Stable insertion of Alzheimer Aβ peptide into the ER membrane strongly correlates with its length
2007 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 581, no 20, 3809-3813 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2007. Vol. 581, no 20, 3809-3813 p.
amyloid beta-protein precursor, A beta-peptide, translocon mediated, membrane insertion
IdentifiersURN: urn:nbn:se:su:diva-25792DOI: 10.1016/j.febslet.2007.07.003ISI: 000248903600008OAI: oai:DiVA.org:su-25792DiVA: diva2:200524