Ganglioside G(D1α) in cerebellar Purkinje cells: Its specific absence in mouse mutants with Purkinje cell abnormality and altered immunoreactivity in response tc conjunctive stimuli causing long term desensitization

S. Furuya, F. Irie, T. Hashikawa, K. Nakazawa, A. Kozakai, A. Hasegawa, K. Sudo, Y. Hirabayashi

研究成果: ジャーナルへの寄稿記事

49 引用 (Scopus)

抄録

The α-series ganglioside, IV3NeuAc,III6NeuAcGgOse4Cer (G(D1α)), was previously identified as a minor constituent in bovine brain gangliosides (Hirabayashi, Y., Hyogo, A., Nakao, T., Tsuchiya, K., Suzuki, Y., Matsumoto, M., Kon, K., and Ando, S. (1990) J. Biol. Chem. 265, 81448151). In the present study, we have generated a specific mouse monoclonal antibody against G(D1α) and explored the distribution of G(D1α) in murine central nervous system. In adult rat brain, G(D1α) occurred as a minor constituent, and its expression was exclusively detected in the forebrain, the midbrain and the cerebellum. In the mouse cerebellum, the content of G(D1α) was reduced significantly in the Purkinje cell-deficient mutants, lurcher (Lc/+), staggerer (sg/sg), and Purkinje cell degeneration (pcd/pcd), but were not reduced in the weaver (wv/wv) mutant, which loses mostly granule cells. The G(D1α) synthase, assayed in cerebellar microsomes, was also reduced in Purkinje cell-deficient mutants. Immunohistochemistry showed that the staining for G(D1α) in rat and mouse cerebella was mostly found in the proximal dendrites and cell bodies of Purkinje cells. Also, it appeared slightly in the processes of Bergmann glial cells. The immunoreactivity of G(D1α) disappeared specifically from the Purkinje cell dendrites and the Bergmann glial processes after co-application of α-amino-3-hydroxy-5- methyl-4-isoxazolepropionic acid (AMPA) and 8-bromo-guanosine 3':5'-cyclic monophosphate, which induced long-term desensitization of the AMPA-selective glutamate receptors in Purkinje cells. The present data provide suggestive evidence that G(D1α) ganglioside is enriched in Purkinje cells and may have a role in Purkinje cell functions in the cerebellum.

元の言語英語
ページ(範囲)32418-32425
ページ数8
ジャーナルJournal of Biological Chemistry
269
発行部数51
出版物ステータス出版済み - 12 1 1994
外部発表Yes

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Gangliosides
Purkinje Cells
alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
Rats
Brain
Cerebellum
Glutamate Receptors
Neurology
Dendrites
Monoclonal Antibodies
Cells
Neuroglia
Acids
Guanosine
Prosencephalon
Mesencephalon
Microsomes
Central Nervous System
Immunohistochemistry
Staining and Labeling

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Ganglioside G(D1α) in cerebellar Purkinje cells : Its specific absence in mouse mutants with Purkinje cell abnormality and altered immunoreactivity in response tc conjunctive stimuli causing long term desensitization. / Furuya, S.; Irie, F.; Hashikawa, T.; Nakazawa, K.; Kozakai, A.; Hasegawa, A.; Sudo, K.; Hirabayashi, Y.

:: Journal of Biological Chemistry, 巻 269, 番号 51, 01.12.1994, p. 32418-32425.

