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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1996-12-16
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pubmed:abstractText |
The binding of the 1,25-dihydroxyvitamin D3 receptor to the vitamin D response elements (VDREs) in the rat osteocalcin (OSC-DRE), mouse osteopontin (MOP-DRE), rat calbindin D-9k (CaBP-DRE), and human parathyroid hormone genes (PTH-DRE) was studied. Binding of VDR to the three positive VDREs is cooperative. The degree of cooperativity is highest with the calbindin VDRE compared with either the OSC-DRE or the MOP-DRE. This cooperativity is largely absent in the case of the negative element, the PTH-DRE. The VDR binds in order of decreasing affinity to PTH-DRE > OSC-DRE = MOP-DRE > CaBP-DRE. Thus, the greatest affinity is associated with the lowest degree of cooperativity. Further study has revealed that the PTH-VDRE actually consists of two repeat elements like all other VDREs and is not a single six-base sequence. A nuclear factor has also been found that binds downstream from the GGTTCA element in the PTH promoter. The binding site of this factor overlaps the PTH-DRE nucleotide sequence.
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pubmed:grant |
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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/Calcium-Binding Protein, Vitamin...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Probes,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotide Probes,
http://linkedlifedata.com/resource/pubmed/chemical/Osteocalcin,
http://linkedlifedata.com/resource/pubmed/chemical/Osteopontin,
http://linkedlifedata.com/resource/pubmed/chemical/Parathyroid Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitriol,
http://linkedlifedata.com/resource/pubmed/chemical/SPP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Spp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Spp1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin D,
http://linkedlifedata.com/resource/pubmed/chemical/calbindin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
334
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
223-34
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8900396-Animals,
pubmed-meshheading:8900396-Base Sequence,
pubmed-meshheading:8900396-Binding, Competitive,
pubmed-meshheading:8900396-Binding Sites,
pubmed-meshheading:8900396-Calcium-Binding Protein, Vitamin D-Dependent,
pubmed-meshheading:8900396-Cell Nucleus,
pubmed-meshheading:8900396-DNA Probes,
pubmed-meshheading:8900396-DNA-Binding Proteins,
pubmed-meshheading:8900396-Humans,
pubmed-meshheading:8900396-Kinetics,
pubmed-meshheading:8900396-Mice,
pubmed-meshheading:8900396-Oligonucleotide Probes,
pubmed-meshheading:8900396-Osteocalcin,
pubmed-meshheading:8900396-Osteopontin,
pubmed-meshheading:8900396-Parathyroid Hormone,
pubmed-meshheading:8900396-Rats,
pubmed-meshheading:8900396-Receptors, Calcitriol,
pubmed-meshheading:8900396-Sialoglycoproteins,
pubmed-meshheading:8900396-Vitamin D
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pubmed:year |
1996
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pubmed:articleTitle |
Analysis of binding of the 1,25-dihydroxyvitamin D3 receptor to positive and negative vitamin D response elements.
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pubmed:affiliation |
Department of Biochemistry, University of Wisconsin-Madison, 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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