| | |  | | | | Record from Web of Science® | | | | | | |
| The unfolded protein response and Alzheimer's disease |
|
|
| Author(s): Imaizumi K, Miyoshi K, Katayama T, Yoneda T, Taniguchi M, Kudo T, Tohyama M |
| Source: BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE Volume: 1536 Issue: 2-3 Pages: 85-96 Published: MAY 31 2001 |
| Times Cited: 66 References: 74 |
| Abstract: Disruption of calcium homeostasis, inhibition of protein glycosylation, and reduction of disulfide bonds provoke accumulation of unfolded protein in the endoplasmic reticulum (ER), and are therefore a type of 'ER stress'. Normal cells respond to ER stress by increasing transcription of genes encoding ER-resident chaperones such as GRP78/BiP, GRP94 and protein disulfide isomerase to facilitate protein folding. This induction system is termed the unfolded protein response. Familial Alzheimer's disease-linked presenilin-1 (PS1) mutation downregulates the unfolded protein response and leads to vulnerability to ER stress. The mechanisms by which mutant PS1 affects the ER stress response are attributed to the inhibited activation of ER stress transducers such as IRE1, PERK and ATF6. (C) 2001 Elsevier Science B.V. All rights reserved. |
| Document Type: Review |
| Language: English |
| Reprint Address: Imaizumi, K (reprint author), Nara Inst Sci & Technol, Div Struct Cell Biol, 8916-5 Takayama, Nara 6300101, Japan |
Addresses:
1. Nara Inst Sci & Technol, Div Struct Cell Biol, Nara 6300101, Japan
2. Osaka Univ, Grad Sch Med, Dept Anat & Neurosci, Suita, Osaka 5650871 Japan
3. Japan Sci & Technol Corp, CREST, Suita, Osaka 5650871 Japan
4. Osaka Univ, Grad Sch Med, Dept Clin Neurosci, Suita, Osaka 5650871 Japan |
| Publisher: ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: 444TF |
| ISSN: 0925-4439 |
|
| | | | | | | | | Record from Web of Science® | | | | | | | | | |