このエントリーをはてなブックマークに追加
ID 47062
本文ファイル
著者
Kaneko, Masayuki 大学院医歯薬保健学研究科(医) 広大研究者総覧
Imaizumi, Kazunori 大学院医歯薬保健学研究科(医) 広大研究者総覧
Saito, Atsushi 大学院医歯薬保健学研究科(医) 広大研究者総覧
Kanemoto, Soshi 大学院医歯薬保健学研究科(医)
Asada, Rie 大学院医歯薬保健学研究科(医)
Matsuhisa, Koji 大学院医歯薬保健学研究科(医) 広大研究者総覧
Ohtake, Yosuke
キーワード
endoplasmic reticulum stress
unfolded protein response
neurodegenerative disease
diabetes
metabolic syndrome
cancer
NDC
医学
抄録(英)
Secretory and membrane proteins are synthesized in ribosomes, then mature in the endoplasmic reticulum (ER), but if ER function is impaired, immature defective proteins accumulate in the ER. This situation is called ER stress: in response, a defensive mechanism called the unfolded protein response (UPR) is activated in cells to reduce the defective proteins. During the UPR, the ER transmembrane sensor molecules inositol-requiring enzyme 1 (IRE1), activating transcription factor 6 (ATF6), and RNA-dependent protein kinase (PKR)-like ER kinase (PERK) are activated, stress signals are transduced to the outside of the ER, and various cell responses, including gene induction, occur. In ER-associated degradation (ERAD), one type of UPR, defective proteins are eventually expelled from the ER and degraded in the cytoplasm through the ubiquitin proteasome system. Since ER stress has been reported to have relationships with neurodegenerative diseases, diabetes, metabolic syndromes, and cancer, it is the focus of increased attention from the perspectives of elucidating pathogenic mechanisms, and in the development of therapeutics.
掲載誌名
Biological and Pharmaceutical Bulletin
40巻
9号
開始ページ
1337
終了ページ
1343
出版年月日
2017-09-01
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
© 2018 The Pharmaceutical Society of Japan
関連情報URL
部局名
医歯薬保健学研究科