Title :

O-linked N-acetylglucosaminylation is involved in the Ca2+ activation properties of rat skeletal muscle.

Author(s) :

Hedou, Julie [Auteur]
Université de Lille
Cieniewski-Bernard, Caroline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Leroy, Yves [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Mounier, Yvonne [Auteur]
Université de Lille
Bastide, Bruno [Auteur]
Université de Lille

Journal title :

THE JOURNAL OF BIOLOGICAL CHEMISTRY

Abbreviated title :

J Biol Chem

Volume number :

282

Pages :

10360-9

Publication date :

2007-04-06

ISSN :

0021-9258

English keyword(s) :

Acetylglucosamine
Animals
Calcium
Glycolysis
Glycosylation
Homeostasis
Male
Muscle Contraction
Muscle Fibers
Skeletal
Muscle Proteins
Muscle
Skeletal
Muscular Atrophy
Phosphorylation
Protein Processing
Post-Translational
Rats
Rats
Wistar

HAL domain(s) :

Sciences du Vivant [q-bio]

English abstract : [en]

O-Linked N-acetylglucosaminylation termed O-GlcNAc is a dynamic cytosolic and nuclear glycosylation that is dependent both on glucose flow through the hexosamine biosynthesis pathway and on phosphorylation because of the ...
Show more >O-Linked N-acetylglucosaminylation termed O-GlcNAc is a dynamic cytosolic and nuclear glycosylation that is dependent both on glucose flow through the hexosamine biosynthesis pathway and on phosphorylation because of the existence of a balance between phosphorylation and O-GlcNAc. This glycosylation is a ubiquitous post-translational modification, which probably plays an important role in many aspects of protein functions. We have previously reported that, in skeletal muscle, proteins of the glycolytic pathway, energetic metabolism, and contractile proteins were O-GlcNAc-modified and that O-Glc-NAc variations could control the muscle protein homeostasis and be implicated in the regulation of muscular atrophy. In this paper, we report O-N-acetylglucosaminylation of a number of key contractile proteins (i.e. myosin heavy and light chains and actin), which suggests that this glycosylation could be involved in skeletal muscle contraction. Moreover, our results showed that incubation of skeletal muscle skinned fibers in N-acetyl-d-glucosamine, in a concentration solution known to inhibit O-GlcNAc-dependent interactions, induced a decrease in calcium sensitivity and affinity of muscular fibers, whereas the cooperativity of the thin filament proteins was not modified. Thus, our results suggest that O-GlcNAc is involved in contractile protein interactions and could thereby modulate muscle contraction.Show less >

Language :

Anglais

Audience :

Non spécifiée

Administrative institution(s) :

Université de Lille
Univ. Artois
Univ. Littoral Côte d’Opale

Collections :

• Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369

Research team(s) :

Activité Physique, Muscle, Santé (APMS)

Submission date :

2020-07-20T15:33:11Z
2020-08-18T12:11:21Z