| http://purl.uniprot.org/citations/17956871 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17956871 | http://www.w3.org/2000/01/rdf-schema#comment | "Bone sialoprotein (BSP) is a bone matrix glycoprotein whose expression coincides with terminal osteoblastic differentiation and the onset of mineralization. In this study we show that BSP expression is considerably increased in confluent Saos-2 human osteosarcoma cells and in differentiating normal human osteoblasts, concomitantly with the decrease of Runx2, a key transcription factor controlling bone formation. Therefore, we investigated the role of Runx2 in the regulation of BSP expression in Saos-2 cells. Using a mobility shift assay, we demonstrated that Runx2 binds to the BSP promoter only in preconfluent cells. Histone deacetylase 3 (HDAC3) has been recently shown to act as a Runx2 co-repressor. Chromatin immunoprecipitation assays demonstrated that both Runx2 and HDAC3 are detectable at the BSP promoter in preconfluent Saos-2 cells but not when they are confluent and overexpress BSP. Consistently, nuclear Runx2 protein level is down-regulated, whereas Saos-2 cells became increasingly confluent. Finally, the suppression of HDAC3, Runx2, or both by RNA interference induced the expression of BSP at both mRNA and protein levels in Saos-2 cells. Our data demonstrate that Runx2 and HDAC3 repress BSP gene expression and that this repression is suspended upon osteoblastic cell differentiation. Both the nuclear disappearance of Runx2 and the non-recruitment of HDAC3 represent new means to relieve Runx2-mediated suppression of BSP expression, thus allowing the acquisition of a fully differentiated and mineralization-competent phenotype by osteoblast cells."xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m705833200"xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/author | "Sanchez C."xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/author | "Lamour V."xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/author | "Castronovo V."xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/author | "Detry C."xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/author | "Bellahcene A."xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/author | "Henrotin Y."xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/pages | "36240-36249"xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/title | "Runx2- and histone deacetylase 3-mediated repression is relieved in differentiating human osteoblast cells to allow high bone sialoprotein expression."xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/17956871 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17956871 |
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