A novel C-domain-dependent inhibition of ...
Type de document :
Article dans une revue scientifique
PMID :
URL permanente :
Titre :
A novel C-domain-dependent inhibition of the rainbow trout CMP-sialic acid synthetase activity by CMP-deaminoneuraminic acid
Auteur(s) :
Wu, Di [Auteur]
Nagoya University
Gilormini, Pierre-André [Auteur]
Simon Fraser University = Université Simon Fraser [SFU.ca]
Toda, Sakura [Auteur]
Nagoya University
Biot, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Lion, Cédric [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Sato, Chihiro [Auteur]
Nagoya University
Kitajima, Ken [Auteur]
Nagoya University
Nagoya University
Gilormini, Pierre-André [Auteur]
Simon Fraser University = Université Simon Fraser [SFU.ca]
Toda, Sakura [Auteur]
Nagoya University
Biot, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Lion, Cédric [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Sato, Chihiro [Auteur]
Nagoya University
Kitajima, Ken [Auteur]
Nagoya University
Titre de la revue :
Biochemical and Biophysical Research Communications
Nom court de la revue :
Biochem Biophys Res Commun
Numéro :
617
Pagination :
16-21
Date de publication :
2022-08-20
ISSN :
1090-2104
Mot(s)-clé(s) en anglais :
Animals
Cytidine Monophosphate
Mice
N-Acetylneuraminic Acid
N-Acylneuraminate Cytidylyltransferase
Neuraminic Acids
Oncorhynchus mykiss
Sialic Acids
CMAS
CMP-Sialic acid synthetase
CSS
Deaminoneuraminic acid
N-acetylneuraminic acid
Rainbow trout
Sialic acid
Cytidine Monophosphate
Mice
N-Acetylneuraminic Acid
N-Acylneuraminate Cytidylyltransferase
Neuraminic Acids
Oncorhynchus mykiss
Sialic Acids
CMAS
CMP-Sialic acid synthetase
CSS
Deaminoneuraminic acid
N-acetylneuraminic acid
Rainbow trout
Sialic acid
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
The CMP-sialic acid synthetase (CSS) activates free sialic acid (Sia) to CMP-Sia using CTP, and is prerequisite for the sialylation of cell surface glycoconjugates. The vertebrate CSS consists of two domains, a catalytic ...
Lire la suite >The CMP-sialic acid synthetase (CSS) activates free sialic acid (Sia) to CMP-Sia using CTP, and is prerequisite for the sialylation of cell surface glycoconjugates. The vertebrate CSS consists of two domains, a catalytic N-domain and a non-catalytic C-domain. Although the C-domain is not required for the CSS enzyme to synthesize CMP-Sia, its involvement in the catalytic activity remains unknown. First, the real-time monitoring of CSS-catalyzed reaction was performed by P NMR using the rainbow trout CSS (rtCSS). While a rtCSS lacking the C-domain (rtCSS-N) similarly activated both deaminoneuraminic acid (Kdn) and N-acetylneuraminic acid (Neu5Ac), the full-length rtCSS (rtCSS-FL) did not activate Kdn as efficiently as Neu5Ac. These results suggest that the C-domain of rtCSS affects the enzymatic activity, when Kdn was used as a substrate. Second, the enzymatic activity of rtCSS-FL and rtCSS-N was measured under various concentrations of CMP-Kdn. Inhibition by CMP-Kdn was observed only for rtCSS-FL, but not for rtCSS-N, suggesting that the inhibition was C-domain-dependent. Third, the inhibitory effect of CMP-Kdn was also investigated using the mouse CSS (mCSS). However, no inhibition was observed with mCSS even at high concentrations of CMP-Kdn. Taken together, the data demonstrated that the C-domain is involved in the CMP-Kdn-dependent inhibition of rtCSS, which is a novel regulation of the Sia metabolism in rainbow trout.Lire moins >
Lire la suite >The CMP-sialic acid synthetase (CSS) activates free sialic acid (Sia) to CMP-Sia using CTP, and is prerequisite for the sialylation of cell surface glycoconjugates. The vertebrate CSS consists of two domains, a catalytic N-domain and a non-catalytic C-domain. Although the C-domain is not required for the CSS enzyme to synthesize CMP-Sia, its involvement in the catalytic activity remains unknown. First, the real-time monitoring of CSS-catalyzed reaction was performed by P NMR using the rainbow trout CSS (rtCSS). While a rtCSS lacking the C-domain (rtCSS-N) similarly activated both deaminoneuraminic acid (Kdn) and N-acetylneuraminic acid (Neu5Ac), the full-length rtCSS (rtCSS-FL) did not activate Kdn as efficiently as Neu5Ac. These results suggest that the C-domain of rtCSS affects the enzymatic activity, when Kdn was used as a substrate. Second, the enzymatic activity of rtCSS-FL and rtCSS-N was measured under various concentrations of CMP-Kdn. Inhibition by CMP-Kdn was observed only for rtCSS-FL, but not for rtCSS-N, suggesting that the inhibition was C-domain-dependent. Third, the inhibitory effect of CMP-Kdn was also investigated using the mouse CSS (mCSS). However, no inhibition was observed with mCSS even at high concentrations of CMP-Kdn. Taken together, the data demonstrated that the C-domain is involved in the CMP-Kdn-dependent inhibition of rtCSS, which is a novel regulation of the Sia metabolism in rainbow trout.Lire moins >
Langue :
Anglais
Comité de lecture :
Oui
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Chemical Glycobiology
Date de dépôt :
2022-07-25T12:25:00Z
2022-08-24T12:44:21Z
2022-08-24T12:44:21Z
Fichiers
- P22.12 Wu Di BBRC 2022.pdf
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