Contribution of Sulfated Glycosaminoglycans ...
Type de document :
Article dans une revue scientifique
DOI :
URL permanente :
Titre :
Contribution of Sulfated Glycosaminoglycans to the Pathology of Amyloidosis
Auteur(s) :
Nishitsuji, Kazuchika [Auteur]
Wakayama University
Uchimura, Kenji [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Wakayama University
Uchimura, Kenji [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Titre de la revue :
trends in glycoscience and glycotechnology
Numéro :
33
Pagination :
E141-E145
Éditeur :
Forum: Carbohydrates Coming of Age
Date de publication :
2021-11-25
ISSN :
0915-7352
Mot(s)-clé(s) en anglais :
protein misfolding disease
amyloidosis
amyloid
glycosaminoglycan
heparan sulfate
amyloidosis
amyloid
glycosaminoglycan
heparan sulfate
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Intracellular or extracellular deposition of highly ordered fibrillar aggregates is a characteristic of protein misfolding diseases. Proteins can aggregate alone in vitro; however, deposits of fibrillar aggregates in vivo ...
Lire la suite >Intracellular or extracellular deposition of highly ordered fibrillar aggregates is a characteristic of protein misfolding diseases. Proteins can aggregate alone in vitro; however, deposits of fibrillar aggregates in vivo contain a number of proteinaceous and non-protein components in addition to the major protein that forms the aggregates. These components are thought to play critical roles in the pathology of protein misfolding diseases. Among these components, glycosaminoglycans (GAGs), which are heteropolysaccharides that occur in all mammalian tissues, are modified by sulfation that determines specific interactions between GAGs and their protein ligands. This mini-review summarizes our current understanding of how sulfated GAGs contribute to the pathology of protein misfolding diseases, with a particular focus on amyloidosis.Lire moins >
Lire la suite >Intracellular or extracellular deposition of highly ordered fibrillar aggregates is a characteristic of protein misfolding diseases. Proteins can aggregate alone in vitro; however, deposits of fibrillar aggregates in vivo contain a number of proteinaceous and non-protein components in addition to the major protein that forms the aggregates. These components are thought to play critical roles in the pathology of protein misfolding diseases. Among these components, glycosaminoglycans (GAGs), which are heteropolysaccharides that occur in all mammalian tissues, are modified by sulfation that determines specific interactions between GAGs and their protein ligands. This mini-review summarizes our current understanding of how sulfated GAGs contribute to the pathology of protein misfolding diseases, with a particular focus on amyloidosis.Lire moins >
Langue :
Anglais
Japonais
Japonais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Diversité structurale des héparanes sulfates et régulation de la réponse inflammatoire
Date de dépôt :
2023-02-24T14:33:06Z
2023-02-28T15:21:16Z
2023-02-28T15:21:16Z
Fichiers
- P21.55 Sulfated GAGs Pathology Amyloidosis_TIGG2021_KU (1).pdf
- Version soumise (preprint)
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