pubmed-article:8673472 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8673472 | lifeskim:mentions | umls-concept:C0897757 | lld:lifeskim |
pubmed-article:8673472 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
pubmed-article:8673472 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:8673472 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:8673472 | pubmed:dateCreated | 1996-8-15 | lld:pubmed |
pubmed-article:8673472 | pubmed:abstractText | In intact neutrophils, phorbol ester treatment activates the respiratory burst oxidase, the enzyme responsible for O2-production by phagocytes. This effect is thought to be dependent on protein kinase C and on the phosphorylation of p47phox. In this paper, we report that protein kinase C activates the respiratory burst oxidase in a cell-free system consisting of isolated neutrophil cytosol and membrane. Oxidase activation required a highly active protein kinase C, recombinant p47phow and ATP, and was inhibited by the protein kinase C inhibitors H-7 and GF-109203X. PERIl depletion of cytosolic ATP by dialysis reduced oxidase activation by over 50% In contrast, neither protein kinase C inhibitors nor ATP depletion affected oxidase activation by SDS. These findings strongly suggest that in the cell-free system, the oxidase can be activated by the phosphorylation of p47phox. | lld:pubmed |
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pubmed-article:8673472 | pubmed:language | eng | lld:pubmed |
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pubmed-article:8673472 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8673472 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8673472 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8673472 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8673472 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8673472 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8673472 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8673472 | pubmed:issn | 1079-9796 | lld:pubmed |
pubmed-article:8673472 | pubmed:author | pubmed-author:BabiorB MBM | lld:pubmed |
pubmed-article:8673472 | pubmed:author | pubmed-author:ParkJ WJW | lld:pubmed |
pubmed-article:8673472 | pubmed:author | pubmed-author:RuediJ MJM | lld:pubmed |
pubmed-article:8673472 | pubmed:author | pubmed-author:el-BennaJJ | lld:pubmed |
pubmed-article:8673472 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8673472 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:8673472 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8673472 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8673472 | pubmed:pagination | 201-6 | lld:pubmed |
pubmed-article:8673472 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:8673472 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:8673472 | pubmed:articleTitle | Cell-free activation of the respiratory burst oxidase by protein kinase C. | lld:pubmed |
pubmed-article:8673472 | pubmed:affiliation | Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037, USA. | lld:pubmed |
pubmed-article:8673472 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8673472 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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