Membrane inserted APP fragments containing the βA4 sequence of Alzheimer's disease do not aggregate

FEBS Letters

Dyrks, Thomas²  Masters, Colin¹  Beyreuther, Konrad²  Dyrks, Elke² 

[1] Department of Pathology, University of Melbourne, Parkville, Vic. 3052, Australia;Center for Molecular Biology, University of Heidelberg, Heidelberg, Germany

关键词: A4CT;    In vitro translation;    Aggregation;    Alzheimer's disease;   

DOI  :  10.1016/0014-5793(92)80730-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 βA4 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.

【 授权许可】

Unknown