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P3–369: Intraneuronal amyloid–β42 may silence oxidative stress in Alzheimer's disease
Author(s) -
Nunomura Akihiko,
Chiba Shigeru,
Yamaguchi Haruyasu,
Smith Mark A.,
Perry George
Publication year - 2006
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.2006.05.1639
Subject(s) - oxidative stress , hippocampal formation , cytoplasm , chemistry , antibody , amyloid (mycology) , microbiology and biotechnology , biochemistry , endocrinology , biology , immunology , inorganic chemistry
from these partially purified preparations were compared with purified recombinant APP751 expressed in yeast, and ceruloplasmin obtained from commercial sources. Oxidative activity was characterized using various substrates (including PPD; p-Phenylenediamine dihydrochloride) and Fe oxidation, in the presence and absence of Cu and chelators. Results and Conclusion: Plasma APP and ceruloplasmin separated by electroelution both readily oxidized PPD. Cellular APP derived from neuronal (M17 and SY5Y) and hepatic (HepG2) cell lines also oxidized PPD, indicating a ubiquitous activity. Moreover, the oxidase activity of APP is not apparently dependent upon delivery of copper by the copper transporter ATP7A (Menkes protein) as activity was still detected with APP derived from ATP7A-null fibroblast. As the PPD oxidase activity of APP does not require Cu , it is mechanistically more similar to that of ferritin than that of ceruloplasmin.