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Gene Expression of a Rat Cerebellar Ca-Binding Protein, Spot 35 Protein

  • Y. Takahashi
  • T. Yamakuni
  • R. Kuwano
  • T. Kumanishi
  • E. Ohama
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 255)

Abstract

About ten years ago we discovered a cerebellar protein, spot 35 protein, during the systematic analysis of the rat brain protein by using two dimensional gel-electrophoresis.1 Then we found that this spot 35 protein is an acidic Ca-binding protein by using 45Ca-binding assay procedure and is localized in Purkinje cells, their dendrite and axons using immunohistochemical examination.2,3 Translational experiment of cerebellar mRNA suggested the transcriptional regulation of gene expression of spot 35 protein.3 Next immunohistochemical studies revealed the developmental changes of Purkinje cells in the rat and human cerebella.4 Furthermore, our neurophysiological study showed involvement of spot 35 protein in modulation of Purkinje cell activity of rat cerebellum.5 Recently, we succeeded in cloning the cDNA encoding this protein.6,7 This cDNA was used to analyze the developmental and regional changes of mRNA coding for spot 35 protein in the rat brain, to probe the in situ hybridization of this mRNA in the rat cerebellum and to isolate the spot 35 gene in order to analyze its structure.

Keywords

Purkinje Cell Noncoding Region Human Cerebellum Internal Granule Cell Layer Purkinje Cell Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Y. Yoshida and Y. Takahashi, Compositional changes in soluble proteins of cerebral mantle, cerebellum and brain stem of rat brain during development: a two-dimensional gel electrophoretic analysis, Neurochem. Res. 5:81 (1980).PubMedCrossRefGoogle Scholar
  2. 2.
    T. Yamakuni, H. Usui, T. Iwanaga, H. Kondo, S. Odani, and Y. Takahashi, Isolation and immunohistochemical localization of a cerebellar protein, Neurosci. Lett. 45:235 (1984).PubMedCrossRefGoogle Scholar
  3. 3.
    T. Yamakuni, K. Araki, and Y. Takahashi, The developmental changes of mRNA levels for a cerebellar protein (spot 35 protein) in the rat brain, FEBS Lett. 188:127 (1985).PubMedCrossRefGoogle Scholar
  4. 4.
    H. Takahashi-Iwanaga, H. Kondo, T. Yamakuni, and Y. Takahashi, An immunohistochemical study on the ontogeny of cell immunoreactive for spot 35 protein, a novel Purkinje cell-specific protein, in the rat cerebella, Dev. Brain Res. 29:225 (1986).CrossRefGoogle Scholar
  5. 5.
    S. Maruyama, G. Zhang, Y. Tamura, T. Yamakuni, and Y. Takahashi, Involvement of spot 35 protein, a cerebellar protein in modulation of Purkinje cell activity of the rat cerebellum, Eur. J. Pharmacol. 108:309 (1985).PubMedCrossRefGoogle Scholar
  6. 6.
    T. Yamakuni, R. Kuwano, S. Odani, N. Miki, Y. Yamaguchi, and Y. Takahashi, Nucleotide sequence of cDNA to mRNA for a cerebellar Ca-binding protein, spot 35 protein, Nucleic Acids Res. 14:6768 (1986).PubMedCrossRefGoogle Scholar
  7. 7.
    T. Yamakuni, R. Kuwano, S. Odani, N. Miki, K. Yamaguchi, and Y. Takahashi, Molecular cloning of cDNA to mRNA for a cerebellar spot 35 protein, J. Neurochem. 48:1590 (1987).PubMedCrossRefGoogle Scholar
  8. 8.
    P. W. Wilson, M. Harding, and D. E. M. Lawson, Putative amino acid sequence of chick calcium-binding protein deduced from a complementary DNA sequence, Nucleic Acids Res. 13:8867 (1985).PubMedCrossRefGoogle Scholar
  9. 9.
    M. Parmentier, D. E. M. Lawson, and G. Vassart, Human 27-KDA calbindin complementary DNA sequence, evolutionary and functional implications, Eur. J. Biochem. 170:207 (1987).PubMedCrossRefGoogle Scholar
  10. 10.
    T. Yamakuni, R. Kuwano, K. Araki, H. Usui, Y. Inoue, and Y. Takahashi, Developmental and regional changes of mRNA for a cerebellar protein (spot 35) in the rat brain, J. Neurochem. 50:282 (1988).PubMedCrossRefGoogle Scholar
  11. 11.
    J. J. Leary, D. J. Brigati, and D. C. Ward, Rapid and sensitive colorimetrie method for visualizing biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bio-blots, Proc. Natl. Acad. Sci. U.S.A. 80:4045 (1983).PubMedCrossRefGoogle Scholar
  12. 12.
    P. W. Wilson, J. Rogers, M. Harding, V. Pohl, G. Pattyn, and D. E. M. Lawson, Structure of chick chromosomal genes for calbindin and calretinin, J. Mol. Biol. 200:615 (1988).PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Y. Takahashi
    • 1
  • T. Yamakuni
    • 1
  • R. Kuwano
    • 1
  • T. Kumanishi
    • 2
  • E. Ohama
    • 3
  1. 1.Departments of Neuropharmacology, Brain Research InstituteNiigata UniversityNiigata 951Japan
  2. 2.Departments of Neuropathology, Brain Research InstituteNiigata UniversityNiigata 951Japan
  3. 3.Departments of Experimental Neuropathology, Brain Research InstituteNiigata UniversityNiigata 951Japan

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