Abstract
The main biochemical characteristics of Parkinson’s disease are the reduction of dopamine the neurotransmitter, and of tyrosine hydroxylase (TH) and the biopterin cofactor, the dopamine-synthesizing enzyme system, in the nigrostriatal dopamine neurons. A deficiency in the dopamine-synthesizing enzymes is accompanied by cell loss of the nigrostriatal dopamine neurons, which is assumed to be caused by unknown exogenous, environmental factors and endogenous, genetic factors. Not only the nigrostriatal dopamine neurons but also other catecholamine neurons may be impaired, as suggested by decreases in dopamine β-hydroxylase (DBH) in norepinephrine neurons and phenylethanolamine Nmethyltransferase (PNMT) in epinephrine neurons (Nagatsu et al., 1977; Nagatsu et al., 1984).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Coker III, G. T., Studelska, D., Harmon, S., Burke, W., and O’Malley, K. L., 1990, Analysis of tyrosine hydroxylase and insulin transcript in human neuroendocrine tissues, Mol. Brain Res. 8: 93–98.
D’ Mello, S. R., Weisberg, E. P., Stachowiak, M. K., Turzai, L. M., Gioio, A. E., and Kaplan, B. B., 1988, Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: comparative analysis of tyrosine hydroxylase gene products, J. Neurosci. Res. 19: 440449.
Grima, B., Lamouroux, A., Blanot, F., Biguet, N. F., and Mallet, J., 1985, Complete coding sequence of rat tyrosine hydroxylase mRNA, Proc. Natl. Acad. Sci. USA, 82: 617–621.
Grima, B., Lamouroux, A., Boni, C., Julien, J. -F., Javoy-Agid, F., and Mallet, J., 1987, A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics, Nature 326: 707–711.
Haycook, J. W., 1993, Multiple forms of tyrosine hydroxylase in human neuroblastoma cells: quantitation with isoform-specific antibodies., J. Neurochem. 60: 493–502.
Ichikawa, S., Ichinose, H., and Nagatsu, T., 1990, Multiple mRNAs of monkey tyrosine hydroxylase, Biochem. Biophys. Res. Commun. 173: 1331–1336.
Ichikawa, S., Sasaoka, T., and Nagatsu, T., 1991, Primary structure of mouse tyrosine hydroxylase deduced from its cDNA, Biochem. Biophys. Res. Commun. 176: 1610–1616.
Ichinose, H., Ohye, T., Fujita, K., and Nagatsu, T., 1992, Multiplicity of tyrosine hydroxylase in primates, J. Neurochem. 59, Suppl. S20.
Ichinose, H., Ohye, T., Fujita, K., Yoshida, M., Ueda, S., and Nagatsu, T., 1993, Increased heterogeneity of tyrosine hydroxylase in humans, Biochem. Biophys. Res. Commun. 195: 158–165.
Iwata, N., Kobayashi, K., Sasaoka, T., Hidaka, H., and Nagatsu, T., 1992, Structure of the mouse tyrosine hydroxylase gene, Biochem. Biophys. Res. Commun. 182: 348–354.
Kaneda, N., Kobayashi, K., Ichinose, H., Kishi, F., Nakazawa, A., Kurosawa, Y., Fujita, K., and Nagatsu, T., 1987, Isolation of novel cDNA clone for human tyrosine hydroxylase: alternative RNA splicing produces four kinds of mRNA from a single gene, Biochem. Biophys. Res. Commun. 146: 971–975.
Kobayashi, K., Kaneda, N., Ichinose, H., Kishi, F., Nakazawa, A., Kurosawa, Y., Fujita, K., and Nagatsu, T., 1987, Isolation of a full-length cDNA-clone encoding human tyrosine hydroxylase type 3. Nucleic Acids Res. 15: 6733–6733.
Kobayashi, K., Kaneda, N., Ichinose, H., Kishi, F., Nakazawa, A., Kurosawa, Y., Fujita, K., and Nagatsu, T., 1988, Structures of the human tyrosine hydroxylase gene: alternative splicing from a single gene accounts for generation of four mRNA types. J. Biochem. 103: 907–912.
Le Bourdelles, B., Boularand, S., Boni, P., Horellou, P., Dumas, S., Grima, B., and Mallet, J., 1988, Analysis of the 5’ region of the human tyrosine hydroxylase gene:combined patterns of exon slicing generate multiple regulated tyrosine hydroxylase isoforms, J. Neurochem. 50: 988–991.
Lewis, D. A., Melchitzky, D. S., and Haycock, J. W., 1993, Four isoforms of tyrosine hydroxylase are present in human brain, Neuroscience 54: 477–492.
Mogi, M., Harada, M., Kiuchi, K., Kojima, K., Kondo, T., Narabayashi, H., Rausch, D., Riederer, P., Jellinger, K., and Nagatsu, T., 1988, Homospecific activity (activity per enzyme protein) of tyrosine hydroxylase increases in parkinsonian brain, J. Neural Transm. 72: 77–91.
Mogi, M., Harada, M., Kojima, K., Kiuchi, K., Nagatsu, I., and Nagatsu, T., 1987, Effects of repeated systemic administration of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) on striatal tyrosine hydroxylase activity in vitro and tyrosine hydroxylase content, Neurosci. Leu. 80: 213–238.
Nagatsu, T., 1991, Genes for human catecholamine-synthesizing enzymes, Neurosci. Res. 12: 315–345.
Nagatsu, T., Kato, T., Numata (Sudo), Y., Ikuta, K., Sano, M., Nagatsu, I., Kondo, Y., Inagaki, S., Iizuka, R.,Hori, A., and Narabayashi, H., 1977, Phenylethanolamine N-methyltransferase and other enzymes of catecholamine metabolism in human brain, Clin. Chim. Acta 75: 221–232.
Nagatsu, T., Yamaguchi, T., Rahman, M. K., Trocewicz, J., Oka, K., Hirata, Y., Nagatsu, I., Narabayashi, H., Kondo, T., and Iizuka, R., 1984, Catecholamine-related enzymes and the biopterin cofactor in Parkinson’s disci disesme and related extrapyramidal diseases, in: “Advances in Neurology’, R. G. Hassler and J. F. Christ, eds., Raven Press, New York, pp. 463473.
O’ Malley, K. L., Anhalt, M. J., Martin, B. M., Kalsoe, J. R., Winfield, S. L., and Ginns, E. I., 1987, Isolation and characterization of the human tyrosine hydroxylase splice sites responsible for multiple mRNAs, Biochemistry 26: 6910–6914.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Nagatsu, T., Ichinose, H. (1995). Molecular Biology of Catecholamine Systems: Multiple Tyrosine Hydroxylases in Different Simian Species, and in Humans in Relation to Parkinson’s Disease. In: Hanin, I., Yoshida, M., Fisher, A. (eds) Alzheimer’s and Parkinson’s Diseases. Advances in Behavioral Biology, vol 44. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9145-7_94
Download citation
DOI: https://doi.org/10.1007/978-1-4757-9145-7_94
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-9147-1
Online ISBN: 978-1-4757-9145-7
eBook Packages: Springer Book Archive