Nos tutelles

CNRS

Nos fédérations

Nos partenaires

Rechercher




Accueil > Animation scientifique > Séminaires passés

Séminaire hebdomadaire - Pr Kazuchika NISHITSUJI - 24 mai 2019 - André Verbert

SEMINAIRE HEBDOMADAIRE DE L’UGSF

"Heparan sulfate S-domains and Sulfs : their possible roles in protein aggregation diseases"

Animé par : Pr Kazuchika NISHITSUJI, Department of Biochemistry, Wakayama Medical University, Wakayama, Japan

Invité de l’Equipe "Diversité des héparanes sulfates et réponse inflammatoire", Fabrice ALLAIN de l’UMR 8576 - Université de Lille - CNRS, dans le cadre du “160ème anniversaire des relations franco-japonaises

Abstract :

Highly sulfated domains of heparan sulfate (HS), also known as HS S-domains, consist of repeated trisulfated disaccharide units [iduronic acid (2S)-glucosamine (NS, 6S)–]. The expression of HS S-domains at the cell surface is determined by two mechanisms : tightly regulated biosynthetic machinery and enzymatic remodeling by extracellular endoglucosamine 6-sulfatases, Sulfs. Intracellular or extracellular deposits of misfolded and aggregated proteins are characteristic of protein aggregation diseases. Although proteins can aggregate alone in vitro, deposits of protein aggregates in vivo contain a number of proteinaceous and non-protein components. We have shown that HS S-domains are one of the non-protein components of these aggregated deposits. HS S-domains are considered to be critical for signal transduction of several growth factors and several disease conditions, such as tumor progression, however, their roles in protein aggregation diseases are not yet fully understood. Here, I will discuss the current understanding of the possible roles of HS S-domains and Sulfs in protein aggregation diseases.

1. Hosono-Fukao, T. et al., Heparan sulfate subdomains that are degraded by Sulf accumulate in cerebral amyloid β plaques of Alzheimer’s disease : evidence from mouse models and patients. Am J Pathol 2012, 180:2056-67.[Link]
2. Kuwabara, K. et al., Cellular Interaction and Cytotoxicity of the Iowa Mutation of Apolipoprotein A-I (ApoA-IIowa) Amyloid Mediated by Sulfate Moieties of Heparan Sulfate. J Biol Chem 2015, 290:24210-21.[Link]
3. Nishitsuji, K., Heparan sulfate S-domains and extracellular sulfatases (Sulfs) : their possible roles in protein aggregation diseases. Glycoconj J 2018, 35:387-396.[Link]
4. Kameyama, H. et al., The Accumulation of Heparan Sulfate S-Domains in Kidney Transthyretin Deposits Accelerates Fibril Formation and Promotes Cytotoxicity. Am J Pathol 2019, 189:308-319.[Link]


About :

Prof Nishitsuji is visiting the UGSF with the support of “le 160ème anniversaire des relations franco-japonaises” from the Embassy of France in Japan. The aim is to discover and explore the French research landscape in the specific field, thereby encouraging the establishment of new French-Japanese collaborations.

Le vendredi 24 mai 2019 à 11h00 au C9 - Salle André Verbert.