| pubmed-article:15878343 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15878343 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
| pubmed-article:15878343 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:15878343 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15878343 | pubmed:dateCreated | 2005-5-9 | lld:pubmed |
| pubmed-article:15878343 | pubmed:abstractText | Hypoxia-inducible factor-1 (HIF-1), the master regulator of transcriptional responses to reduced oxygen tension (hypoxia) in mammalian cells, consists of one HIF-1alpha and one HIF-1beta subunit. In normoxia, HIF-1alpha subunits are hydroxylated on specific proline residues; modifications that signal ubiquitination and degradation of HIF-1alpha by the proteasome. To test the effect of saturating HIF-1alpha degradation, we generated a construct, denoted the saturating domain (SD), based on a region surrounding proline 564 (Pro564) in HIF-1alpha. Expression of the SD led to accumulation of endogenous HIF-1alpha proteins in nuclei of normoxic cells. The induced HIF-1alpha was functional as it activated expression from a hypoxia-regulated reporter gene and from the endogenous vascular endothelial growth facor-a (Vegf-a) and carbonic anhydrase 9 (Ca9) genes. The effect of the SD was dependent on Pro564 since a mutated SD, in which Pro564 had been replaced by a glycine residue, failed to bind the von Hippel-Lindau protein (pVHL) and to stabilise HIF-1alpha. Treatment of cells with the prolylhydroxylase inhibitor dimethyloxalylglycine, or the proteasome inhibitor MG-132, mimicked the effect of the SD. In conclusion, we show that blocking HIF-1alpha degradation, either by saturation, or inhibition of prolyl hydroxylases or proteosomal degradation, leads to nuclear localisation of active HIF-1alpha proteins. | lld:pubmed |
| pubmed-article:15878343 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15878343 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15878343 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15878343 | pubmed:month | May | lld:pubmed |
| pubmed-article:15878343 | pubmed:issn | 0014-4827 | lld:pubmed |
| pubmed-article:15878343 | pubmed:author | pubmed-author:HäggMariaM | lld:pubmed |
| pubmed-article:15878343 | pubmed:author | pubmed-author:WennströmStef... | lld:pubmed |
| pubmed-article:15878343 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15878343 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15878343 | pubmed:volume | 306 | lld:pubmed |
| pubmed-article:15878343 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15878343 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15878343 | pubmed:pagination | 180-91 | lld:pubmed |
| pubmed-article:15878343 | pubmed:dateRevised | 2007-5-2 | lld:pubmed |
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| pubmed-article:15878343 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15878343 | pubmed:articleTitle | Activation of hypoxia-induced transcription in normoxia. | lld:pubmed |
| pubmed-article:15878343 | pubmed:affiliation | Department of Genetics and Pathology, Rudbeck Laboratory, Dag Hammarskjölds väg 20, S-751 85 Uppsala, Sweden. | lld:pubmed |
| pubmed-article:15878343 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15878343 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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