Linked Life Data

10536369

Source:http://linkedlifedata.com/resource/pubmed/id/10536369

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-1-24
pubmed:abstractText
The vitamin D receptor (VDR) is a transcription factor believed to function as a heterodimer with the retinoid X receptor (RXR). However, it was reported [Schräder et al., 1994] that, on putative vitamin D response elements (VDREs) within the rat 9k and mouse 28k calcium binding protein genes (rCaBP 9k and mCaBP 28k), VDR and thyroid hormone receptor (TR) form heterodimers that transactivate in response to both 1,25-dihydroxyvitamin D(3) (1,25(OH)(2)D(3)) and triiodothyronine (T(3)). We, therefore, examined associations of these receptors on the putative rCaBP 9k and mCaBP 28k VDREs, as well as on established VDREs from the rat osteocalcin (rOC) and mouse osteopontin (mOP) genes, plus the thyroid hormone response element (TRE) from the rat myosin heavy chain (rMHC) gene. In gel mobility shift assays, we found no evidence for VDR-TR heterodimer interaction with any tested element. Further, employing these hormone response elements linked to reporter genes in transfected cells, VDR and TR mediated responses to their cognate ligands only from the rOC/mOP and rMHC elements, respectively, while the CaBP elements were unresponsive to any combination of ligand(s). Utilizing the rOC and mOP VDREs, two distinct repressive actions of TR on VDR-mediated signaling were demonstrated: a T(3)-independent action, presumably via direct TR-RXR competition for DNA binding, and a T(3)-dependent repression, likely by diversion of limiting RXR from VDR-RXR toward the formation of TR-RXR heterodimers. The relative importance of these two mechanisms differed in a response element-specific manner. These results may provide a partial explanation for the observed association between hyperthyroidism and bone demineralization/osteoporosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0730-2312
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
462-80
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10536369-Animals, pubmed-meshheading:10536369-Base Sequence, pubmed-meshheading:10536369-COS Cells, pubmed-meshheading:10536369-DNA, pubmed-meshheading:10536369-DNA, Complementary, pubmed-meshheading:10536369-Dimerization, pubmed-meshheading:10536369-Humans, pubmed-meshheading:10536369-Ligands, pubmed-meshheading:10536369-Mice, pubmed-meshheading:10536369-Models, Biological, pubmed-meshheading:10536369-Protein Structure, Quaternary, pubmed-meshheading:10536369-Rats, pubmed-meshheading:10536369-Receptor Cross-Talk, pubmed-meshheading:10536369-Receptors, Calcitriol, pubmed-meshheading:10536369-Receptors, Retinoic Acid, pubmed-meshheading:10536369-Receptors, Thyroid Hormone, pubmed-meshheading:10536369-Recombinant Proteins, pubmed-meshheading:10536369-Retinoid X Receptors, pubmed-meshheading:10536369-Transcription Factors, pubmed-meshheading:10536369-Transcriptional Activation
pubmed:year
1999
pubmed:articleTitle
Vitamin D receptor displays DNA binding and transactivation as a heterodimer with the retinoid X receptor, but not with the thyroid hormone receptor.
pubmed:affiliation
Department of Biochemistry, College of Medicine, The University of Arizona, Tucson, Arizona 85724, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.