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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1995-4-18
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pubmed:abstractText |
The human neutrophil NADPH oxidase-associated H+ channel acts as a charge compensator for the electrogenic generation of superoxide (O2-.). The expression of the channel activity was found to increase in parallel with that of the stimulatable generation of O2-. in differentiated HL60 cells. HL60 cells induced to differentiate in the presence of succinyl acetone (a inhibitor of heme synthesis) were unable to generate O2-., failed to express p22-phox but retained H+ channel activity. EBV transformed B lymphocyte cell lines from normal and CGD patients lacking expression of either p47-phox or p67-phox all expressed unaltered channel activity; however, the activity was completely absent in the lymphocyte cell line lacking gp91-phox. CHO cells and undifferentiated HL60 cells transfected with gp91-phox cDNA expressed H+ channel activity correlating with the expression of gp91-phox. We therefore conclude that the large subunit of the NADPH oxidase cytochrome b (gp91-phox) is the arachidonate activable H+ channel of human neutrophils.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/CYBA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CYBB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Hygromycin B,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proton Pumps,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/neutrophil cytosolic factor 1
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5909-16
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7890722-Animals,
pubmed-meshheading:7890722-Arachidonic Acid,
pubmed-meshheading:7890722-B-Lymphocytes,
pubmed-meshheading:7890722-Base Sequence,
pubmed-meshheading:7890722-CHO Cells,
pubmed-meshheading:7890722-Cell Differentiation,
pubmed-meshheading:7890722-Cell Line,
pubmed-meshheading:7890722-Cell Line, Transformed,
pubmed-meshheading:7890722-Cricetinae,
pubmed-meshheading:7890722-DNA, Complementary,
pubmed-meshheading:7890722-Herpesvirus 4, Human,
pubmed-meshheading:7890722-Humans,
pubmed-meshheading:7890722-Hydrogen-Ion Concentration,
pubmed-meshheading:7890722-Hygromycin B,
pubmed-meshheading:7890722-Kinetics,
pubmed-meshheading:7890722-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:7890722-Membrane Glycoproteins,
pubmed-meshheading:7890722-Membrane Transport Proteins,
pubmed-meshheading:7890722-Models, Biological,
pubmed-meshheading:7890722-Molecular Sequence Data,
pubmed-meshheading:7890722-NADH, NADPH Oxidoreductases,
pubmed-meshheading:7890722-NADPH Dehydrogenase,
pubmed-meshheading:7890722-NADPH Oxidase,
pubmed-meshheading:7890722-Neutrophils,
pubmed-meshheading:7890722-Phosphoproteins,
pubmed-meshheading:7890722-Plasmids,
pubmed-meshheading:7890722-Proton Pumps,
pubmed-meshheading:7890722-Recombinant Proteins,
pubmed-meshheading:7890722-Restriction Mapping,
pubmed-meshheading:7890722-Superoxides,
pubmed-meshheading:7890722-Tetradecanoylphorbol Acetate,
pubmed-meshheading:7890722-Transfection,
pubmed-meshheading:7890722-Tumor Cells, Cultured
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pubmed:year |
1995
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pubmed:articleTitle |
The arachidonate-activable, NADPH oxidase-associated H+ channel. Evidence that gp91-phox functions as an essential part of the channel.
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pubmed:affiliation |
Department of Biochemistry, School of Medical Sciences, University of Bristol, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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