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• W4220777737 abstract "La O-GlcNAcylation (addition de N-Acétyl glucosamine [GlcNAc] sur sérine ou thréonine) est une modification post-traductionnelle réversible des protéines cytosoliques, nucléaires et mitochondriales. À l’instar des phosphorylations, cette modification contrôle l’activité, la stabilité et la localisation subcellulaire des protéines. La O-GlcNAcylation peut en outre contrôler positivement ou négativement la phosphorylation des protéines, et moduler ainsi la signalisation cellulaire. Deux enzymes seulement, l’O-GlcNAc transférase (OGT) et l’O-GlcNAcase (OGA), contrôlent l’addition ou la suppression de la GlcNAc sur les protéines. Cette modification post-traductionnelle dépend de l’environnement énergétique de la cellule, et en particulier de la disponibilité en glucose. De nombreux travaux ont montré que dans les situations d’hyperglycémie chronique, des niveaux de O-GlcNAcylation anormalement élevées sur les protéines participent aux complications observées dans des pathologies comme le diabète et l’obésité. Cependant, plusieurs études récentes utilisant des modèles animaux présentant des délétions tissu-spécifiques de l’OGT indiquent que la O-GlcNAcylation est indispensable au maintien de l’homéostasie énergétique, qu’elle atténue les processus inflammatoires et qu’elle a un rôle protecteur vis-à-vis de différents stress cellulaires comme le stress du réticulum endoplasmique ou le stress oxydant. O-GlcNAcylation (addition of N-Acetyl glucosamine [GlcNAc] to serine or threonine) is a reversible post-translational modification of cytosolic, nuclear and mitochondrial proteins. Like phosphorylations, this modification regulates the activity, stability and subcellular localization of proteins. In addition, O-GlcNAcylation can up-regulate or down-regulate protein phosphorylation, and thereby modulate cell signaling. Only two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), control the addition or removal of GlcNAc from proteins. This post-translational modification depends on the energy environment of the cell, and in particular on the availability of glucose. Numerous studies have shown that in situations of chronic hyperglycemia, abnormally high levels of O-GlcNAcylation on proteins participate in the complications observed in pathologies such as diabetes and obesity. However, several recent studies using animal models with tissue-specific deletions of OGT indicate that O-GlcNAcylation is essential for the maintenance of energy homeostasis, that it attenuates inflammatory processes and has a protective role against cellular stresses, including endoplasmic reticulum or oxidative stresses." @default.
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• W4220777737 date "2022-06-01" @default.
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• W4220777737 title "O-GlcNAcylation des protéines, homéostasie énergétique et maladies métaboliques" @default.
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