title: Glycosaminoglycans, protein aggregation and neurodegeneration.
abstract: A number of neurodegenerative diseases, as Parkinson, prion, and Alzheimer's 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.
authors.affiliation: Laboratoire CRRET, EAC/CNRS, Université Paris Est Créteil Val de Marne, Faculté des Sciences et Technologie, France. papy@u-pec.fr
authors.forename: Dulce
authors.initials: D
authors.lastname: Papy-Garcia
authors.forename: Morin
authors.initials: M
authors.lastname: Christophe
authors.forename: Minh Bao
authors.initials: MB
authors.lastname: Huynh
authors.forename: Sineriz
authors.initials: S
authors.lastname: Fernando
authors.forename: Sissoeff
authors.initials: S
authors.lastname: Ludmilla
authors.forename: Julia Elisa
authors.initials: JE
authors.lastname: Sepulveda-Diaz
authors.forename: Rita
authors.initials: R
authors.lastname: Raisman-Vozari
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism; D006025:Glycosaminoglycans / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D019636:Neurodegenerative Diseases / Q000276:immunology / Q000503:physiopathology*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017096:Prion Diseases; D011328:Prions / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D051844:alpha-Synuclein / Q000737:chemistry / Q000378:metabolism; D016875:tau Proteins
chemical_list: D016229:Amyloid beta-Peptides; D006025:Glycosaminoglycans; D008565:Membrane Proteins; D010446:Peptide Fragments; D011328:Prions; D011506:Proteins; D051844:alpha-Synuclein; C075222:amyloid beta-protein (1-42); C054369:MAPT protein, human; D016875:tau Proteins