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Mercier T, Bouvet M, Dubois-Deruy E, et al. Interplay Between Phosphorylation and O-GlcNAcylation of Sarcomeric Proteins in Ischemic Heart Failure. Front Endocrinol (Lausanne). 2018;9:598doi: 10.3389/fendo.2018.00598.
Mercier, T., Bouvet, M., Dubois-Deruy, E., Dechaumes, A., Beseme, O., Richard, V., Mulder, P., & Pinet, F. (2018). Interplay Between Phosphorylation and O-GlcNAcylation of Sarcomeric Proteins in Ischemic Heart Failure. Frontiers in endocrinology, 9598. https://doi.org/10.3389/fendo.2018.00598
Mercier, Thomas, et al. "Interplay Between Phosphorylation and O-GlcNAcylation of Sarcomeric Proteins in Ischemic Heart Failure." Frontiers in endocrinology vol. 9 (2018): 598. doi: https://doi.org/10.3389/fendo.2018.00598
Mercier T, Bouvet M, Dubois-Deruy E, Dechaumes A, Beseme O, Richard V, Mulder P, Pinet F. Interplay Between Phosphorylation and O-GlcNAcylation of Sarcomeric Proteins in Ischemic Heart Failure. Front Endocrinol (Lausanne). 2018 Oct 05;9:598. doi: 10.3389/fendo.2018.00598. eCollection 2018. PMID: 30344511; PMCID: PMC6182077.
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Front Endocrinol (Lausanne). 2018 Oct 05;9:598. doi: 10.3389/fendo.2018.00598. eCollection 2018.

Interplay Between Phosphorylation and O-GlcNAcylation of Sarcomeric Proteins in Ischemic Heart Failure.

Frontiers in endocrinology

Thomas Mercier, Marion Bouvet, Emilie Dubois-Deruy, Arthur Dechaumes, Olivia Beseme, Vincent Richard, Paul Mulder, Florence Pinet

Affiliations

  1. INSERM U1167 Unité d'Epidémiologie et de Santé Publique, Lille, France.
  2. INSERM UMR1096, Endothélium, Valvulopathies et Insuffisance Cardiaque, Rouen, France.

PMID: 30344511 PMCID: PMC6182077 DOI: 10.3389/fendo.2018.00598

Abstract

Post-translational modifications (PTMs) of sarcomeric proteins could participate to left ventricular (LV) remodeling and contractile dysfunction leading in advanced heart failure (HF) with altered ejection fraction. Using an experimental rat model of HF (ligation of left coronary artery) and phosphoproteomic analysis, we identified an increase of desmin phosphorylation and a decrease of desmin O-N-acetylglucosaminylation (O-GlcNAcylation). We aim to characterize interplay between phosphorylation and O-GlcNAcylation for desmin in primary cultures of cardiomyocyte by specific O-GlcNAcase (OGA) inhibition with thiamet G and silencing O-GlcNAc transferase (OGT) and, in perfused heart perfused with thiamet G in sham- and HF-rats. In each model, we found an efficiency of O-GlcNAcylation modulation characterized by the levels of O-GlcNAcylated proteins and OGT expression (for silencing experiments in cells). In perfused heart, we found an improvement of cardiac function under OGA inhibition. But none of the treatments either in

Keywords: O-GlcNAcylation; desmin; heart failure; interplay; phosphorylation; rat models; systolic

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