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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6 Suppl
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pubmed:dateCreated |
1995-7-18
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pubmed:abstractText |
Recent studies have identified a heterodimer of the vitamin D receptor (VDR) and the retinoid X receptor (RXR) as the active complex for mediating positive transcriptional effects of 1,25-dihydroxyvitamin D3 [1,25(OH)2D3], the active hormonal form of vitamin D. The VDR-RXR heterodimer has been shown to bind to direct repeat vitamin D-responsive elements (VDREs) upstream of positively controlled genes in the target tissues for vitamin D, including bone (osteocalcin, osteopontin, and beta 3 integrin), kidney (24-hydroxylase) and intestine (calbindin). Residues that participate in heterodimer formation have been identified in the C-terminal hormone-binding domain by analysis of VDR mutants. The role of the 1,25(OH)2D3 ligand in transcriptional activation by the VDR-RXR heterodimer is not entirely clear, but studies of two natural VDR mutants suggest that the binding of both hormone and RXR are required to induce a receptor conformation that is competent to activate transcription. A final level of complexity is added by recent observations that VDR is modified by phosphorylation. Thus, the VDR-mediated action of 1,25(OH)2D3 is now known to involve multiple factors that may provide a conceptual basis for future understanding of the tissue-specific genomic effects of 1,25(OH)2D3.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcitriol,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitriol,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoid X Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin A
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-3166
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
125
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1690S-1694S
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7782928-Animals,
pubmed-meshheading:7782928-Base Sequence,
pubmed-meshheading:7782928-Calcitriol,
pubmed-meshheading:7782928-Humans,
pubmed-meshheading:7782928-Molecular Sequence Data,
pubmed-meshheading:7782928-Receptors, Calcitriol,
pubmed-meshheading:7782928-Receptors, Retinoic Acid,
pubmed-meshheading:7782928-Retinoid X Receptors,
pubmed-meshheading:7782928-Transcription Factors,
pubmed-meshheading:7782928-Transcriptional Activation,
pubmed-meshheading:7782928-Vitamin A
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pubmed:year |
1995
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pubmed:articleTitle |
Genomic actions of 1,25-dihydroxyvitamin D3.
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pubmed:affiliation |
Department of Biochemistry, University of Arizona College of Medicine, Tucson 85724, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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