1 Ocak 2000 Dergi makalesi Açık Erişim

Guzey, M; Takayama, S; Reed, JC

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{
  "URL": "https://aperta.ulakbim.gov.tr/record/100871", 
  "abstract": "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.", 
  "author": [
    {
      "family": "Guzey", 
      "given": " M"
    }, 
    {
      "family": "Takayama", 
      "given": " S"
    }, 
    {
      "family": "Reed", 
      "given": " JC"
    }
  ], 
  "container_title": "JOURNAL OF BIOLOGICAL CHEMISTRY", 
  "id": "100871", 
  "issue": "52", 
  "issued": {
    "date-parts": [
      [
        2000, 
        1, 
        1
      ]
    ]
  }, 
  "page": "40749-40756", 
  "title": "BAG1L enhances trans-activation function of the vitamin D receptor", 
  "type": "article-journal", 
  "volume": "275"
}