| pubmed-article:12925778 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C0028128 | lld:lifeskim |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C0033384 | lld:lifeskim |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C0965644 | lld:lifeskim |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C1333897 | lld:lifeskim |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C1704838 | lld:lifeskim |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:12925778 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:12925778 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:12925778 | pubmed:dateCreated | 2003-8-19 | lld:pubmed |
| pubmed-article:12925778 | pubmed:abstractText | Hypoxia inducible factor-1 (HIF-1) is the master regulator of metabolic adaptation to hypoxia. It is appreciated that HIF-1alpha accumulation is achieved under normoxic conditions by e.g., nitric oxide. We determined molecular mechanisms of HIF-1alpha accumulation under the impact of S-nitrosoglutathione (GSNO). In human embryonic kidney cells GSNO provoked nuclear accumulation of HIF-1alpha. This appeared unrelated to gene transcription and protein translation, thus pointing to inhibition of HIF-1alpha degradation. Indeed, GSNO as well as the hypoxia mimic CoCl2 decreased ubiquitination of HIF-1alpha and GSNO-induced HIF-1alpha failed to coimmunoprecipitate with pVHL (von Hippel Lindau protein). Considering that HIF-1alpha-pVHL interactions require prolyl hydroxylation of HIF-1alpha, we went on to demonstrate inhibition of HIF-1alpha prolyl hydroxylases (PHDs) by GSNO. In vitro HIF-1alpha-pVHL interactions revealed that GSNO dose-dependently inhibits PHD activity but not the interaction of a synthetic peptide resembling the hydroxylated oxygen-dependent degradation domain of HIF-1alpha with pVHL. We conclude that GSNO-attenuated prolyl hydroxylase activity accounts for HIF-1alpha accumulation under conditions of NO formation during normoxia and that PHD activity is subject to regulation by NO. | lld:pubmed |
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| pubmed-article:12925778 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12925778 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12925778 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12925778 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12925778 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12925778 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12925778 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:12925778 | pubmed:author | pubmed-author:ZhouJieJ | lld:pubmed |
| pubmed-article:12925778 | pubmed:author | pubmed-author:JelkmannWolfg... | lld:pubmed |
| pubmed-article:12925778 | pubmed:author | pubmed-author:BrüneBernhard... | lld:pubmed |
| pubmed-article:12925778 | pubmed:author | pubmed-author:MetzenEricE | lld:pubmed |
| pubmed-article:12925778 | pubmed:author | pubmed-author:FandreyJoachi... | lld:pubmed |
| pubmed-article:12925778 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12925778 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:12925778 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12925778 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12925778 | pubmed:pagination | 3470-81 | lld:pubmed |
| pubmed-article:12925778 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12925778 | pubmed:meshHeading | pubmed-meshheading:12925778... | lld:pubmed |
| pubmed-article:12925778 | pubmed:meshHeading | pubmed-meshheading:12925778... | lld:pubmed |
| pubmed-article:12925778 | pubmed:meshHeading | pubmed-meshheading:12925778... | lld:pubmed |
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| pubmed-article:12925778 | pubmed:meshHeading | pubmed-meshheading:12925778... | lld:pubmed |
