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Membrane inserted APP fragments containing the βA4 sequence of Alzheimer's disease do not aggregate
Author(s) -
Dyrks Thomas,
Dyrks Elke,
Masters Colin,
Beyreuther Konrad
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80730-5
Subject(s) - sequence (biology) , membrane , amyloid precursor protein , chemistry , in vitro , n terminus , p3 peptide , amyloid (mycology) , amyloid β , biophysics , alzheimer's disease , biochemistry , peptide , peptide sequence , microbiology and biotechnology , biology , disease , medicine , gene , pathology , inorganic chemistry
Previously we have shown that the COOH‐terminal fragment (A4CT) of the Alzheimer amyloid protein precursor (APP), which at the NH 2 ‐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 NH 2 ‐terminus (SPA4CT) under conditions which allow membrane insertion. Aggregates from SPA4CT are obtained after removal of membranes by chloroform/methanol extraction or heating.