Multiple γ-secretase product peptides are coordinately increased in concentration in the cerebrospinal fluid of a subpopulation of sporadic Alzheimer's disease subjects.
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概要
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Alcadeinα (Alcα) is a neuronal membrane protein that colocalizes with the Alzheimer's amyloid-β precursor protein (APP). Successive cleavage of APP by β- and γ-secretases generates the aggregatable amyloid-β peptide (Aβ), while cleavage of APP or Alcα by α- and γ-secretases generates non-aggregatable p3 or p3-Alcα peptides. Aβ and p3-Alcα can be recovered from human cerebrospinal fluid (CSF). We have previously reported alternative processing of APP and Alcα in the CSF of some patients with sporadic mild cognitive impairment (MCI) and AD (SAD).
著者
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Suzuki Toshiharu
北海道大学 薬学研究科
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Suzuki Toshiharu
Graduate School Of Pharmaceutical Sciences Hokkaido University
関連論文
- Trafficking of Alzheimer's Disease-Related Membrane Proteins and Its Participation in Disease Pathogenesis
- Interaction of N-Terminal Acetyltransferase with the Cytoplasmic Domain of β-Amyloid Precursor Protein and Its Effect on Aβ Secretion
- 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
- Constitutive Cleavage of the Single-Pass Transmembrane Protein Alcadeinα Prevents Aberrant Peripheral Retention of Kinesin-1
- Multiple γ-secretase product peptides are coordinately increased in concentration in the cerebrospinal fluid of a subpopulation of sporadic Alzheimer's disease subjects
- 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.
- Multiple γ-secretase product peptides are coordinately increased in concentration in the cerebrospinal fluid of a subpopulation of sporadic Alzheimer's disease subjects.
- Increased amyloidogenic processing of transgenic human APP in X11-like deficient mouse brain
- Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP.
- Intracellular Trafficking of the Amyloid beta-Protein Precursor (APP) Regulated by Novel Function of X11-Like