研究成果: ジャーナルへの寄稿記事

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title = "Ganglioside G(D1α) in cerebellar Purkinje cells: Its specific absence in mouse mutants with Purkinje cell abnormality and altered immunoreactivity in response tc conjunctive stimuli causing long term desensitization",
abstract = "The α-series ganglioside, IV3NeuAc,III6NeuAcGgOse4Cer (G(D1α)), was previously identified as a minor constituent in bovine brain gangliosides (Hirabayashi, Y., Hyogo, A., Nakao, T., Tsuchiya, K., Suzuki, Y., Matsumoto, M., Kon, K., and Ando, S. (1990) J. Biol. Chem. 265, 81448151). In the present study, we have generated a specific mouse monoclonal antibody against G(D1α) and explored the distribution of G(D1α) in murine central nervous system. In adult rat brain, G(D1α) occurred as a minor constituent, and its expression was exclusively detected in the forebrain, the midbrain and the cerebellum. In the mouse cerebellum, the content of G(D1α) was reduced significantly in the Purkinje cell-deficient mutants, lurcher (Lc/+), staggerer (sg/sg), and Purkinje cell degeneration (pcd/pcd), but were not reduced in the weaver (wv/wv) mutant, which loses mostly granule cells. The G(D1α) synthase, assayed in cerebellar microsomes, was also reduced in Purkinje cell-deficient mutants. Immunohistochemistry showed that the staining for G(D1α) in rat and mouse cerebella was mostly found in the proximal dendrites and cell bodies of Purkinje cells. Also, it appeared slightly in the processes of Bergmann glial cells. The immunoreactivity of G(D1α) disappeared specifically from the Purkinje cell dendrites and the Bergmann glial processes after co-application of α-amino-3-hydroxy-5- methyl-4-isoxazolepropionic acid (AMPA) and 8-bromo-guanosine 3':5'-cyclic monophosphate, which induced long-term desensitization of the AMPA-selective glutamate receptors in Purkinje cells. The present data provide suggestive evidence that G(D1α) ganglioside is enriched in Purkinje cells and may have a role in Purkinje cell functions in the cerebellum.",
author = "S. Furuya and F. Irie and T. Hashikawa and K. Nakazawa and A. Kozakai and A. Hasegawa and K. Sudo and Y. Hirabayashi",
year = "1994",
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T1 - Ganglioside G(D1α) in cerebellar Purkinje cells

T2 - Its specific absence in mouse mutants with Purkinje cell abnormality and altered immunoreactivity in response tc conjunctive stimuli causing long term desensitization

AU - Furuya, S.

AU - Irie, F.

AU - Hashikawa, T.

AU - Nakazawa, K.

AU - Kozakai, A.

AU - Hasegawa, A.

AU - Sudo, K.

AU - Hirabayashi, Y.

PY - 1994/12/1

Y1 - 1994/12/1

N2 - The α-series ganglioside, IV3NeuAc,III6NeuAcGgOse4Cer (G(D1α)), was previously identified as a minor constituent in bovine brain gangliosides (Hirabayashi, Y., Hyogo, A., Nakao, T., Tsuchiya, K., Suzuki, Y., Matsumoto, M., Kon, K., and Ando, S. (1990) J. Biol. Chem. 265, 81448151). In the present study, we have generated a specific mouse monoclonal antibody against G(D1α) and explored the distribution of G(D1α) in murine central nervous system. In adult rat brain, G(D1α) occurred as a minor constituent, and its expression was exclusively detected in the forebrain, the midbrain and the cerebellum. In the mouse cerebellum, the content of G(D1α) was reduced significantly in the Purkinje cell-deficient mutants, lurcher (Lc/+), staggerer (sg/sg), and Purkinje cell degeneration (pcd/pcd), but were not reduced in the weaver (wv/wv) mutant, which loses mostly granule cells. The G(D1α) synthase, assayed in cerebellar microsomes, was also reduced in Purkinje cell-deficient mutants. Immunohistochemistry showed that the staining for G(D1α) in rat and mouse cerebella was mostly found in the proximal dendrites and cell bodies of Purkinje cells. Also, it appeared slightly in the processes of Bergmann glial cells. The immunoreactivity of G(D1α) disappeared specifically from the Purkinje cell dendrites and the Bergmann glial processes after co-application of α-amino-3-hydroxy-5- methyl-4-isoxazolepropionic acid (AMPA) and 8-bromo-guanosine 3':5'-cyclic monophosphate, which induced long-term desensitization of the AMPA-selective glutamate receptors in Purkinje cells. The present data provide suggestive evidence that G(D1α) ganglioside is enriched in Purkinje cells and may have a role in Purkinje cell functions in the cerebellum.

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