| pubmed-article:16507982 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16507982 | lifeskim:mentions | umls-concept:C0694897 | lld:lifeskim |
| pubmed-article:16507982 | lifeskim:mentions | umls-concept:C1512474 | lld:lifeskim |
| pubmed-article:16507982 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:16507982 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:16507982 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:16507982 | lifeskim:mentions | umls-concept:C2266853 | lld:lifeskim |
| pubmed-article:16507982 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:16507982 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:16507982 | pubmed:dateCreated | 2006-3-1 | lld:pubmed |
| pubmed-article:16507982 | pubmed:abstractText | Adaptation to hypoxic microenvironment is critical for tumor survival and metastatic spread. Hypoxia-inducible factor 1alpha (HIF-1alpha) plays a key role in this adaptation by stimulating the production of proangiogenic factors and inducing enzymes necessary for anaerobic metabolism. Histone deacetylase inhibitors (HDACIs) produce a marked inhibition of HIF-1alpha expression and are currently in clinical trials partly based on their potent antiangiogenic effects. Although it has been postulated that HDACIs affect HIF-1alpha expression by enhancing its interactions with VHL (von Hippel Lindau), thus promoting its ubiquitination and degradation, the actual mechanisms by which HDACIs decrease HIF-1alpha levels are not clear. Here, we present data indicating that HDACIs induce the proteasomal degradation of HIF-1alpha by a mechanism that is independent of VHL and p53 and does not require the ubiquitin system. This degradation pathway involves the enhanced interaction of HIF-1alpha with HSP70 and is secondary to a disruption of the HSP70/HSP90 axis function that appears mediated by the activity of HDAC-6. | lld:pubmed |
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| pubmed-article:16507982 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16507982 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16507982 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16507982 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16507982 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16507982 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16507982 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:16507982 | pubmed:author | pubmed-author:SangNianliN | lld:pubmed |
| pubmed-article:16507982 | pubmed:author | pubmed-author:CaroJaimeJ | lld:pubmed |
| pubmed-article:16507982 | pubmed:author | pubmed-author:ZhaoLinL | lld:pubmed |
| pubmed-article:16507982 | pubmed:author | pubmed-author:KongXianguoX | lld:pubmed |
| pubmed-article:16507982 | pubmed:author | pubmed-author:LiangDongming... | lld:pubmed |
| pubmed-article:16507982 | pubmed:author | pubmed-author:FathDonnaD | lld:pubmed |
| pubmed-article:16507982 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16507982 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:16507982 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16507982 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16507982 | pubmed:pagination | 2019-28 | lld:pubmed |
| pubmed-article:16507982 | pubmed:dateRevised | 2011-6-13 | lld:pubmed |
| pubmed-article:16507982 | pubmed:meshHeading | pubmed-meshheading:16507982... | lld:pubmed |
| pubmed-article:16507982 | pubmed:meshHeading | pubmed-meshheading:16507982... | lld:pubmed |
