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Examining the mechanisms that link β-amyloid and α-synuclein pathologies

Samuel E Marsh1 and Mathew Blurton-Jones123*

Author Affiliations

1 Department of Neurobiology & Behavior, University of California, Irvine, Irvine, CA 92697-4545, USA

2 Sue and Bill Gross Stem Cell Research Center, University of California Irvine, Irvine, CA 92697, USA

3 Institute for Memory Impairments and Neurological Disorders, University of California Irvine, Irvine, CA 92697, USA

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Alzheimer's Research & Therapy 2012, 4:11  doi:10.1186/alzrt109

Published: 30 April 2012


β-amyloid (Aβ) and α-synuclein (α-syn) are aggregation-prone proteins typically associated with two distinct neurodegenerative disorders: Alzheimer's disease (AD) and Parkinson's disease. Yet α-syn was first found in association with AD plaques several years before being linked to Parkinson's disease or Lewy body formation. Nowadays, a large subset of AD patients (~50%) is well recognized to co-exhibit significant α-syn Lewy body pathology. Unfortunately, these AD Lewy body variant patients suffer from additional symptoms and an accelerated disease course. Basic research has begun to show that Aβ and α-syn may act synergistically to promote the aggregation and accumulation of each other. While the exact mechanisms by which these proteins interact remain unclear, growing evidence suggests that Aβ may drive α-syn pathology by impairing protein clearance, activating inflammation, enhancing phosphorylation, or directly promoting aggregation. This review examines the interactions between Aβ and α-syn and proposes potential mechanistic links between Aβ accumulation and α-syn pathogenesis.