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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1994-10-6
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pubmed:abstractText |
The binding of transcription factor AP-1 and vitamin D receptor (VDR) to the composite AP-1 plus vitamin-D-responsive promoter region (AP-1 + VDRE) of the human osteocalcin gene was characterized in osteocalcin-producing (MG-63) and non-producing (U2-Os, SaOs-2) human osteosarcoma cell lines. In mobility-shift assays with AP-1 + VDRE, AP-1, and VDRE probes and nuclear extracts from these cells, one AP-1-specific and two VDR-specific (fast and slow mobility) interactions were observed. Characterization of the complexes indicated that AP-1 and VDR do not bind simultaneously to the AP-1 + VDRE oligonucleotide. Intensity of the complexes was greatly influenced by cell density: in MG-63 and SaOs-2 cells, AP-1 binding was strong during the proliferative period disappearing at confluency whereas, in U2-Os cells, AP-1 binding was prominent also at the confluent stage. Furthermore, MG-63 cells possessed the faster migrating VDR complex at all stages of confluency whereas, in U2-Os and SaOs-2 cells, it was very weak or absent. There were no detectable differences in the levels of VDR protein between these cell lines. In U2-Os cells, the level of c-jun mRNA was higher than in the other two cell lines, whereas none of these cell lines exhibited detectable levels of c-fos mRNA at the confluent stage. Exogenous c-Jun protein effectively blocked the VDR-DNA interaction. Further, all these cell lines expressed mRNA for retinoid X receptor alpha (RXR alpha), the factor suggested to be required for the VDR-DNA interaction. The presence of an accessory factor in the VDR-DNA complexes was indirectly shown by treatment of the cells with 9-cis retinoic acid and by cycloheximide. Both treatments reduced VDR binding without affecting the VDR protein level. These results suggest that AP-1 interferes with VDR binding to the AP-1 + VDRE element and that the vitamin D responsiveness of the osteocalcin gene correlates with weak AP-1 binding and strong binding of the faster migrating VDR complex.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Osteocalcin,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fos,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-jun,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitriol,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
224
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-20
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8076631-Base Sequence,
pubmed-meshheading:8076631-Blotting, Northern,
pubmed-meshheading:8076631-Blotting, Western,
pubmed-meshheading:8076631-Cycloheximide,
pubmed-meshheading:8076631-DNA,
pubmed-meshheading:8076631-Gene Expression,
pubmed-meshheading:8076631-Humans,
pubmed-meshheading:8076631-Molecular Sequence Data,
pubmed-meshheading:8076631-Osteocalcin,
pubmed-meshheading:8076631-Osteosarcoma,
pubmed-meshheading:8076631-Polymerase Chain Reaction,
pubmed-meshheading:8076631-Promoter Regions, Genetic,
pubmed-meshheading:8076631-Proto-Oncogene Proteins c-fos,
pubmed-meshheading:8076631-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:8076631-RNA, Messenger,
pubmed-meshheading:8076631-Receptors, Calcitriol,
pubmed-meshheading:8076631-Transcription, Genetic,
pubmed-meshheading:8076631-Tretinoin,
pubmed-meshheading:8076631-Tumor Cells, Cultured
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pubmed:year |
1994
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pubmed:articleTitle |
Functional interference between AP-1 and the vitamin D receptor on osteocalcin gene expression in human osteosarcoma cells.
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pubmed:affiliation |
Department of Biochemistry and Biotechnology and A. I. Virtanen Institute, University of Kuopio, Finland.
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pubmed:publicationType |
Journal Article,
Comparative Study
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