • Superoxide anion release was measured in response to various stimuli, including f-Met-Leu-Phe (fMLP), C5a, phorbol myristate acetate, A23187, and NaF.
  • fMLP surface receptor expression and degranulation were assessed.
  • The role of de novo mRNA and protein synthesis was evaluated.

Main Results:

  • IFN-gamma selectively primed superoxide anion release towards receptor-initiated (fMLP, C5a) and guanine nucleotide regulatory protein-activating (NaF) stimuli, but not transduction-mediated stimuli (phorbol myristate acetate, A23187).
  • Priming did not alter fMLP receptor expression or degranulation.
  • Priming was dependent on de novo mRNA and protein synthesis.

Conclusions:

  • The immuno-regulatory lymphokine IFN-gamma primes PMN oxidative responses.
  • This priming appears to involve the production of proteins that modulate early post-receptor signal transduction pathways in oxidative metabolism.

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