MEMBRANE INSERTED APP FRAGMENTS CONTAINING THE BETA-A4 SEQUENCE OF ALZHEIMERS-DISEASE DO NOT AGGREGATE

被引：31

作者：

DYRKS, T ^{[1
]}

DYRKS, E ^{[1
]}

MASTERS, C ^{[1
]}

BEYREUTHER, K ^{[1
]}

机构：

[1] UNIV MELBOURNE,DEPT PATHOL,PARKVILLE,VIC 3052,AUSTRALIA

来源：

FEBS LETTERS | 1992年 / 309卷 / 01期

关键词：

A4CT; INVITRO TRANSLATION; AGGREGATION; ALZHEIMERS DISEASE;

D O I：

10.1016/0014-5793(92)80730-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Previously we have shown that the COOH-terminal fragment (A4CT) of the Alzheimer amyloid protein precursor (APP), which at the NH2-terminus carries the sequence of the amyloid beta-A4 protein, forms highly insoluble aggregates [EMBO J. (1988) 7, 949-957]. Here we report that aggregation is prevented if A4CT is expressed in vitro with a signal sequence at the NH2-terminus (SPA4CT) under conditions which allow membrane insertion. Aggregates from SPA4CT are obtained after removal of membranes by chloroform/methanol extraction or heating.

引用

页码：20 / 24

页数：5

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