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Immunoelectron microscopy shows a clustered distribution of NADPH oxidase components in the human neutrophil plasma membrane
Author(s) -
Wientjes Frans B.,
Segal Anthony W.,
Hartwig John H.
Publication year - 1997
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.61.3.303
Subject(s) - nadph oxidase , immunoelectron microscopy , immunolabeling , p22phox , cytosol , cytoplasm , biology , membrane , microbiology and biotechnology , biophysics , biochemistry , reactive oxygen species , enzyme , immunology , immunohistochemistry
The NADPH oxidase that produces superoxide in professional phagocytic cells is a flavocytochrome b electron transport chain in the membrane, a heterodimer of gp91 phox and p22 phox , that is activated by a number of cytosolic proteins, including p47 phox p67 phox , and the small GTP‐binding protein p21 rac , which translocate to the membrane and attach to the flavocytochrome on activation. The components of this oxidase were localized on the cytoplasmic surface of the plasma membrane of adherent unroofed neutrophils by immunolabeling. Components of the NADPH oxidase and p21 rac were found together in punctate clusters occupying 0.03–0.1 μm 2 of the cytoplasmic surface of the plasma membrane where the density of labeling of the cytosolic components was increased after stimulation with phorbol myristate acetate. J. Leukoc. Biol . 61: 303–312; 1997.