@article{oai:niigata-u.repo.nii.ac.jp:00022042,
 author = {藤田, 信也},
 issue = {9},
 journal = {新潟医学会雑誌, 新潟医学会雑誌},
 month = {Sep},
 note = {The structures of three forms of mouse myelin-associated glycoprotein(MAG) mRNAs were determined from full-length cDNA clones. Two forms of mRNAs have been reported to be different by alternate inclusion of exon 2 and 12 portions in the rat brain. One of the three forms of clones obtained here appeared to be a novel mRNA which lacked both the exon 2 and 12 portions, although others were identical splicing patterns to those of rat. Two polypeptide isoforms of MAG with molecular masses of 72 and 67 kDa are produced by alternative splicing of the exon 12 portion containing a termination codon. Evidence was presented that expression of the two MAG mRNAs was developmentally regulated in the mouse brain. In the quaking mouse, the mRNA without the exon 12 portion coding the large MAG isoform was scarcely expressed throughout development. Specific antibodies to L-MAG and S-MAG respectively were prepared, and immunoblots showed that the L-MAG band was scarcely detectable in the quaking mouse brain, whereas the S-MAG had a higher apparent molecular mass than in the normal control. Immunohistochemical study also showed that L-MAG was not stained in the quaking mouse brain. These results seemed to reflect a reduction in the L-MAG mRNA and abnormal glycosylation in the quaking mouse brain.},
 pages = {745--755},
 title = {Myelin-associated Glycoprotein(MAG)遺伝子のAlternative Splicingに関する分子生物学的研究},
 volume = {104},
 year = {1990}
}