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The Large Isoform of Myelin‐Associated Glycoprotein Is Scarcely Expressed in the Quaking Mouse Brain
Author(s) -
Fujita Nobuya,
Sato Shuzo,
Ishiguro Hideaki,
Inuzuka Takashi,
Baba Hiroko,
Kurihara Tadashi,
Takahashi Yasuo,
Miyatake Tadashi
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb04596.x
Subject(s) - myelin associated glycoprotein , gene isoform , alternative splicing , microbiology and biotechnology , exon , myelin , glycoprotein , biology , antiserum , molecular mass , glycosylation , rna splicing , messenger rna , immunohistochemistry , biochemistry , gene , antibody , central nervous system , genetics , endocrinology , enzyme , rna , immunology
Two polypeptide isoforms of myelin‐associated glycoprotein (MAG) with molecular masses of 72 and 67 kDa are produced by alternative splicing of the exon 12 portion. Our previous work has demonstrated that in the quaking mouse brain this alternative splicing is lacking and that the mRNA coding the large MAG isoform (L‐MAG) is scarcely expressed, whereas that of small MAG isoform (S‐MAG) is overexpressed. In the present study, we prepared antisera specific to the S‐MAG and L‐MAG amino acid residues, respectively. Immunoblots showed that the L‐MAG band was scarcely detectable in the quaking mouse brain, whereas the S‐MAG band had an apparently higher molecular mass than in the normal control. Our immunohistochemical study also showed that L‐MAG was scarcely stained in the quaking mouse brain. These results seemed to reflect a reduction in content of L‐MAG mRNA and abnormal glycosylation in the quaking mouse brain.