A truncated Reelin protein is produced but not secreted in the 'Orleans' reeler mutation (Reln(rl-Orl))

V. De Bergeyck, Kazunori Nakajima, C. Lambert de Rouvrait, B. Naerhuyzen, A. M. Goffinet, T. Miyata, M. Ogawa, K. Mikoshiba

研究成果: Article

104 引用 (Scopus)

抄録

Reelin is the protein defective in reeler mutant mice. In the Orleans allele of reeler (symbol: Reln(rl-Orl)), a 220 nucleotide deletion is present in the 3' region of the Reelin message, resulting in a frame shift with production of a predicted protein amputated from its C-terminal amino acids. In this study, we first show that the predicted truncated protein indeed exists in Orleans reeler mice, using several anti-Reelin antibodies. Three antibodies are directed against epitopes located in the N-terminal region of the protein, namely: monoclonal antibody CR-50 (epitope region between Reelin residues 251-407), monoclonal antibody G10 (epitope located between amino acids 199 and 244) and the polyclonal antipeptide rp4 (positions 381-399). A fourth antibody, antipeptide rp5, reacts with the C-terminal (3443-3461) Reelin sequence. In normal embryos, all four antibodies stained cells in the marginal zone with features of Cajal-Retzius cells. While N-terminal specific antibodies detected Reelin immunoreactivity in mouse embryos homozygous for the reeler-Orleans mutation, no staining was obtained with the rp5 antibody, showing the presence of a truncated protein. Moreover, although Reelin could be detected at the surface of living Cajal-Retzius cells of normal mice, it was not revealed after vital staining of embryonic cortex from Orleans reeler mice. These results indicate that the C-terminal region of Reelin is essential for its secretion and suggest that the Orleans reeler phenotype is due to defective Reelin secretion rather than to secretion of an inactive protein.

元の言語English
ページ(範囲)85-90
ページ数6
ジャーナルMolecular Brain Research
50
発行部数1-2
DOI
出版物ステータスPublished - 1997 10 15
外部発表Yes

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Neurologic Mutant Mice
Mutation
Antibodies
Epitopes
Proteins
Embryonic Structures
Monoclonal Antibodies
Staining and Labeling
Amino Acids
Anti-Idiotypic Antibodies
Nucleotides
Alleles
reelin protein
Phenotype

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience

これを引用

De Bergeyck, V., Nakajima, K., Lambert de Rouvrait, C., Naerhuyzen, B., Goffinet, A. M., Miyata, T., ... Mikoshiba, K. (1997). A truncated Reelin protein is produced but not secreted in the 'Orleans' reeler mutation (Reln(rl-Orl)). Molecular Brain Research, 50(1-2), 85-90. https://doi.org/10.1016/S0169-328X(97)00166-6

A truncated Reelin protein is produced but not secreted in the 'Orleans' reeler mutation (Reln(rl-Orl)). / De Bergeyck, V.; Nakajima, Kazunori; Lambert de Rouvrait, C.; Naerhuyzen, B.; Goffinet, A. M.; Miyata, T.; Ogawa, M.; Mikoshiba, K.

:: Molecular Brain Research, 巻 50, 番号 1-2, 15.10.1997, p. 85-90.

研究成果: Article

De Bergeyck, V, Nakajima, K, Lambert de Rouvrait, C, Naerhuyzen, B, Goffinet, AM, Miyata, T, Ogawa, M & Mikoshiba, K 1997, 'A truncated Reelin protein is produced but not secreted in the 'Orleans' reeler mutation (Reln(rl-Orl))', Molecular Brain Research, 巻. 50, 番号 1-2, pp. 85-90. https://doi.org/10.1016/S0169-328X(97)00166-6
De Bergeyck, V. ; Nakajima, Kazunori ; Lambert de Rouvrait, C. ; Naerhuyzen, B. ; Goffinet, A. M. ; Miyata, T. ; Ogawa, M. ; Mikoshiba, K. / A truncated Reelin protein is produced but not secreted in the 'Orleans' reeler mutation (Reln(rl-Orl)). :: Molecular Brain Research. 1997 ; 巻 50, 番号 1-2. pp. 85-90.
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abstract = "Reelin is the protein defective in reeler mutant mice. In the Orleans allele of reeler (symbol: Reln(rl-Orl)), a 220 nucleotide deletion is present in the 3' region of the Reelin message, resulting in a frame shift with production of a predicted protein amputated from its C-terminal amino acids. In this study, we first show that the predicted truncated protein indeed exists in Orleans reeler mice, using several anti-Reelin antibodies. Three antibodies are directed against epitopes located in the N-terminal region of the protein, namely: monoclonal antibody CR-50 (epitope region between Reelin residues 251-407), monoclonal antibody G10 (epitope located between amino acids 199 and 244) and the polyclonal antipeptide rp4 (positions 381-399). A fourth antibody, antipeptide rp5, reacts with the C-terminal (3443-3461) Reelin sequence. In normal embryos, all four antibodies stained cells in the marginal zone with features of Cajal-Retzius cells. While N-terminal specific antibodies detected Reelin immunoreactivity in mouse embryos homozygous for the reeler-Orleans mutation, no staining was obtained with the rp5 antibody, showing the presence of a truncated protein. Moreover, although Reelin could be detected at the surface of living Cajal-Retzius cells of normal mice, it was not revealed after vital staining of embryonic cortex from Orleans reeler mice. These results indicate that the C-terminal region of Reelin is essential for its secretion and suggest that the Orleans reeler phenotype is due to defective Reelin secretion rather than to secretion of an inactive protein.",
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T1 - A truncated Reelin protein is produced but not secreted in the 'Orleans' reeler mutation (Reln(rl-Orl))

