期刊论文详细信息
Journal of Veterinary Medical Science
Binding of Curcumin to Senile Plaques and Cerebral Amyloid Angiopathy in the Aged Brain of Various Animals and to Neurofibrillary Tangles in Alzheimer's Brain
Akihiko TAKASHIMA2  Mayu MUTSUGA3  Tatsuya MIZOROGI2  Kazuyuki UCHIDA3  Takao MAKIBUCHI1  Meina TEI3  Hiroyuki NAKAYAMA3  James Kenn CHAMBERS3 
[1]National Saigata Hospital
[2]RIKEN, Brain Science Institute
[3]Department of Veterinary Pathology, Graduate School of Agricultural and Life Sciences, The University of Tokyo
关键词: β amyloid;    cerebral amyloid angiopathy;    curcumin;    neurofibrillary tangle;    senile plaque;   
DOI  :  10.1292/jvms.11-0307
学科分类:兽医学
来源: Japanese Society of Veterinary Science
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【 摘 要 】
References(30)Cited-By(14)The binding of curcumin to senile plaques (SPs) and cerebral amyloid angiopathy (CAA) was examined in the aged brain of various animal species and a human patient with Alzheimer's disease (AD), together with its binding to neurofibrillary tangles (NFTs). Brain sections were immunostained with anti-amyloid β protein 1-42 (Aβ42) and anti-amyloid β protein 1-40 (Aβ40) antibodies. These sections were also stained with alkaline Congo red, periodic acid-methenamine silver (PAM), and curcumin (0.009% curcumin solution) with or without formic acid pretreatment. The sections from the AD brain were also immunostained for anti-paired helical filament-tau (PHF-tau), and were stained with Gallyas silver for NFTs. Some SPs in the AD, monkey, dog, bear, and amyloid precursor protein transgenic mouse (APP Tg-mouse) brains contained congophilic materials, and were intensely positive for curcumin. In addition, curcumin labeled some diffuse SPs negative for Congo red in the AD, monkey, bear, and APP Tg-mouse brains. In all animals, CAA was intensely positive for both Congo red and curcumin. The specific curcumin staining activity was lost by formic acid pretreatment. In the AD brain, NFTs positive for PHF-tau and Gallyas silver were moderately stained with curcumin. These findings indicate that curcumin specifically binds to the aggregated Aβ molecules in various animals, and further to phosphorylated tau protein, probably according to its conformational nature.
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