1 Ocak 2000 Dergi makalesi Açık Erişim

Guzey, M; Takayama, S; Reed, JC

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  <identifier identifierType="URL">https://aperta.ulakbim.gov.tr/record/100871</identifier>
  <creators>
    <creator>
      <creatorName>Guzey, M</creatorName>
      <givenName>M</givenName>
      <familyName>Guzey</familyName>
    </creator>
    <creator>
      <creatorName>Takayama, S</creatorName>
      <givenName>S</givenName>
      <familyName>Takayama</familyName>
    </creator>
    <creator>
      <creatorName>Reed, JC</creatorName>
      <givenName>JC</givenName>
      <familyName>Reed</familyName>
    </creator>
  </creators>
  <titles>
    <title>Bag1L Enhances Trans-Activation Function Of The Vitamin D Receptor</title>
  </titles>
  <publisher>Aperta</publisher>
  <publicationYear>2000</publicationYear>
  <dates>
    <date dateType="Issued">2000-01-01</date>
  </dates>
  <resourceType resourceTypeGeneral="Text">Journal article</resourceType>
  <alternateIdentifiers>
    <alternateIdentifier alternateIdentifierType="url">https://aperta.ulakbim.gov.tr/record/100871</alternateIdentifier>
  </alternateIdentifiers>
  <relatedIdentifiers>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsVersionOf">10.81043/aperta.100870</relatedIdentifier>
    <relatedIdentifier relatedIdentifierType="DOI" relationType="IsIdenticalTo">10.81043/aperta.100871</relatedIdentifier>
  </relatedIdentifiers>
  <rightsList>
    <rights rightsURI="http://www.opendefinition.org/licenses/cc-by">Creative Commons Attribution</rights>
    <rights rightsURI="info:eu-repo/semantics/openAccess">Open Access</rights>
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  <descriptions>
    <description descriptionType="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.</description>
  </descriptions>
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