Contribution of Sulfated Glycosaminoglycans ...
Document type :
Article dans une revue scientifique
DOI :
Permalink :
Title :
Contribution of Sulfated Glycosaminoglycans to the Pathology of Amyloidosis
Author(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
Journal title :
trends in glycoscience and glycotechnology
Volume number :
33
Pages :
E141-E145
Publisher :
Forum: Carbohydrates Coming of Age
Publication date :
2021-11-25
ISSN :
0915-7352
English keyword(s) :
protein misfolding disease
amyloidosis
amyloid
glycosaminoglycan
heparan sulfate
amyloidosis
amyloid
glycosaminoglycan
heparan sulfate
HAL domain(s) :
Sciences du Vivant [q-bio]
Chimie/Chimie théorique et/ou physique
Chimie/Chimie théorique et/ou physique
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Japonais
Japonais
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
Diversité structurale des héparanes sulfates et régulation de la réponse inflammatoire
Submission date :
2023-02-24T14:33:06Z
2023-02-28T15:21:16Z
2023-02-28T15:21:16Z
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