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Glycosaminoglycans, Protein Aggregation and Neurodegeneration

[ Vol. 12 , Issue. 3 ]


Dulce Papy-Garcia, Morin Christophe, Huynh Minh Bao, Sineriz Fernando, Sissoeff Ludmilla, Sepulveda Diaz Julia Elisa and Raisman-Vozari Rita   Pages 258 - 268 ( 11 )


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.


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


Laboratoire CRRET, EAC/CNRS-7149, Universite Paris Est Creteil Val de Marne, Faculte des Sciences et Technologie, 94010 Creteil, France.

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