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ID 47062
file
creator
Ohtake, Yosuke
subject
endoplasmic reticulum stress
unfolded protein response
neurodegenerative disease
diabetes
metabolic syndrome
cancer
NDC
Medical sciences
abstract
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.
journal title
Biological and Pharmaceutical Bulletin
volume
Volume 40
issue
Issue 9
start page
1337
end page
1343
date of issued
2017-09-01
publisher
The Pharmaceutical Society of Japan
issn
0918-6158
1347-5215
ncid
publisher doi
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
publisher
rights
© 2018 The Pharmaceutical Society of Japan
relation url
department
Graduate School of Biomedical & Health Sciences