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Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases

The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases including Alzheimer’s disease, Parkinson’s disease, and prion diseases. It is believed that misfolded and abnormal β-sheets forms of wild-type proteins are the vectors of these diseases by acting as se...

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Autor principal: Sarnataro, Daniela
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6213118/
https://www.ncbi.nlm.nih.gov/pubmed/30304819
http://dx.doi.org/10.3390/ijms19103081
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author Sarnataro, Daniela
author_facet Sarnataro, Daniela
author_sort Sarnataro, Daniela
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description The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases including Alzheimer’s disease, Parkinson’s disease, and prion diseases. It is believed that misfolded and abnormal β-sheets forms of wild-type proteins are the vectors of these diseases by acting as seeds for the aggregation of endogenous proteins. Cellular prion protein (PrP(C)) is a glycosyl-phosphatidyl-inositol (GPI) anchored glycoprotein that is able to misfold to a pathogenic isoform PrP(Sc), the causative agent of prion diseases which present as sporadic, dominantly inherited and transmissible infectious disorders. Increasing evidence highlights the importance of prion-like seeding as a mechanism for pathological spread in Alzheimer’s disease and Tauopathy, as well as other neurodegenerative disorders. Here, we report the latest findings on the mechanisms controlling protein folding, focusing on the ER (Endoplasmic Reticulum) quality control of GPI-anchored proteins and describe the “prion-like” properties of amyloid-β and tau assemblies. Furthermore, we highlight the importance of pathogenic assemblies interaction with protein and lipid membrane components and their implications in both prion and Alzheimer’s diseases
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spelling pubmed-62131182018-11-14 Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases Sarnataro, Daniela Int J Mol Sci Review The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases including Alzheimer’s disease, Parkinson’s disease, and prion diseases. It is believed that misfolded and abnormal β-sheets forms of wild-type proteins are the vectors of these diseases by acting as seeds for the aggregation of endogenous proteins. Cellular prion protein (PrP(C)) is a glycosyl-phosphatidyl-inositol (GPI) anchored glycoprotein that is able to misfold to a pathogenic isoform PrP(Sc), the causative agent of prion diseases which present as sporadic, dominantly inherited and transmissible infectious disorders. Increasing evidence highlights the importance of prion-like seeding as a mechanism for pathological spread in Alzheimer’s disease and Tauopathy, as well as other neurodegenerative disorders. Here, we report the latest findings on the mechanisms controlling protein folding, focusing on the ER (Endoplasmic Reticulum) quality control of GPI-anchored proteins and describe the “prion-like” properties of amyloid-β and tau assemblies. Furthermore, we highlight the importance of pathogenic assemblies interaction with protein and lipid membrane components and their implications in both prion and Alzheimer’s diseases MDPI 2018-10-09 /pmc/articles/PMC6213118/ /pubmed/30304819 http://dx.doi.org/10.3390/ijms19103081 Text en © 2018 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Sarnataro, Daniela
Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases
title Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases
title_full Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases
title_fullStr Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases
title_full_unstemmed Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases
title_short Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases
title_sort attempt to untangle the prion-like misfolding mechanism for neurodegenerative diseases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6213118/
https://www.ncbi.nlm.nih.gov/pubmed/30304819
http://dx.doi.org/10.3390/ijms19103081
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