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Regulation of the tyrosine hydroxylase gene promoter by histone deacetylase inhibitors

Title
Regulation of the tyrosine hydroxylase gene promoter by histone deacetylase inhibitors
Authors
Kim H.-S.Park J.-S.Hong S.-J.Woo M.-S.Kim S.-Y.Kim K.-S.
Ewha Authors
김희선박진선
SCOPUS Author ID
김희선scopus; 박진선scopus
Issue Date
2003
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 312, no. 4, pp. 950 - 957
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
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.
DOI
10.1016/j.bbrc.2003.11.012
Appears in Collections:
의학전문대학원 > 의학과 > Journal papers
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