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Lessons from two prevalent amyloidoses—what amylin and Aβ have in common

The amyloidogenic peptide Aβ plays a key role in Alzheimer's disease (AD) forming insoluble aggregates in the brain. The peptide shares its amyloidogenic properties with amylin that forms aggregates in the pancreas of patients with Type 2 Diabetes mellitus (T2DM). While epidemiological studies...

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Autores principales: Götz, Jürgen, Lim, Yun-An, Eckert, Anne
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3737661/
https://www.ncbi.nlm.nih.gov/pubmed/23964237
http://dx.doi.org/10.3389/fnagi.2013.00038
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author Götz, Jürgen
Lim, Yun-An
Eckert, Anne
author_facet Götz, Jürgen
Lim, Yun-An
Eckert, Anne
author_sort Götz, Jürgen
collection PubMed
description The amyloidogenic peptide Aβ plays a key role in Alzheimer's disease (AD) forming insoluble aggregates in the brain. The peptide shares its amyloidogenic properties with amylin that forms aggregates in the pancreas of patients with Type 2 Diabetes mellitus (T2DM). While epidemiological studies establish a link between these two diseases, it is becoming increasingly clear that they also share biochemical features suggesting common pathogenic mechanisms. We discuss commonalities as to how Aβ and amylin deregulate the cellular proteome, how they impair mitochondrial functions, to which receptors they bind, aspects of their clearance and how therapeutic strategies exploit the commonalities between Aβ and amylin. We conclude that research into these two molecules is mutually beneficial for the treatment of AD and T2DM.
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spelling pubmed-37376612013-08-20 Lessons from two prevalent amyloidoses—what amylin and Aβ have in common Götz, Jürgen Lim, Yun-An Eckert, Anne Front Aging Neurosci Neuroscience The amyloidogenic peptide Aβ plays a key role in Alzheimer's disease (AD) forming insoluble aggregates in the brain. The peptide shares its amyloidogenic properties with amylin that forms aggregates in the pancreas of patients with Type 2 Diabetes mellitus (T2DM). While epidemiological studies establish a link between these two diseases, it is becoming increasingly clear that they also share biochemical features suggesting common pathogenic mechanisms. We discuss commonalities as to how Aβ and amylin deregulate the cellular proteome, how they impair mitochondrial functions, to which receptors they bind, aspects of their clearance and how therapeutic strategies exploit the commonalities between Aβ and amylin. We conclude that research into these two molecules is mutually beneficial for the treatment of AD and T2DM. Frontiers Media S.A. 2013-08-08 /pmc/articles/PMC3737661/ /pubmed/23964237 http://dx.doi.org/10.3389/fnagi.2013.00038 Text en Copyright © 2013 Götz, Lim and Eckert. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Neuroscience
Götz, Jürgen
Lim, Yun-An
Eckert, Anne
Lessons from two prevalent amyloidoses—what amylin and Aβ have in common
title Lessons from two prevalent amyloidoses—what amylin and Aβ have in common
title_full Lessons from two prevalent amyloidoses—what amylin and Aβ have in common
title_fullStr Lessons from two prevalent amyloidoses—what amylin and Aβ have in common
title_full_unstemmed Lessons from two prevalent amyloidoses—what amylin and Aβ have in common
title_short Lessons from two prevalent amyloidoses—what amylin and Aβ have in common
title_sort lessons from two prevalent amyloidoses—what amylin and aβ have in common
topic Neuroscience
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3737661/
https://www.ncbi.nlm.nih.gov/pubmed/23964237
http://dx.doi.org/10.3389/fnagi.2013.00038
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