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ID 47059
本文ファイル
著者
Saito, Ryo
Okuma, Yasunobu
Nomura, Yasuyuki
キーワード
Alzheimer’s disease
amyloid β
HRD1
endoplasmic reticulum stress
SEL1L
insolubilization
NDC
医学
抄録(英)
Endoplasmic reticulum (ER)-associated degradation (ERAD) selectively retro-transports and degrades unfolded proteins accumulated in the ER. We have demonstrated that the ubiquitin ligase HRD1 involved in ERAD was significantly decreased in the cerebral cortex of Alzheimer’s disease patients. Furthermore, the HRD1 level was negatively correlated with amyloid β (Aβ) production levels. Here we found that the HRD1 protein level decrease was due to its insolubilization. Moreover, these protein levels extracted from detergent insoluble fraction were positively correlated with those of SEL1L and Aβs (Aβ40 and Aβ42). Thus, the insolubilization-induced decrease in the HRD1 and SEL1L levels might involve in Aβ generation.
内容記述
This study was supported by Grants-in-Aid for Science Research (KAKENHI) 21790089, 21300142, and 20659013 from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and by the Research Foundation for Pharmaceutical Sciences.
掲載誌名
Biological and Pharmaceutical Bulletin
35巻
2号
開始ページ
269
終了ページ
272
出版年月日
2012-02-01
出版者
The Pharmaceutical Society of Japan
ISSN
0918-6158
1347-5215
NCID
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
publisher
権利情報
© 2012 The Pharmaceutical Society of Japan
関連情報URL
部局名
医歯薬保健学研究科