Abstract
A number of neurodegenerative diseases, as Parkinson, prion, and Alzheimers diseases, has been directly associated with altered conformations of certain peptides or proteins that assemble to form highly organized aggregates, also called amyloid fibers. Glycosaminoglycans have shown to play important roles on fibrils formation, stability and resistance to proteolysis. This manuscript reviews from basic concepts on the biochemistry and biology of glycosaminoglycans to their implications in neurodegeneration with particular emphasis in pathologic protein aggregation. Prion protein, Aβ42, Tau, and α-synuclein, are all proteins that can interact with glycosaminoglycans. We document here how these interactions may modify protein conformation, aggregation kinetics, and fibers stabilization with important consequences in disease. We also raise questions which answers may make advance the understanding of the implication of GAGs in neurodegeneration.
Keywords: Glycosaminoglycans, heparan sulfate, protein aggregation, prion, Aβ42, tau, α-synuclein, neurodegeneration, amyloid fibers, synuclein, Parkinson disease, Alzheimer's disease, polypeptide aggregation, histopathological method, heparin binding proteins
Current Protein & Peptide Science
Title: Glycosaminoglycans, Protein Aggregation and Neurodegeneration
Volume: 12 Issue: 3
Author(s): Dulce Papy-Garcia, Morin Christophe, Huynh Minh Bao, Sineriz Fernando, Sissoeff Ludmilla, Sepulveda Diaz Julia Elisa and Raisman-Vozari Rita
Affiliation:
Keywords: Glycosaminoglycans, heparan sulfate, protein aggregation, prion, Aβ42, tau, α-synuclein, neurodegeneration, amyloid fibers, synuclein, Parkinson disease, Alzheimer's disease, polypeptide aggregation, histopathological method, heparin binding proteins
Abstract: A number of neurodegenerative diseases, as Parkinson, prion, and Alzheimers diseases, has been directly associated with altered conformations of certain peptides or proteins that assemble to form highly organized aggregates, also called amyloid fibers. Glycosaminoglycans have shown to play important roles on fibrils formation, stability and resistance to proteolysis. This manuscript reviews from basic concepts on the biochemistry and biology of glycosaminoglycans to their implications in neurodegeneration with particular emphasis in pathologic protein aggregation. Prion protein, Aβ42, Tau, and α-synuclein, are all proteins that can interact with glycosaminoglycans. We document here how these interactions may modify protein conformation, aggregation kinetics, and fibers stabilization with important consequences in disease. We also raise questions which answers may make advance the understanding of the implication of GAGs in neurodegeneration.
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Cite this article as:
Papy-Garcia Dulce, Christophe Morin, Minh Bao Huynh, Fernando Sineriz, Ludmilla Sissoeff, Diaz Julia Elisa Sepulveda and Rita Raisman-Vozari, Glycosaminoglycans, Protein Aggregation and Neurodegeneration, Current Protein & Peptide Science 2011; 12 (3) . https://dx.doi.org/10.2174/138920311795860188
DOI https://dx.doi.org/10.2174/138920311795860188 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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