Abstract:
:Alzheimer's disease is characterized by the deposition of amyloid beta-peptide (Abeta) 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 Abeta fragments. As different Abeta 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 Abeta fragments. Our results show a strong correlation between the length of an Abeta-derived segment and its ability to integrate into the microsomal membrane.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lundin C,Johansson S,Johnson AE,Näslund J,von Heijne G,Nilsson Idoi
10.1016/j.febslet.2007.07.003subject
Has Abstractpub_date
2007-08-07 00:00:00pages
3809-13issue
20eissn
0014-5793issn
1873-3468pii
S0014-5793(07)00750-8journal_volume
581pub_type
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