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- W2071803058 endingPage "638" @default.
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- W2071803058 abstract "Growing evidence suggests that mitochondrial dysfunction is one of the key intracellular lesions associated with the pathogenesis of Alzheimer's disease (AD). Mitochondria, the powerhouses of the cell, participate in a number of physiological functions that include calcium homeostasis, signal transduction, and apoptosis. However, the pathophysiological mechanisms underlying the decline of mitochondrial vital functions leading to the dysfunction of mitochondria during AD are not well understood. Recent literature has observed the accumulation of Alzheimer's amyloid precursor protein (APP) and its C-terminal—cleaved product β-amyloid (Aβ) in the mitochondrial compartment. Furthermore, evidence also implicates that the accumulation of full-length APP and Aβ in the mitochondrial compartment has a causative role in impairing mitochondrial physiological functions. Here, we review the mode of mitochondrial transport of full-length APP and Aβ and its pathological implications in bringing about mitochondrial dysfunction as seen in AD. NEUROSCIENTIST 13(6):626—638, 2007. DOI: 10.1177/1073858407303536" @default.
- W2071803058 created "2016-06-24" @default.
- W2071803058 creator A5059299823 @default.
- W2071803058 creator A5063404637 @default.
- W2071803058 date "2007-10-02" @default.
- W2071803058 modified "2023-09-27" @default.
- W2071803058 title "Amyloid Precursor Protein and Mitochondrial Dysfunction in Alzheimer's Disease" @default.
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- W2071803058 doi "https://doi.org/10.1177/1073858407303536" @default.
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