PMID: 9541257Apr 16, 1998Paper

Characteristics of vitamin D3 receptor (VDR) binding to the vitamin D response element (VDRE) in rat bone sialoprotein gene promoter

European Journal of Oral Sciences
J J LiJ Sodek

Abstract

Bone sialoprotein (BSP) is a mineralised tissue-specific protein that is highly expressed during the initial formation of bone and cementum. Expression of BSP is suppressed by the osteotropic hormone, 1,25-dihydroxyvitamin D3 (vitamin D3), which regulates bone remodelling. In previous studies, we have identified a vitamin D response element (VDRE) that is integrated with a novel inverted TATA box in the rat BSP promoter which mediates the suppression of BSP transcription (1). Although the nucleotide sequences of VDREs in different genes conform to a direct (hexamer) repeat, spaced by three nucleotides, the precise sequences are unique for each VDRE. To determine whether the nucleotide differences in the VDRE influence VDR binding, we have compared interactions of VDR proteins with various VDREs using gel mobility shift analysis. Both natural and recombinant VDRs bound to rat BSP and both mouse and porcine osteopontin (OPN) VDRE oligonucleotides in a concentration-dependent manner with a strong preference for dimer formation, whereas equal amounts of dimer and monomer were bound to the human osteocalcin VDRE. However, whereas a truncated VDR comprising the DNA binding domain alone bound the mouse osteopontin VDRE, it failed to i...Continue Reading

Citations

Oct 6, 2000·Critical Reviews in Oral Biology and Medicine : an Official Publication of the American Association of Oral Biologists·J SodekM D McKee
Feb 3, 2009·Molecular Carcinogenesis·Haibo XuFrederick C Campbell
Jan 22, 2005·Annals of the New York Academy of Sciences·Yasuhiro KumeiPeggy A Whitson
Oct 21, 2004·Molecular Cell·Pascal DranéJean-Marc Egly

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