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dc.contributor.authorAslam, Fauzia
dc.contributor.authorMcCabe, Laura R.
dc.contributor.authorFrenkel, Baruch
dc.contributor.authorVan Wijnen, Andre J.
dc.contributor.authorStein, Gary S.
dc.contributor.authorLian, Jane B.
dc.contributor.authorStein, Janet L.
dc.date2022-08-11T08:08:59.000
dc.date.accessioned2022-08-23T16:14:48Z
dc.date.available2022-08-23T16:14:48Z
dc.date.issued1999-01-14
dc.date.submitted2008-07-02
dc.identifier.citation<p>Endocrinology. 1999 Jan;140(1):63-70.</p>
dc.identifier.issn0013-7227 (Print)
dc.identifier.doi10.1210/endo.140.1.6429
dc.identifier.pmid9886808
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33947
dc.description.abstractResponsiveness of genes to steroid hormones is a complex process involving synergistic and/or antagonistic interactions between specific receptors and other nonreceptor transcription factors. Thus, DNA recognition elements for steroid hormone receptors are often located among binding sites for other trans-acting factors. The hormonal form of vitamin D, 1,25-dihydroxyvitamin D3, stimulates transcription of the tissue-specific osteocalcin (OC) gene in osteoblastic cells. The rat OC vitamin D response element contains an internal acitvating protein-1 (AP-1) site. Here, we report for the first time that this AP-1 site is critical for the transcriptional enhancement of rat osteocalcin gene expression mediated by vitamin D. Precise mutations were introduced either in the steroid half-elements or in the internal AP-1 sequences. One mutation within the internal AP-1 site retained vitamin D receptor/retinoid X receptor binding equivalent to that of the wild-type sequence, but resulted in complete loss of vitamin D inducibility of the OC promoter. These results suggest a functional interaction between the hormone receptor and nuclear oncoproteins at the rat OC vitamin D response element. This cooperation of activities may have important consequences in physiological regulation of osteocalcin transcription during osteoblast differentiation and bone tissue development in vivo.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9886808&dopt=Abstract ">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1210/endo.140.1.6429
dc.subjectAnimals; DNA; Humans; Inhibitor of Apoptosis Proteins; Osteocalcin; Promoter Regions (Genetics); Rats; Receptors, Calcitriol; Receptors, Retinoic Acid; Retinoid X Receptors; *Signal Transduction; Trans-Activation (Genetics); Transcription Factor AP-1; Transcription Factors; Transcription, Genetic; Transfection; Tumor Cells, Cultured; Viral Proteins
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleAP-1 and vitamin D receptor (VDR) signaling pathways converge at the rat osteocalcin VDR element: requirement for the internal activating protein-1 site for vitamin D-mediated trans-activation
dc.typeJournal Article
dc.source.journaltitleEndocrinology
dc.source.volume140
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/60
dc.identifier.contextkey542472
html.description.abstract<p>Responsiveness of genes to steroid hormones is a complex process involving synergistic and/or antagonistic interactions between specific receptors and other nonreceptor transcription factors. Thus, DNA recognition elements for steroid hormone receptors are often located among binding sites for other trans-acting factors. The hormonal form of vitamin D, 1,25-dihydroxyvitamin D3, stimulates transcription of the tissue-specific osteocalcin (OC) gene in osteoblastic cells. The rat OC vitamin D response element contains an internal acitvating protein-1 (AP-1) site. Here, we report for the first time that this AP-1 site is critical for the transcriptional enhancement of rat osteocalcin gene expression mediated by vitamin D. Precise mutations were introduced either in the steroid half-elements or in the internal AP-1 sequences. One mutation within the internal AP-1 site retained vitamin D receptor/retinoid X receptor binding equivalent to that of the wild-type sequence, but resulted in complete loss of vitamin D inducibility of the OC promoter. These results suggest a functional interaction between the hormone receptor and nuclear oncoproteins at the rat OC vitamin D response element. This cooperation of activities may have important consequences in physiological regulation of osteocalcin transcription during osteoblast differentiation and bone tissue development in vivo.</p>
dc.identifier.submissionpathgsbs_sp/60
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages63-70


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