Activation of NADPH oxidase and phosphorylation of membrane proteins in human neutrophils: Coordinate inhibition by a surface antigen-directed monoclonal antibody

S. Pontremoli, E. Melloni, F. Salamino, B. Sparatore, M. Michetti, O. Sacco, B. L. Horecker

Research output: Contribution to journalArticle

Abstract

Exposure of human neutrophils to low concentrations of phorbol myristate acetate (PMA) results, after a brief lag, in the production of superoxide anion and the phosphorylation of membrane proteins. Evidence that these responses are linked has now been obtained using a monoclonal antibody directed against an undefined macrophage surface antigen. The addition of this antibody, which recognizes a 90 kDa neutrophil membrane protein, caused dose-dependent delays in the onset of both phosphorylation of neutrophil membrane proteins and in the appearance of superoxide anion, following addition of PMA to the cell suspensions. For each response the lag period increased with increasing concentrations of antibody, but the onset of phosphorylation always preceded by a few minutes the initial appearance of superoxide anion.

Original languageEnglish
Pages (from-to)1121-1126
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume140
Issue number3
DOIs
Publication statusPublished - Nov 14 1986

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Phosphorylation
NADPH Oxidase
Surface Antigens
Superoxides
Membrane Proteins
Neutrophils
Chemical activation
Monoclonal Antibodies
Tetradecanoylphorbol Acetate
Antibodies
Macrophages
Suspensions

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Activation of NADPH oxidase and phosphorylation of membrane proteins in human neutrophils : Coordinate inhibition by a surface antigen-directed monoclonal antibody. / Pontremoli, S.; Melloni, E.; Salamino, F.; Sparatore, B.; Michetti, M.; Sacco, O.; Horecker, B. L.

In: Biochemical and Biophysical Research Communications, Vol. 140, No. 3, 14.11.1986, p. 1121-1126.

Research output: Contribution to journalArticle

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