Biopterin in the Brain of Controls and Patients with Parkinson’s Disease and Related Striatal Degenerative Diseases: Application of New Biopterin Radioimmunoassay

  • Toshiharu Nagatsu
  • Tokio Yamaguchi
  • Takeshi Kato
  • Takashi Sugimoto
  • Sadao Matsuura
  • Miki Akino
  • Ikuko Nagatsu
  • Reiji Iizuka
  • Hirotaro Narabayashi

Abstract

We reported that tyrosine hydroxylase activity in the dopaminergic regions of nigro-striato-pallidal complex of the brain is greatly reduced (5–10% of controls) in all 12 cases of parkinsonian patients (Nagatsu, et al., 1977, 1979). The reduction in tyrosine hydroxylase activity in the parkinsonian brain was also reported by several groups (Lloyd, et al., 1975; McGeer and McGeer, 1976; Riederer, et al., 1979).

Keywords

Dopamine Tyrosine Tryptophan Catecholamine Acetylcholine 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Brenneman, A. R. and Kaufman, S. (1964). The role of tetrahydropteridines in the enzymatic conversion of tyrosine to 3,4-dihydroxyphenylalanine. Biochem. Biophys. Res. Commun., 17, 177–183.CrossRefGoogle Scholar
  2. Bullard, W. P., Guthrie, P. B., Russo, P. B. and Mandell, A. J. (1978). Regional and subcellular distribution and some factors in the regulation of reduced pterins in rat brain. J. Pharmacol. Exp. Therap., 206, 4–20Google Scholar
  3. Fukushima, T. and Nixon, J. C. (1980). Analysis of reduced forms of biopterin in biological tissues and fluids. Anal. Biochem., 102, 176–188.CrossRefGoogle Scholar
  4. Kettler, R., Bartholini, G. and Pletscher, A. (1974). In vivo enhancement of tyrosine hydroxylation in rat striatum by tetrahydrobiopterin. Nature, 249, 476–478.CrossRefGoogle Scholar
  5. Levine, R. A., Kuhn, D. M. and Lovenberg, W. (1979). The regional distribution of hydroxylase cofactor in rat brain. J. Neurochem., 32, 1575–1578.CrossRefGoogle Scholar
  6. Lloyd, K. G., Davidson, L. and Hornykiewicz, O. (1975). The neurochemistry of Parkinson’s disease: effect of L-DOPA therapy. J. Pharmacol. Exp. Therap., 195, 453–464.Google Scholar
  7. Lovenberg, W., Levine, R. A., Robinson, D. S., Ebert, M., Williams, A. C. and Calne, D. B. (1979). Hydroxylase cofactor activity in cerebrospinal fluid of normal subjects and patients with Parkinson’s disease. Science, 204, 624–626.CrossRefGoogle Scholar
  8. McGeer, P. L. and McGeer, E. G. (1976). Enzymes associated with the metabolism of catecholamines, acetylcholine and GABA in human controls and patients with Parkinson’s disease and Huntington’s chorea. J. Neurochem., 6, 65–76.Google Scholar
  9. Nagatsu, T. (1973). Biochemistry of Catecholamines, Univ. Tokyo Press and Univ. Park Press, Tokyo and Baltimore.Google Scholar
  10. Nagatsu, T. (1979) Regulation of tyrosine hydroxylase. In Frontiers in Catecholamine Research, (eds. E. Usdin and S. Snyder), Pergamon Press, Oxford.Google Scholar
  11. 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.CrossRefGoogle Scholar
  12. Nagatsu, T., Kato, T., Nagatsu, I., Kondo, Y., Inagaki, S., Iizukz, R. and Narabayashi, H., (1979). Catecholamine-related enzymes in the brain of patients with parkinsonism and Wilson’s disease. Adv. in Neurol., 24, 283–292.Google Scholar
  13. Nagatsu, T., Levitt, M and Udenfriend, S. (1964). Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis. J. Biol. Chem., 239, 2910–2917.Google Scholar
  14. Nagatsu, T., Numata(Sudo), Y., Kato, T., Sugiyama, K. and Akino, M. (1978). Effects of melanin on tyrosine hydroxyalse and phenylalanine hydroxylase. Biochim. Biophsy. Acta, 523, 47–52.CrossRefGoogle Scholar
  15. Nagatsu, T., Oka, K. and Kato, T. (1979). Highly sensitive assay for tyrosine hydroxylase activity by high-performance liquid chromatography. J. Chromatogr. 163, 247–252.CrossRefGoogle Scholar
  16. Nagatsu, T., Yamaguchi, T., Kato, T., Sugimoto, T., Matsuura, S., Kobayashi, K., Akino, M., Tsushima, S., Nakazawa, N. and Ogawa, H. (1979) Proc. Japan Acad., 55, Ser. B, 317–322.CrossRefGoogle Scholar
  17. Numata(Sudo), Y., Kato, T., Nagatsu, T., Sugimoto, T. and Matsuura, S. (1977). Effects of stereochemical structures of tetrahydrobiopterin on tyrosine hydroxylase. Biochim. Biophys. Acta, 480, 104–112.CrossRefGoogle Scholar
  18. Riederer, P., Rausch, W. -D., Birkmayer, W., Jellinger, K. and Seemann, D. (1978). CNS modulation of adrenal tyrosine hydroxylase in Parkinson’s disease and metabolic encephalopathies. J. Neural Transmission, Suppl. 14, 121–131.Google Scholar
  19. Weiner, N., Lee, F. -L., Dreyer, E. and Barnes, E. (1978). The activation of tyrosine hydroxylase in noradrenergic neurons during acute nerve stimulation. Life Sci., 22, 1197–1216.CrossRefGoogle Scholar

Copyright information

© The Contributors 1981

Authors and Affiliations

  • Toshiharu Nagatsu
    • 1
  • Tokio Yamaguchi
    • 1
  • Takeshi Kato
    • 1
  • Takashi Sugimoto
    • 2
  • Sadao Matsuura
    • 2
  • Miki Akino
    • 3
  • Ikuko Nagatsu
    • 4
  • Reiji Iizuka
    • 5
  • Hirotaro Narabayashi
    • 6
  1. 1.Laboratory of Cell Physiology, Department of Life Chemistry, Graduate School at NagatsutaTokyo Institute of TechnologyYokohamaJapan
  2. 2.Department of ChemistryNagoya UniversityNagoyaJapan
  3. 3.Department of BiologyTokyo Metropolitan UniversityTokyoJapan
  4. 4.Department of Anatomy, School of MedicineFujita-Gakuen UniversityToyoakeJapan
  5. 5.Department of Psychiatry, School of MedicineJuntends UniversityTokyoJapan
  6. 6.Department of Neurology, School of MedicineJuntends UniversityTokyoJapan

Personalised recommendations