Cell-free activation of phagocyte NADPH-oxidase: Tissue and differentiation-specific expression of cytosolic cofactor activity

John F. Parkinson, Luke P. Akard, Michael J. Schell, Theodore G. Gabig

Research output: Contribution to journalArticlepeer-review

Abstract

We examined a variety of tissues for the presence of cytosolic cofactor activity that would support arachidonate-dependent cell-free activation of NADPH-oxidase in isolated human neutrophil membranes. Cofactor activity was not found in cytosol isolated from erythrocytes, lymphocytes, placenta, brain, liver, or the human promyelocytic leukemic cell line HL-60. Induction of differentiation in HL-60 cells led to expression of cytosolic cofactor activity. In dimethylsulphoxide-induced HL-60 cells the level of cytosolic cofactor activity was closely correlated with phorbol myristate acetate-stimulated whole cell superoxide production. These results strongly suggest that the cytosolic cofactor is a phagocyte-specific regulatory protein of physiologic importance in NADPH-oxidase activation.

Original languageEnglish (US)
Pages (from-to)1198-1204
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume145
Issue number3
DOIs
StatePublished - Jun 30 1987

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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