Membrane inserted APP fragments containing the beta A4 sequence of Alzheimer's disease do not aggregate

T Dyrks; E Dyrks; C Masters; K Beyreuther

doi:10.1016/0014-5793(92)80730-5

Membrane inserted APP fragments containing the beta A4 sequence of Alzheimer's disease do not aggregate

FEBS Lett. 1992 Aug 31;309(1):20-4. doi: 10.1016/0014-5793(92)80730-5.

Authors

T Dyrks¹, E Dyrks, C Masters, K Beyreuther

Affiliation

¹ Center for Molecular Biology, University of Heidelberg, Germany.

PMID: 1511741
DOI: 10.1016/0014-5793(92)80730-5

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alzheimer Disease / metabolism*
Amino Acid Sequence
Amyloid beta-Protein Precursor / genetics
Amyloid beta-Protein Precursor / metabolism*
Animals
Dogs
Humans
Intracellular Membranes / metabolism*
Membrane Proteins / metabolism
Microsomes / metabolism
Molecular Sequence Data
Plasmids
Protein Biosynthesis
RNA, Messenger / genetics
RNA, Messenger / metabolism
Restriction Mapping
Transcription, Genetic

Substances

Amyloid beta-Protein Precursor
Membrane Proteins
RNA, Messenger