Regulation of the tyrosine hydroxylase gene promoter by histone deacetylase inhibitors

Hee Sun Kim, Jin Sun Park, Seok Jong Hong, Moon Sook Woo, So Young Kim, Kwang Soo Kim

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


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.

Original languageEnglish
Pages (from-to)950-957
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - 26 Dec 2003

Bibliographical note

Funding Information:
This work was supported by Korea Research Foundation Grant KRF-2002-003-C00114 to H.S. Kim.


  • Chromatin structure
  • CRE
  • Histone deacetylase
  • Sodium butyrate
  • Sp1
  • Transcriptional regulation
  • Trichostatin A
  • Tyrosine hydroxylase


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