1 Ocak 2000 Dergi makalesi Açık Erişim

Guzey, M; Takayama, S; Reed, JC

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  <dc:creator>Guzey, M</dc:creator>
  <dc:creator>Takayama, S</dc:creator>
  <dc:creator>Reed, JC</dc:creator>
  <dc:date>2000-01-01</dc:date>
  <dc:description>The vitamin D receptor (VDR) is a member of the steroid/retinoid receptor superfamily of nuclear receptors that has potential tumor-suppressive functions. We show here that VDR interacts with and is regulated by BAG1L, a nuclear protein that binds heat shock 70-kDa (Hsp70) family molecular chaperones. Endogenous BAG1L can be eo-immunoprecipitated with VDR from prostate cancer cells (ALVA31; LNCaP) in a ligand-dependent manner. BAG1L, but not shorter non-nuclear isoforms of this protein (BAG1; BAG1M/Rap46), markedly enhanced, in a ligand-dependent manner, the ability of VDR to trans-activate reporter gene plasmids containing a vitamin D response element in transient transfection assays. Mutant BAG1L lacking the C-terminal Hsc70-binding domain suppressed tin a concentration-dependent fashion) VDR-mediated trans-activation of vitamin D response element-containing reporter gene plasmids, without altering levels of VDR or endogenous BAG1L protein, suggesting that it operates as a trans-dominant inhibitor of BAG1L. Gene transfer-mediated elevations in BAG1L protein levels in a prostate cancer cell line (PC3), which is moderately responsive to VDR ligands, increased the ability of natural (1 alpha ,25(OH)(2) vitamin D-3) and synthetic (1 alpha ,25-dihydroxy19-nor-22(E)-vitamin D-3) VDR ligands to induce expression of the VDR target gene, p21(Waf1), and suppress DNA synthesis. Thus, BAG1L is a direct regulator of VDR, which enhances its trans-activation function and improves tumor cell responses to growth-suppressive VDR ligands.</dc:description>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/100871</dc:identifier>
  <dc:identifier>oai:zenodo.org:100871</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>JOURNAL OF BIOLOGICAL CHEMISTRY 275(52) 40749-40756</dc:source>
  <dc:title>BAG1L enhances trans-activation function of the vitamin D receptor</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
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