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

*Corresponding author for this work

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


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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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