2014
DOI: 10.3233/jad-131544
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Abstract: Late-onset Alzheimer’s disease (LOAD) is the most common neurodegenerative disorder in older adults, affecting over 50% of those over age 85. Aging is the most important risk factor for the development of LOAD. Aging is associated with the decrease in the ability of cells to cope with cellular stress, especially protein aggregation. Here we will describe how the process of aging affects pathways that control the processing and degradation of abnormal proteins including amyloid-β (Aβ). Genetic association studi… Show more

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Cited by 20 publications
(18 citation statements)
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References 184 publications
(176 reference statements)
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“…Intracellular Aβ (iAβ) can be degraded by proteasomes via the ubiquitin–proteasome pathway in neurons, 116 lysosomal cathepsin enzymes, 117 proteases (such as insulin-degrading enzyme, a thiol metalloendopeptidase that degrades monomeric Aβ) and insulin. 118 Extracellular Aβ can also be degraded by proteases, such as neprilysin (a membrane-anchored zinc metalloendopeptidase that degrades the Aβ monomers Aβ 1–40 and Aβ 1–42 , and Aβ oligomers), 119 matrix metalloproteinases 2, 3 and 9, 120 glutamate carboxypeptidase II, 121 endothelin-converting enzyme, 122 tissue plasminogen activator, 123 plasmin, 120 angiotensin-converting enzyme, 120 and insulin-degrading enzyme.…”
Section: Clearance Of Amyloid-βmentioning
confidence: 99%
“…Intracellular Aβ (iAβ) can be degraded by proteasomes via the ubiquitin–proteasome pathway in neurons, 116 lysosomal cathepsin enzymes, 117 proteases (such as insulin-degrading enzyme, a thiol metalloendopeptidase that degrades monomeric Aβ) and insulin. 118 Extracellular Aβ can also be degraded by proteases, such as neprilysin (a membrane-anchored zinc metalloendopeptidase that degrades the Aβ monomers Aβ 1–40 and Aβ 1–42 , and Aβ oligomers), 119 matrix metalloproteinases 2, 3 and 9, 120 glutamate carboxypeptidase II, 121 endothelin-converting enzyme, 122 tissue plasminogen activator, 123 plasmin, 120 angiotensin-converting enzyme, 120 and insulin-degrading enzyme.…”
Section: Clearance Of Amyloid-βmentioning
confidence: 99%
“…Since AD is a multifactorial disease with genetic and environmental etiologies, including lifestyle, diet, stress and toxic exposures [45], there is no consensus of the causes of selective neuronal vulnerability in AD. Neurochemical dysfunctions associated with AD include the accumulation of inflammatory factors and reactive oxygen species (ROS), particularly within the hippocampal complex that mediates memory function [67]. These factors contribute to pathological cascades leading to neurodegeneration and synaptic loss and AD.…”
Section: Introductionmentioning
confidence: 99%
“…The most prevalent hypothesis is that AD results from the accumulation of potentially toxic amyloid-β (Aβ) peptides as extracellular senile plaques [7]. Aβ is cleaved from the amyloid-β precursor protein (APP) sequentially by β-secretase (or BACE1) and γ–secretase activity.…”
Section: Introductionmentioning
confidence: 99%
“…Indeed, the age-related FOXO expression has been related to the development of Aβ plaques and AD pathology both through its regulation of oxidative state and even direct regulation of Aβ plaque formation. One of the major mechanisms in the age-related decline of FOXO activity is the corresponding reduction in Hsp70 levels and autophagy, allowing proteotoxicity to grip neurons and lead to apoptosis [170].…”
Section: Foxomentioning
confidence: 99%