ER Stress and Disease: Toward Prevention and Treatment

Biological and Pharmaceutical Bulletin 40 巻 9 号 1337-1343 頁 2017-09-01 発行
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タイトル ( eng )
ER Stress and Disease: Toward Prevention and Treatment
作成者
Ohtake Yosuke
収録物名
Biological and Pharmaceutical Bulletin
40
9
開始ページ 1337
終了ページ 1343
抄録
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.
著者キーワード
endoplasmic reticulum stress
unfolded protein response
neurodegenerative disease
diabetes
metabolic syndrome
cancer
NDC分類
医学 [ 490 ]
言語
英語
資源タイプ 学術雑誌論文
出版者
The Pharmaceutical Society of Japan
発行日 2017-09-01
権利情報
© 2018 The Pharmaceutical Society of Japan
出版タイプ Version of Record(出版社版。早期公開を含む)
アクセス権 オープンアクセス
収録物識別子
[ISSN] 0918-6158
[ISSN] 1347-5215
[NCID] AA10885497
[DOI] 10.1248/bpb.b17-00342
[DOI] https://doi.org/10.1248/bpb.b17-00342