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dc.contributor.authorMontecino, Martin A.
dc.contributor.authorVan Wijnen, Andre J.
dc.contributor.authorLian, Jane B.
dc.contributor.authorStein, Janet L.
dc.contributor.authorStein, Gary S.
dc.date2022-08-11T08:09:02.000
dc.date.accessioned2022-08-23T16:15:59Z
dc.date.available2022-08-23T16:15:59Z
dc.date.issued1999-02-18
dc.date.submitted2008-11-24
dc.identifier.citation<p>J Cell Biochem. 1999 Mar 15;72(4):586-94.</p>
dc.identifier.issn0730-2312 (Print)
dc.identifier.doi10.1002/(SICI)1097-4644(19990315)72:4<586::AID-JCB13>3.0.CO;2-K
dc.identifier.pmid10022617
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34222
dc.description.abstractWe have analyzed the linkage of protein phosphorylation to the remodeling of chromatin structure that accompanies transcriptional activity of the rat osteocalcin (OC) gene in bone-derived cells. Short incubations with okadaic acid, an inhibitor of protein phosphatases 1 and 2A, induced marked changes in the chromatin organization of the OC gene promoter. These changes were reflected by loss of the two DNase I hypersensitive sites normally present in bone-derived cells expressing this gene. These hypersensitive sites include the elements that control basal tissue-specific expression, as well as steroid hormone regulation. Indeed, the absence of hypersensitivity was accompanied by inhibition of basal and vitamin D-dependent enhancement of OC gene transcription. The effects of okadaic acid on OC chromatin structure and gene activity were specific and reversible. Staurosporine, a protein kinase C inhibitor, did not significantly affect transcriptional activity or DNase I hypersensitivity of the OC gene. We conclude that cellular phosphorylation-dephosphorylation events distinct from protein kinase C-dependent reactions are required for both chromatin remodeling and transcriptional activity of the OC gene in osseous cells.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10022617&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1002/(SICI)1097-4644(19990315)72:4<586::AID-JCB13>3.0.CO;2-K
dc.subjectAnimals; Chromatin; Deoxyribonuclease I; Enzyme Inhibitors; Gene Expression Regulation; Okadaic Acid; Osteocalcin; Phosphoprotein Phosphatases; Phosphorylation; Promoter Regions (Genetics); Protein Kinase C; Rats; Staurosporine; Tumor Cells, Cultured; Vitamin D
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titlePhosphorylation-mediated control of chromatin organization and transcriptional activity of the tissue-specific osteocalcin gene
dc.typeJournal Article
dc.source.journaltitleJournal of cellular biochemistry
dc.source.volume72
dc.source.issue4
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/879
dc.identifier.contextkey671440
html.description.abstract<p>We have analyzed the linkage of protein phosphorylation to the remodeling of chromatin structure that accompanies transcriptional activity of the rat osteocalcin (OC) gene in bone-derived cells. Short incubations with okadaic acid, an inhibitor of protein phosphatases 1 and 2A, induced marked changes in the chromatin organization of the OC gene promoter. These changes were reflected by loss of the two DNase I hypersensitive sites normally present in bone-derived cells expressing this gene. These hypersensitive sites include the elements that control basal tissue-specific expression, as well as steroid hormone regulation. Indeed, the absence of hypersensitivity was accompanied by inhibition of basal and vitamin D-dependent enhancement of OC gene transcription. The effects of okadaic acid on OC chromatin structure and gene activity were specific and reversible. Staurosporine, a protein kinase C inhibitor, did not significantly affect transcriptional activity or DNase I hypersensitivity of the OC gene. We conclude that cellular phosphorylation-dephosphorylation events distinct from protein kinase C-dependent reactions are required for both chromatin remodeling and transcriptional activity of the OC gene in osseous cells.</p>
dc.identifier.submissionpathgsbs_sp/879
dc.contributor.departmentDepartment of Cell Biology and Cancer Center
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages586-94


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