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Regulation of the tyrosine hydroxylase gene promoter by histone deacetylase inhibitors
- Regulation of the tyrosine hydroxylase gene promoter by histone deacetylase inhibitors
- Kim H.-S.; Park J.-S.; Hong S.-J.; Woo M.-S.; Kim S.-Y.; Kim K.-S.
- Ewha Authors
- 김희선; 박진선
- SCOPUS Author ID
- 김희선; 박진선
- Issue Date
- Journal Title
- Biochemical and Biophysical Research Communications
- vol. 312, no. 4, pp. 950 - 957
- SCI; SCIE; SCOPUS
- Tyrosine hydroxylase (TH) catalyzes the conversion of L-tyrosine to 3,4-dihydroxy-L-phenylalanine, which is the first and rate-limiting step in catecholamine biosynthesis. In the present study, we report that treatment with the histone deacetylase (HDAC) inhibitors, trichostatin A (TSA) or sodium butyrate, prominently induces the TH promoter activity in both non-neuronal and neuronal cell lines. By analyzing a series of deletional reporter constructs, we also determined that the proximal 151bp region of the TH promoter is largely responsible for TSA-mediated activation. Finally, we found that mutation of the Sp1 or CRE site, residing in the proximal area, abolishes TSA-mediated activation, strongly suggesting that the Sp1 and CRE sites may mediate TH promoter activation by inhibition of HDAC. In summary, our results provide a novel regulatory frame in which modulation of chromatin structure by histone deacetylase may contribute to transcriptional regulation of the TH via the Sp1 and/or CRE site. © 2003 Elsevier Inc. All rights reserved.
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