Chromatin hyperacetylation abrogates vitamin D-mediated transcriptional upregulation of the tissue-specific osteocalcin gene in vivo

Martin Montecino, Baruch Frenkel, André J. Van Wijnen, Jane B. Lian, Gary S. Stein, Janet L. Stein

Resultado de la investigación: Article

36 Citas (Scopus)

Resumen

Cells expressing the bone-specific osteocalcin (OC) gene exhibit two DNase I hypersensitive sites within the proximal (nt -170 to -70) and distal (nt -600 to -400) promoter. These sites overlap elements that independently or in combination contribute to basal and vitamin D-stimulated OC gene transcription. Here we address mechanisms that participate in control of chromatin remodelling at these sites. By applying nuclease digestion and indirect end-labeling or by combining intranuclear footprinting and ligation- mediated PCR, we investigated the effects of nuclear protein hyperacetylation on both chromatin organization and transcriptional activation of the OC gene in bone-derived cells. We report that chromatin hyperacetylation blocks vitamin D stimulation of OC transcription and prevents a key transition in the chromatin structure of the OC gene which is required for formation of the distal DNase I hypersensitive site. This transition involves interaction of sequence-specific nuclear factors and may be required for the ligand- dependent binding of the vitamin D receptor complex, which results in transcriptional enhancement.

Idioma originalEnglish
Páginas (desde-hasta)1338-1345
Número de páginas8
PublicaciónBiochemistry
Volumen38
N.º4
DOI
EstadoPublished - 26 ene 1999

Huella dactilar

Osteocalcin
Vitamin D
Chromatin
Up-Regulation
Genes
Tissue
Deoxyribonuclease I
Transcription
Bone
Bone and Bones
Calcitriol Receptors
Chromatin Assembly and Disassembly
Nuclear Proteins
Labeling
Transcriptional Activation
Ligation
Digestion
Chemical activation
Cells
Ligands

ASJC Scopus subject areas

  • Biochemistry

Citar esto

Montecino, Martin ; Frenkel, Baruch ; Van Wijnen, André J. ; Lian, Jane B. ; Stein, Gary S. ; Stein, Janet L. / Chromatin hyperacetylation abrogates vitamin D-mediated transcriptional upregulation of the tissue-specific osteocalcin gene in vivo. En: Biochemistry. 1999 ; Vol. 38, N.º 4. pp. 1338-1345.
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abstract = "Cells expressing the bone-specific osteocalcin (OC) gene exhibit two DNase I hypersensitive sites within the proximal (nt -170 to -70) and distal (nt -600 to -400) promoter. These sites overlap elements that independently or in combination contribute to basal and vitamin D-stimulated OC gene transcription. Here we address mechanisms that participate in control of chromatin remodelling at these sites. By applying nuclease digestion and indirect end-labeling or by combining intranuclear footprinting and ligation- mediated PCR, we investigated the effects of nuclear protein hyperacetylation on both chromatin organization and transcriptional activation of the OC gene in bone-derived cells. We report that chromatin hyperacetylation blocks vitamin D stimulation of OC transcription and prevents a key transition in the chromatin structure of the OC gene which is required for formation of the distal DNase I hypersensitive site. This transition involves interaction of sequence-specific nuclear factors and may be required for the ligand- dependent binding of the vitamin D receptor complex, which results in transcriptional enhancement.",
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Chromatin hyperacetylation abrogates vitamin D-mediated transcriptional upregulation of the tissue-specific osteocalcin gene in vivo. / Montecino, Martin; Frenkel, Baruch; Van Wijnen, André J.; Lian, Jane B.; Stein, Gary S.; Stein, Janet L.

En: Biochemistry, Vol. 38, N.º 4, 26.01.1999, p. 1338-1345.

Resultado de la investigación: Article

TY - JOUR

T1 - Chromatin hyperacetylation abrogates vitamin D-mediated transcriptional upregulation of the tissue-specific osteocalcin gene in vivo

AU - Montecino, Martin

AU - Frenkel, Baruch

AU - Van Wijnen, André J.

AU - Lian, Jane B.

AU - Stein, Gary S.

AU - Stein, Janet L.

PY - 1999/1/26

Y1 - 1999/1/26

N2 - Cells expressing the bone-specific osteocalcin (OC) gene exhibit two DNase I hypersensitive sites within the proximal (nt -170 to -70) and distal (nt -600 to -400) promoter. These sites overlap elements that independently or in combination contribute to basal and vitamin D-stimulated OC gene transcription. Here we address mechanisms that participate in control of chromatin remodelling at these sites. By applying nuclease digestion and indirect end-labeling or by combining intranuclear footprinting and ligation- mediated PCR, we investigated the effects of nuclear protein hyperacetylation on both chromatin organization and transcriptional activation of the OC gene in bone-derived cells. We report that chromatin hyperacetylation blocks vitamin D stimulation of OC transcription and prevents a key transition in the chromatin structure of the OC gene which is required for formation of the distal DNase I hypersensitive site. This transition involves interaction of sequence-specific nuclear factors and may be required for the ligand- dependent binding of the vitamin D receptor complex, which results in transcriptional enhancement.

AB - Cells expressing the bone-specific osteocalcin (OC) gene exhibit two DNase I hypersensitive sites within the proximal (nt -170 to -70) and distal (nt -600 to -400) promoter. These sites overlap elements that independently or in combination contribute to basal and vitamin D-stimulated OC gene transcription. Here we address mechanisms that participate in control of chromatin remodelling at these sites. By applying nuclease digestion and indirect end-labeling or by combining intranuclear footprinting and ligation- mediated PCR, we investigated the effects of nuclear protein hyperacetylation on both chromatin organization and transcriptional activation of the OC gene in bone-derived cells. We report that chromatin hyperacetylation blocks vitamin D stimulation of OC transcription and prevents a key transition in the chromatin structure of the OC gene which is required for formation of the distal DNase I hypersensitive site. This transition involves interaction of sequence-specific nuclear factors and may be required for the ligand- dependent binding of the vitamin D receptor complex, which results in transcriptional enhancement.

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