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dc.contributor.authorDu, Heng
dc.contributor.authorYan, Shirley ShiDu
dc.date.accessioned2015-05-28T16:20:11Z
dc.date.available2015-05-28T16:20:11Z
dc.date.issued2010-05-10
dc.identifier.citationDu, Heng, and Shirley Shidu Yan. "Unlocking the Door to Neuronal Woes in Alzheimer’s Disease: Aβ and Mitochondrial Permeability Transition Pore." Pharmaceuticals 3.6 (2010): 1936-948. http://dx.doi.org/10.3390/ph3061936.en_US
dc.identifier.urihttp://hdl.handle.net/1808/17871
dc.descriptionThis is the published version. Copyright 2010 MDPI.en_US
dc.description.abstractMitochondrial dysfunction occurs early in the progression of Alzheimer’s disease. Amyloid-β peptide has deleterious effects on mitochondrial function and contributes to energy failure, respiratory chain impairment, neuronal apoptosis, and generation of reactive oxygen species in Alzheimer’s disease. The mechanisms underlying amyloid-β induced mitochondrial stress remain unclear. Emerging evidence indicates that mitochondrial permeability transition pore is important for maintenance of mitochondrial and neuronal function in aging and neurodegenerative disease. Cyclophilin D (Cyp D) plays a central role in opening mitochondrial permeability transition pores, ultimately leading to cell death. Interaction of amyloid-β with cyclophilin D triggers or enhances the formation of mitochondrial permeability transition pores, consequently exacerbating mitochondrial and neuronal dysfunction, as shown by decreased mitochondrial membrane potential, impaired mitochondrial respiration function, and increased oxidative stress and cytochrome c release. Blockade of cyclophilin D by genetic abrogation or pharmacologic inhibition protects mitochondria and neurons from amyloid-β induced toxicity, suggesting that cyclophilin D dependent mitochondrial transition pores are a therapeutic target for Alzheimer’s disease.en_US
dc.publisherMDPIen_US
dc.titleUnlocking the Door to Neuronal Woes in Alzheimer’s Disease: Aβ and Mitochondrial Permeability Transition Poreen_US
dc.typeArticle
kusw.kuauthorYan, Shirley ShiDu
kusw.kudepartmentPharmacology & Toxicologyen_US
dc.identifier.doi10.3390/ph3061936
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item meets KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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