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- W1847182830 endingPage "483" @default.
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- W1847182830 abstract "This chapter reviews current knowledge of the structure and function of the nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and shows how much of this information has been revealed through an understanding of the molecular pathology of chronic granulomatous disease (CGD). Components of the NADPH oxidase include the flavocytochrome b electron transport chain and cytosolic factors. The electron transporting component is a flavocytochrome that is activated in the wall of the phagocytic vacuole. It is a α1β1 heterodimer. The NADPH oxidase generates superoxide in the professional phagocytic cells, neutrophils, monocytes and macrophages, and a variety of other cells derived from the myeloid lineage as well as B lymphocytes. The superoxide is generated by a short electron transport chain incorporated within a flavocytochrome that spans the membrane of the wall of the phagocytic vacuole. This flavocytochrome is the best characterized of a newly described family that transport electrons across the plasma membrane of plants, yeast, and higher animals. The flavocytochrome is selectively activated in this region of the plasma membrane by a group of specialized cytoplasmic phox proteins under the regulation of various signal transduction pathways. Deficiency of superoxide production because of genetic lesions resulting in deficiencies of the flavocytochrome b, or cytosolic phox proteins, results in CGD. This syndrome is characterized by an abnormal predisposition to infection with bacteria and fungi, and to an abnormal inflammatory response." @default.
- W1847182830 created "2016-06-24" @default.
- W1847182830 creator A5025311351 @default.
- W1847182830 creator A5039715775 @default.
- W1847182830 creator A5041426819 @default.
- W1847182830 creator A5091627593 @default.
- W1847182830 date "1999-01-01" @default.
- W1847182830 modified "2023-10-13" @default.
- W1847182830 title "Components and organization of the nadph oxidase of phagocytic cells" @default.
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