| pubmed-article:12606543 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12606543 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12606543 | lifeskim:mentions | umls-concept:C0009148 | lld:lifeskim |
| pubmed-article:12606543 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12606543 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:12606543 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:12606543 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:12606543 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:12606543 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:12606543 | pubmed:dateCreated | 2003-4-28 | lld:pubmed |
| pubmed-article:12606543 | pubmed:abstractText | The hypoxia-inducible factor (HIF) activates the expression of genes that contain a hypoxia response element. The alpha-subunits of the HIF transcription factors are degraded by proteasomal pathways during normoxia but are stabilized under hypoxic conditions. The von Hippel-Lindau protein (pVHL) mediates the ubiquitination and rapid degradation of HIF-alpha (including HIF-1alpha and HIF-2alpha). Post-translational hydroxylation of a proline residue in the oxygen-dependent degradation (ODD) domain of HIF-alpha is required for the interaction between HIF and VHL. It has previously been established that cobalt mimics hypoxia and causes accumulation of HIF-1alpha and HIF-2alpha. However, little is known about the mechanism by which this occurs. In an earlier study, we demonstrated that cobalt binds directly to the ODD domain of HIF-2alpha. Here we provide the first evidence that cobalt inhibits pVHL binding to HIF-alpha even when HIF-alpha is hydroxylated. Deletion of 17 amino acids within the ODD domain of HIF-2alpha that are required for pVHL binding prevented the binding of cobalt and stabilized HIF-2alpha during normoxia. These findings show that cobalt mimics hypoxia, at least in part, by occupying the VHL-binding domain of HIF-alpha and thereby preventing the degradation of HIF-alpha. | lld:pubmed |
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| pubmed-article:12606543 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12606543 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12606543 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12606543 | pubmed:month | May | lld:pubmed |
| pubmed-article:12606543 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12606543 | pubmed:author | pubmed-author:CoxH BHB | lld:pubmed |
| pubmed-article:12606543 | pubmed:author | pubmed-author:FergusonTsune... | lld:pubmed |
| pubmed-article:12606543 | pubmed:author | pubmed-author:MillhornDavid... | lld:pubmed |
| pubmed-article:12606543 | pubmed:author | pubmed-author:HilliardGeorg... | lld:pubmed |
| pubmed-article:12606543 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12606543 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:12606543 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12606543 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12606543 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12606543 | pubmed:pagination | 15911-6 | lld:pubmed |
| pubmed-article:12606543 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12606543 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12606543 | pubmed:articleTitle | Cobalt inhibits the interaction between hypoxia-inducible factor-alpha and von Hippel-Lindau protein by direct binding to hypoxia-inducible factor-alpha. | lld:pubmed |
| pubmed-article:12606543 | pubmed:affiliation | Genome Research Institute, University of Cincinnati, 231 Albert Sabin Way, Cincinnati, OH 45267-0505, USA. | lld:pubmed |
| pubmed-article:12606543 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12606543 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12606543 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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