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Altered localization of amyloid precursor protein under endoplasmic reticulum stress.

Abstract：

:Recent reports have shown that the endoplasmic reticulum (ER) stress is relevant to the pathogenesis of Alzheimer disease. Following the amyloid cascade hypothesis, we therefore attempted to investigate the effects of ER stress on amyloid-beta peptide (Abeta) generation. In this study, we found that ER stress altered the localization of amyloid precursor protein (APP) from late compartments to early compartments of the secretory pathway, and decreased the level of Abeta 40 and Abeta 42 release by beta- and gamma-cutting. Transient transfection with BiP/GRP78 also caused a shift of APP and a reduction in Abeta secretion. It was revealed that the ER stress response facilitated binding of BiP/GRP78 to APP, thereby causing it to be retained in the early compartments apart from a location suitable for the cleavages of Abeta. These findings suggest that induction of BiP/GRP78 during ER stress may be one of the regulatory mechanisms of Abeta generation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kudo T,Okumura M,Imaizumi K,Araki W,Morihara T,Tanimukai H,Kamagata E,Tabuchi N,Kimura R,Kanayama D,Fukumori A,Tagami S,Okochi M,Kubo M,Tanii H,Tohyama M,Tabira T,Takeda M

doi

10.1016/j.bbrc.2006.03.173

subject

Has Abstract

pub_date

2006-06-02 00:00:00

pages

525-30

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)00730-3

journal_volume

344

pub_type

杂志文章

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