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Cell-Type Specific Gene Regulation of Tyrosine Hydroxylase in the Central Nervous System

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Catecholamine Research

Part of the book series: Advances in Behavioral Biology ((ABBI,volume 53))

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Abstract

Since 1964 when Nagatsu, Levitt and Udenfriend1 identified and partially characterized tyrosine hydroxylase (TH) from the rat adrenal gland as the rate limiting enzyme in the catecholamine (CA) biosynthetic pathway, TH has become one of the most studied enzymes in biochemistry, pharmacology and neuroscience. It has been also widely used as a marker protein for catecholamine neurons in the studies on human brain diseases that include behavioral (Schizophrenia, depression, drug abuse, etc.) and neurodegenerative disorders (Parkinson’s disease).

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References

  1. T. Nagatsu, M. Levitt, and S. Udenfriend, Tyrsosine hydroxylase: The initial step in norepinephrine biosynthesis, J. Biol. Chem., 239, 2910–2918 (1964).

    PubMed  CAS  Google Scholar 

  2. T. H. Joh, C. Geghman, and D. J. Reis, Immunochemical demonstration of increased accumulation of tyrosine hydroxylase protein in sympathetic ganglia and adrenal medulla elicited by reserpine, Proc. Natl. Acad. Sci., USA, 70, 2767–2771 (1973).

    Article  PubMed  CAS  Google Scholar 

  3. T. H. Joh, D. H. Park, and R. J. Reis, Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: mechanism of enzyme activation, Proc. Natl. Acad. Sci., USA, 75, 4744–4748 (1978).

    Article  PubMed  CAS  Google Scholar 

  4. T. H. Joh, J. H. Son, C. Tinti, B. Conti, S. J. Kim, and S. Cho, Unique and cell-type specific tyrosine hydroxylase gene expression, in: Catecholamines, Bridging basic science with clinical medicine, Adv. Pharmacol, 42, edited by D. S. Goldstein, G. Eisenhoffer, and R. McCarty, (1998) pp. 33–36.

    Google Scholar 

  5. T. C. Wessel, and T. H. Joh, Parallel upregulation of catecholamine-synthesizing enzymes in rat brain and adrenal gland: effects of reserpine and correlation with immediate early gene expression, Mol. Brain Res., 15, 349–360 (1992).

    Article  PubMed  CAS  Google Scholar 

  6. M. Weiser, H. Baker, T. Wessel, and T. H. Joh, Differential, spatial and temporal gene expression in response to axotomy and deafferentation following transection of the medial forebrain bundle, J. Neurosci., 13, 3472–3484 (1993).

    PubMed  CAS  Google Scholar 

  7. K. S. Kim, D. H. Park, T. C. Wessel, B. Song, J. A. Wagner, and T. H. Joh, A dual role for the cAMP- dependent protein kinase in tyrosine hydroxylase gene expression, Proc. Natl. Acad. Sci., USA, 90, 3471–3475 (1993).

    Article  PubMed  CAS  Google Scholar 

  8. C. Tinti, B. Conti, J. F. Cubells, K. S. Kim, and T. H. Joh, Inducible cAMP early repressor can modulate tyrosine hydroxylase gene expression after stimulation of cAMP synthesis, J. Biol. Chem., 271, 25375–25381 (1996).

    Article  PubMed  CAS  Google Scholar 

  9. C. Tinti, C. Yang, H. Seo, B. Conti, C. Kim, T. H. Joh, and K. S. Kim, Structure/function relationship of the c-AMP response element in tyrosine hydroxylase gene transcription, J. Biol. Chem., 272, 19158–19164 (1997).

    Article  PubMed  CAS  Google Scholar 

  10. K. Nagamoto-Combs, K. M. Piech, J. A. Best, B Sun, and A. W. Tank, Tyrosine hydroxylase gene promoter activity is regulated by both cyclic AMP-responsive element and API sites following calcium influx, J. Biol. Chem., 272, 6051–6058 (1997).

    Article  PubMed  CAS  Google Scholar 

  11. K. M. Piech-Dumas, J. A. Best, Y. Chen, K. Nagamoto-Combs, C. A. Osterhout, and A. W. Tank, The cAMP responsive element and CREB partially mediate the response of the tyrosine hydroxylase gene to phorbol ester, J. Neurochem., 76, 1376–1385 (2001).

    Article  PubMed  CAS  Google Scholar 

  12. Z. Guo, X. Du, and L. Iacovitti, Regulation of tyrosine hydroxylase gene expression during transdifferentiation of striatal neurons: Changes in transcription factors binding the AP-1 site, J. Neurosci., 18, 8163–8174 (1998).

    PubMed  CAS  Google Scholar 

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Shimizu, Y., Sugama, S., Cho, B.P., Joh, T.H. (2002). Cell-Type Specific Gene Regulation of Tyrosine Hydroxylase in the Central Nervous System. In: Nagatsu, T., Nabeshima, T., McCarty, R., Goldstein, D.S. (eds) Catecholamine Research. Advances in Behavioral Biology, vol 53. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-3538-3_25

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  • DOI: https://doi.org/10.1007/978-1-4757-3538-3_25

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4419-3388-1

  • Online ISBN: 978-1-4757-3538-3

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