Neurochemical Research

, Volume 17, Issue 7, pp 723–727 | Cite as

Increase in nucleoside diphosphatase in rat brain striatum lesioned with kainic acid

  • Shuzo Miyamoto
  • Yoshihiro Matsuda
  • Shin-ichiro Sano
  • Hiroshi Shiraki
  • Hachro Nakagawa
Original Articles

Abstract

The activity of ammoniagenesis from guanine nucleotides was found to increase significantly in rat brain after infusion of kainic acid into the striatum. Among the enzymes involved in degrading guanine nucleotides, nucleoside diphosphatase was markedly increased in the lesioned striatum. The enzyme activity began to increase 2 days after the infusion, and reached the maximum on the 13th day, the level being 4 times as high as that of the intact contralateral region. The increased activity was due to Type L enzyme, judging from its substrate specificity. Puromycin and cycloheximide inhibited this increase, indicating that the increased activity resulted from an increase in the net synthesis of the enzyme. These findings suggest that Type L NDPase might play some important roles in gliosis after neuronal lesion.

Key Words

Ammoniagenesis brain nucleoside diphosphatase kainic acid gliosis 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Lowenstein, J. M. 1972. Ammonia production in muscle and other tissues: the purine nucleotide cycle. Physiol. Rev. 52:382–414.Google Scholar
  2. 2.
    Takagaki, G., Hirano, S., and Tsukada, Y. 1957. Endogenous respiration and ammonia formation in brain slices. Arch. Biochem. Biophys. 68:196–205.Google Scholar
  3. 3.
    Cooper, A. J. L., McDonald, J. M., Gelbard, A. S., Gledhill, R. F., and Duffy, T. E. 1979. The metabolic fate of13N-labeled ammonia in rat brain. J. Biol. Chem. 254:4982–4992.Google Scholar
  4. 4.
    Weil-Malherbe, H., and Green, R. H., 1955. Ammonia formation in brain. Biochem. J. 61:210–224.Google Scholar
  5. 5.
    Schultz, V., and Lowenstein, J. M. 1976. Purine Nucleotide cycle. Evidence for the occurrence of the cycle in brain. J. Biol. Chem. 251:485–492.Google Scholar
  6. 6.
    Miyamoto, S., Ogawa, H., Shiraki, H., and Nakagawa, H. 1982. Guanine deaminase from rat brain. Purification, characteristics, and contribution to ammoniagenesis in the brain. J. Biochem. 91:167–176.Google Scholar
  7. 7.
    Olney, J. W., Rhee, V., and Ho, O. L. 1974. Kainic acid: a powerful neurotoxic analogue of glutamate. Brain Res. 77:507–512.Google Scholar
  8. 8.
    Nicklas, W. J., Nunez, R., Berl, S.,and Duvoisin, R. 1979. Neuronal-glial contributions to transmitter amino acid metabolism: studies with kainic acid-induced lesions of rat striatum. J. Neurochem. 33:839–844.Google Scholar
  9. 9.
    Kitamura, T. 1980. Dynamic aspects of glial reactions in altered brain. Path. Res. Pract. 168:301–343.Google Scholar
  10. 10.
    Coyle, J. T., and Schwarcz, R. 1976. Lesion of striatal neurones with kainic acid provides a model for Huntington's chorea. Nature 263:244–246.Google Scholar
  11. 11.
    Kun, E., and Kearney, E. B. 1974. Ammonia. Pages 1802–1806,in Bergmeyer, H. U. (ed.), Methods of Enzymatic Analysis, Vol. 4, Verlag Chemie Weinheim Academic Press, New York & London.Google Scholar
  12. 12.
    Sano, S., Matsuda, Y., Miyamoto, S., and Nakagawa, H. 1984. Thiamine pyrophosphatase and nucleoside diphosphatase in rat brain. Biochem. Biophys. Res. Commun. 118:292–298.Google Scholar
  13. 13.
    Heinonen, J. K., and Lahti, R. J., 1981. A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Anal. Biochem. 113:313–317.Google Scholar
  14. 14.
    Lowry, O. H., Rosebrough, N. J., Farr, L. A., and Randall, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–275.Google Scholar
  15. 15.
    McGeer, E. G., and McGeer, P. L. 1978. Some factors influencing the neurotoxicity of intrastriatal injections of kainic acid. Neurochem. Res. 3:501–517.Google Scholar
  16. 16.
    Sano, S., Matsuda, Y., and Nakagawa, H. 1988. Type B nucleoside-diphosphatase of rat brain. Purification and properties of an enzyme with high thiamin pyrophosphatase activity. Eur. J. Biochem. 171:231–236.Google Scholar
  17. 17.
    Hattori, T., and McGeer, E. G. 1977. Fine structural changes in the rat striatum after local injections of kainic acid. Brian Res. 129:174–180.Google Scholar
  18. 18.
    Jakubovic, A., Lin, D., and McGeer, E. G. 1979. Protein and RNA synthesis in kainic acid-injected striata. Brain Res. 163:289–294.Google Scholar
  19. 19.
    Martinez-Rodriguez, R., Martinez-Murillo, R., Toledano, A., and Barca, M. A. 1980. A comparative histochemical study of diphosphatenucleosidases and thiaminepyrophosphatase in the mammalian hypothalamus. J. Anat. 130:173–182.Google Scholar
  20. 20.
    Goldfischer, S., Essner, E., and Schiller, B. 1971. Nucleoside diphosphatase and thiamine pyrophosphatase activities in the endoplasmic reticulum and Golgi apparatus. J. Histochem. Cytochem. 19:349–360.Google Scholar
  21. 21.
    Vorbrodt, A. W., and Wisniewski, H. M. 1982. Plasmalemmabound nucleoside diphosphatase as a cytochemical marker of central nervous system (CNS) mesodermal cells. J. Histochem. Cytochem. 30:418–424.Google Scholar
  22. 22.
    Kuhn, N. J., and White, A. 1977. The role of nucleoside diphosphatase in a uridine nucleotide cycle associated with lactose synthesis in rat mammary-gland Golgi apparatus. Biochem. J. 168:423–433.Google Scholar
  23. 23.
    Roth, J., and Berger, E. G. 1982. Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae. J. Cell Biol. 93:223–229.Google Scholar
  24. 24.
    Evan Sadler, J., Beyer, T. A., Oppenheimer, C. L., Paulson, J. C., Prieels, J.-P., Rearick, J. I., and Hill, R. L. 1982. Purification of mammalian glycosyltransferase. Methods Enzymol. 83:458–514.Google Scholar
  25. 25.
    Capasso, J. M., and Hirschberg, C. B. 1984. Mechanisms of glycosylation and sulfation in the Golgi apparatus: evidence for nucleotide sugar/nucleoside monophosphate and nucleotide sulfate/nucleoside monophosphate antiports in the Golgi apparatus membrane. Proc. Natl. Acad. Sci. USA 81:7051–7055.Google Scholar

Copyright information

© Plenum Publishing Corporation 1992

Authors and Affiliations

  • Shuzo Miyamoto
    • 1
  • Yoshihiro Matsuda
    • 1
  • Shin-ichiro Sano
    • 1
  • Hiroshi Shiraki
    • 1
  • Hachro Nakagawa
    • 1
  1. 1.Institute for Protein ResearchOsaka UniversitySuita, OsakaJapan

Personalised recommendations