Immunoelectron microscopy shows a clustered distribution of NADPH oxidase components in the human neutrophil plasma membrane

• Published in: Journal of leukocyte biology Vol. 61; no. 3; pp. 303 - 312
• Main Authors: Wientjes, Frans B., Segal, Anthony W., Hartwig, John H.
• Format: Journal Article
• Language: English
• Published: United States Society for Leukocyte Biology 01.03.1997
• Subjects: Antibodies, Monoclonal; Cell Membrane - enzymology; Cytoskeleton - chemistry; flavocytochrome b; GTP-Binding Proteins - analysis; Humans; Membrane Glycoproteins - analysis; Microscopy, Immunoelectron; NADPH Oxidase 2; NADPH Oxidases - chemistry; Neutrophils - enzymology; phorbol myristate acetate; rac GTP-Binding Proteins; small GTP‐binding protein; Staining and Labeling
• ISSN: 0741-5400; 1938-3673
• DOI: 10.1002/jlb.61.3.303

The NADPH oxidase that produces superoxide in professional phagocytic cells is a flavocytochrome b electron transport chain in the membrane, a heterodimer of gp91phox and p22phox, that is activated by a number of cytosolic proteins, including p47phox p67phox, and the small GTP‐binding protein p21rac, 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 p21rac were found together in punctate clusters occupying 0.03–0.1 μm2 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.