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P2‐070: ADAM10 AS A CANDIDATE BIOMARKER FOR ALZHEIMER'S DISEASE
Author(s) -
Maria de França Bram Jessyka,
Manzine Patricia Regina,
Barham Elizabeth Joan,
Vale Francisco A.C.,
SelistredeAraújo Heloisa S.,
Iost Pavarini Sofia Cristina,
Cominetti Marcia Regina
Publication year - 2014
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2014.05.744
Subject(s) - adam10 , dementia , disease , amyloid (mycology) , amyloid precursor protein , biomarker , amyloid precursor protein secretase , medicine , pathological , alzheimer's disease , neuroscience , oncology , psychology , pathology , chemistry , biochemistry , disintegrin , metalloproteinase , matrix metalloproteinase
on APP and A b expressions. YU101, a selective inhibitor of chymotrypsinlike activity of the 20S proteasome, significantly inhibited APP degradation and increased A b generation.Conclusions: In a Drosophila study, the overexpressed Tpr2 suppressed polyglutamine-induced ocular neurodegeneration. Co-chaperone Tpr2 contains two chaperone-binding TPR domains, each of which has seven tetratricopeptide repeat motifs, and a C-terminal DNA J homologous J domain. Tpr2 was highly expressed in astrocytes as well as in neurons in the AD mouse brain. Our results suggest that the ubiquitin-proteasome system is involved in the regulatory mechanism in APP amyloidogenesis and that the anti-amyloidogenic effect of Tpr2 includes important mechanisms of selective proteasome activation and neurodegeneration inhibition. Therefore, the proteasome-dependent trafficking pathway of APP associated with Tpr2 may be a valid therapeutic target for altering A b production in AD brain.