Titre :

Phosphorylation/glycosylation states of MLC2 regulatory protein in skeletal muscle in disuse conditions

Auteur(s) :

Stevens, Laurence [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Pourrier, Marie [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Cochon, Laetitia [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Montel, Valerie [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369
Bastide, Bruno [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369

Titre de la manifestation scientifique :

47th European Muscle Conference

Ville :

Budapest

Pays :

Hongrie

Date de début de la manifestation scientifique :

2019-08-30

Titre de la revue :

Journal of Muscle Research and Cell Motility

Titre du fascicule / de la collection :

47th European Muscle Conference in Budapest, Hungary

Éditeur :

Springer Nature Switzerland

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

Post-translational modifications such as phosphorylation and O-GlcNAcylation are involved in the physiopathology of several acquired diseases, such as muscle insulin resistance or muscle atrophy. In this study, we compared ...
Lire la suite >Post-translational modifications such as phosphorylation and O-GlcNAcylation are involved in the physiopathology of several acquired diseases, such as muscle insulin resistance or muscle atrophy. In this study, we compared the effects of various durations of disuse conditions on Myosin Light Chain 2 (MLC2) post-translational modifications, i.e. after a short-term 3-day dry immersion (DI), midterm (21 days) and long-term (60 days) bed rest (BR), and 15 day-rat hypodynamia-hypokinesia (HH). Muscle phenotype was identified by myosin heavy chain (MHC) isoform expression. In both conditions, there was a shift from slow to fast Myosin Light Chain MLC2 isoform expression. The extent of the transition was identical in BR and DI conditions, and more important after two weeks of HH. In all conditions, MLC2 phosphorylation state was increased while MLC2 glycosylation was decreased. These results suggested an interplay between phosphorylation and O-GlcNAcylation of MLC2, which might be involved in the regulation of associated phenotype changes. The extent of the modulation by phosphorylation/glycosylation process was proportional to the disuse duration. In conclusion, a short period of muscle disuse by DI was sufficient to significantly induce phenotype changes in MLC2 protein and in its post-translational regulation; the more important was the disuse, the more important the regulation. It is suggested that the O-GlcNAcylation level of the phosphoprotein MLC2 is crucial in the modulation of muscle contraction, and should be responsible for changes in muscle contractile properties observed in functional atrophy. This study also contributed to underline that muscle regulatory proteins such as MLC2 are early good molecular biomarkers of skeletal muscle dysfunction conditions.Lire moins >

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

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

Collections :

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

Équipe(s) de recherche :

Activité Physique, Muscle, Santé (APMS)

Date de dépôt :

2024-03-04T16:02:41Z
2024-03-06T12:05:12Z