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rdf:type |
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lifeskim:mentions |
umls-concept:C0017337,
umls-concept:C0021469,
umls-concept:C0033384,
umls-concept:C0215848,
umls-concept:C0853879,
umls-concept:C1412925,
umls-concept:C1422819,
umls-concept:C1422820,
umls-concept:C1514562,
umls-concept:C1521761,
umls-concept:C1822686,
umls-concept:C1832648,
umls-concept:C1880239,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2348110,
umls-concept:C2348977
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pubmed:issue |
3
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pubmed:dateCreated |
2010-9-15
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pubmed:abstractText |
Hypoxia-inducible factor-1 (HIF-1) activity is regulated by prolyl hydroxylase (PHD1, PHD2, PHD3) and factor inhibiting HIF-1 (FIH) that target the ? subunit of HIF-1 (HIF-1?) for proteosomal degradation. We hypothesised that the elevated HIF-1? level is due in some tumours to epigenetic silencing by DNA hypermethylation of the promoter region of one or more of the PHDs and FIH genes. The aims were to define the presence or absence of promoter methylation of PHDs and FIH in cell lines of various sources and breast carcinomas and, if present, determine its effect on mRNA and protein expression.
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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/Dioxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/EGLN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/EGLN2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/EGLN3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/HIF1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/HIF1AN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Hypoxia-Inducible Factor 1, alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Procollagen-Proline Dioxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1365-2559
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pubmed:author |
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pubmed:copyrightInfo |
© 2010 Blackwell Publishing Limited.
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pubmed:issnType |
Electronic
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
451-60
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:20727020-Breast Neoplasms,
pubmed-meshheading:20727020-Carcinoma,
pubmed-meshheading:20727020-DNA Methylation,
pubmed-meshheading:20727020-Dioxygenases,
pubmed-meshheading:20727020-Female,
pubmed-meshheading:20727020-Humans,
pubmed-meshheading:20727020-Hypoxia-Inducible Factor 1, alpha Subunit,
pubmed-meshheading:20727020-Mixed Function Oxygenases,
pubmed-meshheading:20727020-Nuclear Proteins,
pubmed-meshheading:20727020-Procollagen-Proline Dioxygenase,
pubmed-meshheading:20727020-RNA, Messenger,
pubmed-meshheading:20727020-Repressor Proteins,
pubmed-meshheading:20727020-Transcription Factors
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pubmed:year |
2010
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pubmed:articleTitle |
DNA methylation analysis of the HIF-1? prolyl hydroxylase domain genes PHD1, PHD2, PHD3 and the factor inhibiting HIF gene FIH in invasive breast carcinomas.
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pubmed:affiliation |
Department of Pathology, Molecular Pathology Research and Development Laboratory, Peter MacCallum Cancer Centre, Melbourne, Vic., Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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