Pathogens 2013, 2(3), 506-519; doi:10.3390/pathogens2030506
Curcumin Reduces Amyloid Fibrillation of Prion Protein and Decreases Reactive Oxidative Stress
1
Department of Life Science, Institute of Molecular Biology and Institute of Biomedical Science, College of Science, National Chung Cheng University, Min-Hsiung, Chia-Yi, Taiwan 621, China
2
Department of Clinical Pathology, Buddhist Dalin Tzu Chi General Hospital, Chia-Yi, Taiwan 622, China
3
Department of Chemistry and Biochemistry, Manhattan College, Riverdale, NY 10471, USA
†
Two authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Received: 10 July 2013 / Revised: 17 July 2013 / Accepted: 21 July 2013 / Published: 25 July 2013
(This article belongs to the Special Issue Prions)
Abstract
Misfolding and aggregation into amyloids of the prion protein (PrP) is responsible for the development of fatal transmissible neurodegenerative diseases. Various studies on curcumin demonstrate promise for the prevention of Alzheimer’s disease and inhibition of PrPres accumulation. To evaluate the effect of curcumin on amyloid fibrillation of prion protein, we first investigated the effect of curcumin on mouse prion protein (mPrP) in a cell-free system. Curcumin reduced the prion fibril formation significantly. Furthermore, we monitored the change in apoptosis and reactive oxygen species (ROS) level upon curcumin treatment in mouse neuroblastoma cells (N2a). Curcumin effectively rescues the cells from apoptosis and decreases the ROS level caused by subsequent co-incubation with prion amyloid fibrils. The assays in cell-free mPrP and in N2a cells of this work verified the promising effect of curcumin on the prevention of transmissible neurodegenerative diseases. View Full-Text
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Lin, C.-F.; Yu, K.-H.; Jheng, C.-P.; Chung, R.; Lee, C.-I. Curcumin Reduces Amyloid Fibrillation of Prion Protein and Decreases Reactive Oxidative Stress. Pathogens 2013, 2, 506-519.
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