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PMID: 15293055 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Assembly of the phagocyte NADPH oxidase.

Histochemistry and cell biology ·Vol. 122 ·No. 4 ·2004-10-00 ·Pages 277-91

Nauseef WM

Abstract

Stimulated phagocytes undergo a burst in respiration whereby molecular oxygen is converted to superoxide anion through the action of an NADPH-dependent oxidase. The multicomponent phagocyte oxidase is unassembled and inactive in resting cells but assembles at the plasma or phagosomal membrane upon phagocyte activation. Oxidase components include flavocytochrome b558, an integral membrane heterodimer comprised of gp91phox and p22phox, and three cytosolic proteins, p47phox, p67phox, and Rac1 or Rac2, depending on the species and phagocytic cell. In a sense, the phagocyte oxidase is spatially regulated, with critical elements segregated in the membrane and cytosol but ready to undergo nearly immediate assembly and activation in response to stimulation. To achieve such spatial regulation, the individual components in the resting phagocyte adopt conformations that mask potentially interactive structural domains that might mediate productive intermolecular associations and oxidase assembly. In response to stimulation, post-translational modifications of the oxidase components release these constraints and thereby render potential interfaces accessible and interactive, resulting in translocation of the cytosolic elements to the membrane where the functional oxidase is assembled and active. This review summarizes data on the structural features of the phagocyte oxidase components and on the agonist-dependent conformational rearrangements that contribute to oxidase assembly and activation.

MeSH Terms
Animals Cytochrome b Group/metabolism Humans NADPH Oxidases/metabolism Oxygen/metabolism Phagocytes/enzymology Phosphoproteins/metabolism Protein Binding Protein Conformation Superoxides/metabolism rac GTP-Binding Proteins/metabolism rac1 GTP-Binding Protein/metabolism
Chemicals
Cytochrome b Group Phosphoproteins Superoxides cytochrome b558 NADPH Oxidases rac2 GTP-binding protein rac GTP-Binding Proteins rac1 GTP-Binding Protein Oxygen
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Nauseef William M
Inflammation Program and Department of Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, D160 MTF, 2501 Crosspark Road, Coralville, IA 52241, USA. [email protected]
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Article Info
Journal
Histochemistry and cell biology
Abbr.
Histochem Cell Biol
ISSN
0948-6143
DOI
10.1007/s00418-004-0679-8
Email
[email protected]
Published
2004-10-00
Epub
2004-00-04
Pages
277-91
Language
English
Region
Germany
NLM ID
9506663
Subset
IM
Grants
BLRD VA · I01 BX000513 · United States
NIAID NIH HHS · AI34879 · United States
NIAID NIH HHS · AI44642 · United States
NHLBI NIH HHS · HL53592 · United States
External Links
PubMed source DOI: 10.1007/s00418-004-0679-8 View journal details
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