AU - De Bergeyck, V.

AU - Nakajima, Kazunori

AU - Lambert de Rouvrait, C.

AU - Naerhuyzen, B.

AU - Goffinet, A. M.

AU - Miyata, T.

AU - Ogawa, M.

AU - Mikoshiba, K.

PY - 1997/10/15

Y1 - 1997/10/15

N2 - Reelin is the protein defective in reeler mutant mice. In the Orleans allele of reeler (symbol: Reln(rl-Orl)), a 220 nucleotide deletion is present in the 3' region of the Reelin message, resulting in a frame shift with production of a predicted protein amputated from its C-terminal amino acids. In this study, we first show that the predicted truncated protein indeed exists in Orleans reeler mice, using several anti-Reelin antibodies. Three antibodies are directed against epitopes located in the N-terminal region of the protein, namely: monoclonal antibody CR-50 (epitope region between Reelin residues 251-407), monoclonal antibody G10 (epitope located between amino acids 199 and 244) and the polyclonal antipeptide rp4 (positions 381-399). A fourth antibody, antipeptide rp5, reacts with the C-terminal (3443-3461) Reelin sequence. In normal embryos, all four antibodies stained cells in the marginal zone with features of Cajal-Retzius cells. While N-terminal specific antibodies detected Reelin immunoreactivity in mouse embryos homozygous for the reeler-Orleans mutation, no staining was obtained with the rp5 antibody, showing the presence of a truncated protein. Moreover, although Reelin could be detected at the surface of living Cajal-Retzius cells of normal mice, it was not revealed after vital staining of embryonic cortex from Orleans reeler mice. These results indicate that the C-terminal region of Reelin is essential for its secretion and suggest that the Orleans reeler phenotype is due to defective Reelin secretion rather than to secretion of an inactive protein.

AB - Reelin is the protein defective in reeler mutant mice. In the Orleans allele of reeler (symbol: Reln(rl-Orl)), a 220 nucleotide deletion is present in the 3' region of the Reelin message, resulting in a frame shift with production of a predicted protein amputated from its C-terminal amino acids. In this study, we first show that the predicted truncated protein indeed exists in Orleans reeler mice, using several anti-Reelin antibodies. Three antibodies are directed against epitopes located in the N-terminal region of the protein, namely: monoclonal antibody CR-50 (epitope region between Reelin residues 251-407), monoclonal antibody G10 (epitope located between amino acids 199 and 244) and the polyclonal antipeptide rp4 (positions 381-399). A fourth antibody, antipeptide rp5, reacts with the C-terminal (3443-3461) Reelin sequence. In normal embryos, all four antibodies stained cells in the marginal zone with features of Cajal-Retzius cells. While N-terminal specific antibodies detected Reelin immunoreactivity in mouse embryos homozygous for the reeler-Orleans mutation, no staining was obtained with the rp5 antibody, showing the presence of a truncated protein. Moreover, although Reelin could be detected at the surface of living Cajal-Retzius cells of normal mice, it was not revealed after vital staining of embryonic cortex from Orleans reeler mice. These results indicate that the C-terminal region of Reelin is essential for its secretion and suggest that the Orleans reeler phenotype is due to defective Reelin secretion rather than to secretion of an inactive protein.

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KW - Reelin

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