| A novel superoxide-producing NAD(P)H oxidase in kidney. | |
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MedLine Citation:
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PMID: 11032835 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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During phagocytosis, gp91(phox), the catalytic subunit of the phagocyte NADPH oxidase, becomes activated to produce superoxide, a precursor of microbicidal oxidants. Currently increasing evidence suggests that nonphagocytic cells contain similar superoxide-producing oxidases, which are proposed to play crucial roles in various events such as cell proliferation and oxygen sensing for erythropoiesis. Here we describe the cloning of human cDNA that encodes a novel NAD(P)H oxidase, designated NOX4. The NOX4 protein of 578 amino acids exhibits 39% identity to gp91(phox) with special conservation in membrane-spanning regions and binding sites for heme, FAD, and NAD(P)H, indicative of its function as a superoxide-producing NAD(P)H oxidase. The membrane fraction of kidney-derived human embryonic kidney (HEK) 293 cells, expressing NOX4, exhibits NADH- and NADPH-dependent superoxide-producing activities, both of which are inhibited by diphenylene iodonium, an agent known to block oxygen sensing, and decreased in cells expressing antisense NOX4 mRNA. The human NOX4 gene, comprising 18 exons, is located on chromosome 11q14.2-q21, and its expression is almost exclusively restricted to adult and fetal kidneys. In human renal cortex, high amounts of the NOX4 protein are present in distal tubular cells, which reside near erythropoietin-producing cells. In addition, overexpression of NOX4 in cultured cells leads to increased superoxide production and decreased rate of growth. The present findings thus suggest that the novel NAD(P)H oxidase NOX4 may serve as an oxygen sensor and/or a regulator of cell growth in kidney. |
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Authors:
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A Shiose; J Kuroda; K Tsuruya; M Hirai; H Hirakata; S Naito; M Hattori; Y Sakaki; H Sumimoto |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 276 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2001 Jan |
Date Detail:
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Created Date: 2001-03-06 Completed Date: 2001-04-05 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 1417-23 Citation Subset: IM |
Affiliation:
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Department of Molecular and Structural Biology, Kyushu University Graduate School of Medical Science, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/AB041035 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adult Amino Acid Sequence Bacterial Proteins* Cell Line Chromosome Mapping Chromosomes, Human, Pair 11* Cloning, Molecular Exons Expressed Sequence Tags Fetus Gene Expression Regulation, Developmental Gene Expression Regulation, Enzymologic Humans In Situ Hybridization, Fluorescence Karyotyping Kinetics Molecular Sequence Data NADH, NADPH Oxidoreductases / chemistry NADPH Oxidase / chemistry, genetics*, metabolism* Organ Specificity RNA, Messenger / genetics Recombinant Proteins / metabolism Sequence Alignment Sequence Homology, Amino Acid Superoxides / metabolism Transfection |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/RNA, Messenger; 0/Recombinant Proteins; 11062-77-4/Superoxides; EC 1.6.-/NADH, NADPH Oxidoreductases; EC 1.6.3.-/NOX4 protein, human; EC 1.6.3.1/NADPH Oxidase; EC 1.6.99.-/NADPH oxidase 1; EC 1.6.99.-/Nox-2 protein, bacteria |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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