Abstract
After much initial debate for and against the role of amyloid in Alzheimers disease (AD), mutations on the amyloid precursor protein (APP) and processing pathways that increase levels of the amyloid b peptide of 42 residues (Aβ42) have established that faulty function or processing of these proteins are responsible for AD pathogenesis. Given the neurotoxicity of aggregates of Ab42, the central role of this peptide in AD pathogenesis is self evident. In this article, I summarize the major pieces of evidence adduced to support the amyloid cascade hypothesis and point out their limitations
Keywords: APP mutations, neurodegenerative disease, oxidative stress, apolipoprotein, presenilin
Current Alzheimer Research
Title: Has the Amyloid Cascade Hypothesis for Alzheimers Disease been Proved?
Volume: 3 Issue: 1
Author(s): John Hardy
Affiliation:
Keywords: APP mutations, neurodegenerative disease, oxidative stress, apolipoprotein, presenilin
Abstract: After much initial debate for and against the role of amyloid in Alzheimers disease (AD), mutations on the amyloid precursor protein (APP) and processing pathways that increase levels of the amyloid b peptide of 42 residues (Aβ42) have established that faulty function or processing of these proteins are responsible for AD pathogenesis. Given the neurotoxicity of aggregates of Ab42, the central role of this peptide in AD pathogenesis is self evident. In this article, I summarize the major pieces of evidence adduced to support the amyloid cascade hypothesis and point out their limitations
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Cite this article as:
Hardy John, Has the Amyloid Cascade Hypothesis for Alzheimers Disease been Proved?, Current Alzheimer Research 2006; 3 (1) . https://dx.doi.org/10.2174/156720506775697098
DOI https://dx.doi.org/10.2174/156720506775697098 |
Print ISSN 1567-2050 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5828 |
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