Apple Procyanidins Suppress Amyloidβ-Protein Aggregation | Zendy

Toshihiko Toda | Zendy; Tadahiro Sunagawa | Zendy; Tomomasa Kanda | Zendy; Motoyuki Tagashira | Zendy; Takuji Shirasawa | Zendy; Takahiko Shimizu | Zendy

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Apple Procyanidins Suppress Amyloidβ-Protein Aggregation

Author(s) -

Toshihiko Toda,

Tadahiro Sunagawa,

Tomomasa Kanda,

Motoyuki Tagashira,

Takuji Shirasawa,

Takahiko Shimizu

Publication year - 2011

Publication title -

biochemistry research international

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.631

H-Index - 36

eISSN - 2090-2255

pISSN - 2090-2247

DOI - 10.1155/2011/784698

Subject(s) - caenorhabditis elegans , neuroprotection , neurotoxicity , polyphenol , amyloid β , chemistry , algorithm , biochemistry , biology , pharmacology , computer science , medicine , antioxidant , toxicity , disease , pathology , organic chemistry , gene

Procyanidins (PCs) are major components of the apple polyphenols (APs). We previously reported that treatment with PC extended the mean lifespan of Caenorhabditis elegans (Sunagawa et al., 2011). In order to estimate the neuroprotective effects of PC, we investigated the antiaggregative activity of PC on amyloid β -protein (A β ) aggregation, which is a pathological hallmark of Alzheimer's disease. We herein report that PC significantly suppressed A β 42 aggregation and dissociated A β 42 aggregates in a dose-dependent manner, indicating that PC is a potent suppressor of A β aggregation. Furthermore, PC significantly inhibited A β 42 neurotoxicity and stimulated proliferation in PC-12 cells. These results suggested that the PC and AP acted as neuroprotective factors against toxic A β aggregates.

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