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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1999-6-15
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pubmed:abstractText |
Nitric oxide (NO) release as a result of activation of inducible NO synthase (iNOS) can be sustained and reach cytotoxic concentrations. It is unknown whether cells possess intrinsic systems to attenuate NO-mediated cytotoxicity. One potential system is the heme oxygenase-1 (HO-1) enzyme because it catabolizes heme and therefore may limit synthesis or availability of iNOS. These studies were undertaken to explore whether NO derived from NO donors or from activation of iNOS induces HO-1 in mesangial cells.
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pubmed:grant |
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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/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Cytotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1,
http://linkedlifedata.com/resource/pubmed/chemical/Hmox1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Nos2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nos2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/omega-N-Methylarginine
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0085-2538
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1734-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10231435-Animals,
pubmed-meshheading:10231435-Antineoplastic Agents,
pubmed-meshheading:10231435-Blotting, Northern,
pubmed-meshheading:10231435-Blotting, Western,
pubmed-meshheading:10231435-Cells, Cultured,
pubmed-meshheading:10231435-Cytotoxins,
pubmed-meshheading:10231435-Enzyme Inhibitors,
pubmed-meshheading:10231435-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:10231435-Glomerular Mesangium,
pubmed-meshheading:10231435-Heme Oxygenase (Decyclizing),
pubmed-meshheading:10231435-Heme Oxygenase-1,
pubmed-meshheading:10231435-Interferon-gamma,
pubmed-meshheading:10231435-Lipopolysaccharides,
pubmed-meshheading:10231435-Membrane Proteins,
pubmed-meshheading:10231435-Mice,
pubmed-meshheading:10231435-Nitric Oxide,
pubmed-meshheading:10231435-Nitric Oxide Synthase,
pubmed-meshheading:10231435-Nitric Oxide Synthase Type II,
pubmed-meshheading:10231435-RNA, Messenger,
pubmed-meshheading:10231435-Rats,
pubmed-meshheading:10231435-Rats, Sprague-Dawley,
pubmed-meshheading:10231435-omega-N-Methylarginine
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pubmed:year |
1999
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pubmed:articleTitle |
Nitric oxide induces heme oxygenase-1 gene expression in mesangial cells.
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pubmed:affiliation |
Department of Medicine, Medical College of Wisconsin, Milwaukee, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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