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- W2059851539 abstract "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." @default.
- W2059851539 created "2016-06-24" @default.
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- W2059851539 date "1999-03-15" @default.
- W2059851539 modified "2023-10-02" @default.
- W2059851539 title "Phosphorylation-mediated control of chromatin organization and transcriptional activity of the tissue-specific osteocalcin gene" @default.
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- W2059851539 doi "https://doi.org/10.1002/(sici)1097-4644(19990315)72:4<586::aid-jcb13>3.0.co;2-k" @default.
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