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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)
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Submitter: 鈴木 利治
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