Journal
FEBS LETTERS
Volume 581, Issue 20, Pages 3809-3813Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.07.003
Keywords
amyloid beta-protein precursor; A beta-peptide; translocon mediated; membrane insertion
Funding
- NIGMS NIH HHS [GM26494, R01 GM026494-27, R01 GM026494-26, R01 GM026494] Funding Source: Medline
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Alzheimer's disease is characterized by the deposition of amyloid P-peptide (All) plaques in the brain. Full-length amyloid-beta precursor protein (APP) is processed by alpha- and beta-secretases to yield soluble APP derivatives and membrane-bound C-terminal fragments, which are further processed by gamma-secretase to a non-amyloidogenic 3 kDa product or to All fragments. As different A beta fragments contain different parts of the APP transmembrane helix, one may speculate that they are retained more or less efficiently in the membrane. Here, we use the translocon-mediated insertion of different APP-derived polypeptide segments into the endoplasmic reticulum membrane to assess the propensities for membrane retention of All fragments. Our results show a strong correlation between the length of an A beta-derived segment and its ability to integrate into the microsomal membrane. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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