| pubmed-article:7890722 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7890722 | lifeskim:mentions | umls-concept:C0027303 | lld:lifeskim |
| pubmed-article:7890722 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:7890722 | lifeskim:mentions | umls-concept:C1413844 | lld:lifeskim |
| pubmed-article:7890722 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:7890722 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:7890722 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:7890722 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:7890722 | pubmed:dateCreated | 1995-4-18 | lld:pubmed |
| pubmed-article:7890722 | 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. | lld:pubmed |
| pubmed-article:7890722 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7890722 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7890722 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7890722 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7890722 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7890722 | pubmed:author | pubmed-author:HendersonL... | lld:pubmed |
| pubmed-article:7890722 | pubmed:author | pubmed-author:ChappellJ BJB | lld:pubmed |
| pubmed-article:7890722 | pubmed:author | pubmed-author:BantingGG | lld:pubmed |
| pubmed-article:7890722 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7890722 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:7890722 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7890722 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7890722 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7890722 | pubmed:pagination | 5909-16 | lld:pubmed |
| pubmed-article:7890722 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7890722 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7890722 | pubmed:articleTitle | The arachidonate-activable, NADPH oxidase-associated H+ channel. Evidence that gp91-phox functions as an essential part of the channel. | lld:pubmed |
| pubmed-article:7890722 | pubmed:affiliation | Department of Biochemistry, School of Medical Sciences, University of Bristol, United Kingdom. | lld:pubmed |
| pubmed-article:7890722 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7890722 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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