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Titolo:
The unfolded protein response and Alzheimer's disease
Autore:
Imaizumi, K; Miyoshi, K; Katayama, T; Yoneda, T; Taniguchi, M; Kudo, T; Tohyama, M;
Indirizzi:
Nara Inst Sci & Technol, Div Struct Cell Biol, Nara 6300101, Japan Nara Inst Sci & Technol Nara Japan 6300101 ell Biol, Nara 6300101, Japan Osaka Univ, Grad Sch Med, Dept Anat & Neurosci, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 eurosci, Suita, Osaka 5650871, Japan Japan Sci & Technol Corp, CREST, Suita, Osaka 5650871, Japan Japan Sci & Technol Corp Suita Osaka Japan 5650871 , Osaka 5650871, Japan Osaka Univ, Grad Sch Med, Dept Clin Neurosci, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 eurosci, Suita, Osaka 5650871, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
fascicolo: 2-3, volume: 1536, anno: 2001,
pagine: 85 - 96
SICI:
0925-4439(20010531)1536:2-3<85:TUPRAA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMYLOID PRECURSOR PROTEIN; ENDOPLASMIC-RETICULUM STRESS; GLUCOSE-REGULATED PROTEINS; CIS-ACTING ELEMENT; KAR2 BIP GENE; TRANSMEMBRANE PROTEIN; TRANSCRIPTION FACTOR; MISSENSE MUTATIONS; SIGNALING PATHWAY; BINDING-PROTEIN;
Keywords:
unfolded protein response; endoplasmic reticulum stress; Alzheimer disease; presenilin; amyloid-beta peptide; GRP78/BiP;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
74
Recensione:
Indirizzi per estratti:
Indirizzo: Imaizumi, K Nara Inst Sci & Technol, Div Struct Cell Biol, 8916-5 Takayama, Nara 6300101, Japan Nara Inst Sci & Technol 8916-5 Takayama Nara Japan 6300101 an
Citazione:
K. Imaizumi et al., "The unfolded protein response and Alzheimer's disease", BBA-MOL BAS, 1536(2-3), 2001, pp. 85-96

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 ERstress 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 19:11:54