Abstract
The main biochemical characteristic of Parkinson’s disease (PD) is reduction of the neurotransmitter dopamine and the dopamine-synthesizing enzyme system, including tyrosine hydroxylase (TH, tyrosine 3-monooxygenase, EC 1.14.16.2) and tetrahydrobiopterin (BH4 co-factor, in nigrostriatal neurons (1). The deficiency in dopamine-synthesizing enzymes is accompanied by cell loss, which is thought to be caused by unknown exogenous environmental factors as well as endogenous genetic factors.
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References
Nagatsu, T. (1993) Biochemical aspects of Parkinson’s disease. Adv. Neurol. 60, 165–174.
Nagatsu, T., Levitt, M., and Udenfriend, S. (1964) Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis. J. Biol. Chem. 239, 2910–2917.
Nagatsu, T. (1995) Tyrosine hydroxylase: human isoforms, structure and regulation in physiology and pathology, in Essays in Biochemistry, vol. 30 (Apps, D. K. and Tipton, K. F., eds.), Portland Press, London, pp. 15–35.
Kaufman, S. and Fisher, D. B. (1974) Pterin-requiring aromatic amino acid hydroxylase, in Molecular Mechanisms of Oxygen Activation (Hayaishi, O., ed.), Academic Press, New York, pp. 285–369.
Matsuura, S., Sugimoto, T., Masada, S., Murata, Y., and Iwasaki, H. (1985) Streochemistry of biopterin cofactor and facile methods for the determination of the stereochemistry of a biologically active 5,6,7,8-tetrahydrobiopterin. J.Biochem. 98, 1341–1348.
Nagatsu, T. (1991) Genes for human catecholamine-synthesizing enzymes. Neurosci. Res. 12, 315–345.
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.
Kaneda, N., Kobayashi, K., Ichinose, H., Kishi, F., Nakazawa, A., Kurosawa, Y.,et al. (1987) Isolation of a 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.,et al. (1987) Isolation of a full-length cDNA clone encoding human tyrosine hydroxylase type 3. Nucleic Acids Res. 15, 6733.
Kobayashi, K., Kaneda, N., Ichinose, H., Kishi, F., Nakazawa, A., Kurosawa, Y.,et al. (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.
O’Mally, K. L., Anhalt, M. J., Martin, B. M., Kalsoe, J. R., Winfield, S. L., and Ginns, E. I. (1997) Isolation and characterization of the human tyrosine hydroxylase gene: identification of 5′ alternative splice sites responsible for multiple mRNAs. Biochemistry 26, 6910–6914.
Ichikawa S. Ichise H. and Nagatsu T. 1990 Multiple mRNAs of monkey tyrosine hydroxylase. Biochem. Biophys. Res. Commun. 173 1331–1336
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.
Lamouroux, A., Blanot, F., Biguet, N. F., and Mallet, J. (1985) Complete coding sequence of rat tyrosine hydroxylase mRNA. Proc. Natl. Acad. Set USA 82, 617–621.
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.
Mogi, M., Harada, M., Kiuchi, K., Kojima, K., Kondo, T., Narabayashi, H., et al.(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 and tyrosine hydroxylase content. Neurosci. Lett. 80, 213–218.
Reinhard, J. F. Jr., and O’Callaghan, J. P. (1991) Measurement of tyrosine hydroxylase apoenzyme protein by enzyme-linked immunosorbent assay (ELISA): effects of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) on striatal tyrosine hydroxylase activity and content. Anal. Biochem. 196, 296–301.
Ichinose, H., Ohye, T., Fujita, K., Pantucek, F., Lange, K., Riederer, P., and Nagatsu, T. (1994) Quantification of mRNA of tyrosine hydroxylase and aromatic L-amino acid decarboxylase in the substantia nigra in Parkinson’s disease and schizophrenia. J. Neural Transm. [P-D Sect.] 8, 149–158.
Ohye, T., Ichinose, H., Ogawa, M., Yoshida, M., and Nagatsu, T. (1995) Alterations in multiple tyrosine hydroxylase mRNAs in the substantia nigra, locus coeruleus and adrenal gland of MPTP-treated parkinsonian monkeys. Neurodegeneration 4, 81–85.
Nagatsu, T. and Ichinose, H. (1991) Comparative studies on the structure of human tyrosine hydroxylase with those of the enzyme of various mammals. Comp. Biochem. Physiol. 98C, 203–210.
Wang, M. A., Doyle, M. V., and Mark, D. F. (1989) Quantitation of mRNA by the polymerase chain reaction. Proc. Natl, Acad. Sci. USA 86, 9717–9721.
Haycock, J. W. (1993) Multiple forms of tyrosine hydroxylase in human neuroblastoma cells: quantitation with isoform-specific antibodies. J. Neurochem. 60, 493–502.
Dumas, S., Le Hir, H., Bodeau-Péan, S., Hirsch, E., Thermes, C., and Mallet, J.(1996) New species of human tyrosine hydroxylase mRNA are produced in variable amounts in adrenal medulla and are overexpressed in progressive supranuclear palsy. J. Neurochem. 67, 19–25.
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Ichinose, H., Ohye, T., Suzuki, T., Inagaki, H., Nagatsu, T. (2001). Quantification of Tyrosine Hydroxylase mRNA. In: Maral Mouradian, M. (eds) Parkinson's Disease. Methods in Molecular Medicine™, vol 62. Humana Press. https://doi.org/10.1385/1-59259-142-6:157
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DOI: https://doi.org/10.1385/1-59259-142-6:157
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