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Coordinated increase of γ-secretase reaction products in the plasma of some female Japanese sporadic Alzheimer's disease patients: quantitative analysis of p3-Alcα with a new ELISA system.

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Title: Coordinated increase of γ-secretase reaction products in the plasma of some female Japanese sporadic Alzheimer's disease patients: quantitative analysis of p3-Alcα with a new ELISA system.
Authors: Konno, Tomoko Browse this author
Hata, Saori Browse this author →KAKEN DB
Hamada, Yukiko Browse this author
Horikoshi-Sakuraba, Yuko Browse this author
Nakaya, Tadashi Browse this author
Saito, Yuhki Browse this author →KAKEN DB
Yamamoto, Tohru Browse this author →KAKEN DB
Yamamoto, Takayuki Browse this author
Maeda, Masahiro Browse this author
Ikeuchi, Takeshi Browse this author →KAKEN DB
Gandy, Sam Browse this author
Akatsu, Hiroyasu Browse this author
Suzuki, Toshiharu Browse this author →KAKEN DB
Issue Date: 2011
Publisher: BioMed Central
Journal Title: Molecular neurodegeneration
Volume: 6
Start Page: 76
Publisher DOI: 10.1186/1750-1326-6-76
PMID: 22067061
Abstract: Aggregatable amyloid β-peptide (Aβ) and non-aggregatable p3-Alcα are metabolic products of the γ-secretase cleavage of amyloid β-protein precursor (APP) and Alcadeinα (Alcα), respectively. Familial AD (FAD) -linked mutations in the presenilin 1 or 2 (PS1 or PS2) component of γ-secretase can cause alternative intramembranous processing of APP and Alcα, leading to a coordinated generation of variants of both Aβ and p3-Alcα. Variant Alcα peptides have been observed in the cerebrospinal fluid (CSF) of patients with mild cognitive impairment and sporadic Alzheimer's disease (AD). Since, like APP, Alcα is largely expressed in brain, one might predict that alternative processing of Alcα would be reflected in body fluids of some AD patients. These patients with misprocessing of multiple γ-secretase substrates might define an endophenotype of p3-Alcα, in whom AD is due either to dysfunction of γ-secretase or to a disorder of the clearance of hydrophobic peptides such as those derived from transmembrane domains.
Rights: http://creativecommons.org/licenses/by/3.0/
Type: article
URI: http://hdl.handle.net/2115/51697
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 鈴木 利治

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