WEKO3
アイテム
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ヒトのmyelin-associated glycoprotein(MAG)の分子構造およびその発現と蛋白分解に関する研究
http://hdl.handle.net/10191/39330
http://hdl.handle.net/10191/39330845b0c70-5d17-4079-a192-166888591f97
名前 / ファイル | ライセンス | アクション |
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Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2016-03-10 | |||||
タイトル | ||||||
タイトル | ヒトのmyelin-associated glycoprotein(MAG)の分子構造およびその発現と蛋白分解に関する研究 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | ヒトのmyelin-associated glycoprotein(MAG)の分子構造およびその発現と蛋白分解に関する研究 | |||||
言語 | ||||||
言語 | jpn | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | myelin | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | myelin-associated glycoprotein | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | calcium activated neutral protease | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | cDNA cloning | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | ミエリン | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | ミエリン糖蛋白(MAG) | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | カルシウム依存性中性プロテアーゼ | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | cDNAクローニング | |||||
資源タイプ | ||||||
資源 | http://purl.org/coar/resource_type/c_6501 | |||||
タイプ | departmental bulletin paper | |||||
その他のタイトル | ||||||
その他のタイトル | Study on Molecular Structure, Expression and Degradation of Myelin-Associated Glycoprotein (MAG) | |||||
著者 |
佐藤, 修三
× 佐藤, 修三 |
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著者別名 | ||||||
識別子 | 130356 | |||||
識別子Scheme | WEKO | |||||
姓名 | Sato, Shuzo | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | cDNA cloning of human myelin-associated glycoprotein (MAG) revealed complete amino acid sequence. In rodents, expression of the two forms of mRNA is developmentary regulated; the mRNA without exon 12 portion is expressed mainly in the active myelinating stage of development. Although the cDNA library used here was prepared from adult human brain poly (A)+ RNA all clones obtained corresponded to the mRNA without exon 12 portion. It has been demonstrated that the myelin membrane contains an endogenous calcium activated neutral protease (CANP) which degrades myelin basic protein (MBP) and MAG. The myelin endogenous CANP cleaves the 100KDa MAG molecule to a 90KDa derivative called derivative of MAG (dMAG). Since dMAG does not appear to be as tightly bound to membranes as intact MAG, the CANP is supposed (not proven) to cleave C-terminus of MAG. To confirm the proteolytic cleavage sites in MAG molecules, we raised antisera against the sequences of C-terminus of MAG. The peptides unique to large form of MAG (L-MAG) and small form of MAG (S-MAG) were synthesized using an automatic peptide synthesizer. We incubated purified myelin to produce dMAG and examined each anti-MAG antibody. Both anti-L-MAG and anti-S-MAG antibodies did not recognize dMAG. These results indicate that dMAG does not contain the sequences of C-termini in both L-MAG and S-MAG. Phosphorylation sites are thought to be important for functions of MAG as a recognition molecule and located near C-terminus of the cytoplasmic sequence. As dMAG lacks C-terminus, production of dMAG may result in the disturbance of myelin-axon interactions during demyelinating process. | |||||
書誌情報 |
新潟医学会雑誌 en : 新潟医学会雑誌 巻 105, 号 8, p. 540-547, 発行日 1991-08 |
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出版者 | ||||||
出版者 | 新潟医学会 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 00290440 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AN00182415 | |||||
著者版フラグ | ||||||
値 | publisher |