C. Torres and G. Hart, Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc, J Biol Chem, vol.259, pp.3308-3317, 1984.

N. Zachara and G. Hart, Cell signaling, the essential role of O-GlcNAc!, Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, vol.1761, issue.5-6, pp.599-617, 2006.
DOI : 10.1016/j.bbalip.2006.04.007

G. Hart, M. Housley, and C. Slawson, Cycling of O-linked ??-N-acetylglucosamine on nucleocytoplasmic proteins, Nature, vol.278, issue.7139, pp.1017-1022, 2007.
DOI : 10.1038/nature05815

J. Hanover, M. Krause, and D. Love, The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine, Biochimica et Biophysica Acta (BBA) - General Subjects, vol.1800, issue.2, pp.80-95, 2010.
DOI : 10.1016/j.bbagen.2009.07.017

W. Dias and G. Hart, O-GlcNAc modification in diabetes and Alzheimer's disease, Molecular BioSystems, vol.48, issue.11, pp.766-772, 2007.
DOI : 10.1039/b704905f

T. Lefebvre, V. Dehennaut, C. Guinez, S. Olivier, and L. Drougat, Dysregulation of the nutrient/stress sensor O-GlcNAcylation is involved in the etiology of cardiovascular disorders, type-2 diabetes and Alzheimer's disease, Biochimica et Biophysica Acta (BBA) - General Subjects, vol.1800, issue.2, pp.67-79, 2010.
DOI : 10.1016/j.bbagen.2009.08.008

C. Slawson, R. Copeland, and G. Hart, O-GlcNAc signaling: a metabolic link between diabetes and cancer?, Trends in Biochemical Sciences, vol.35, issue.10, pp.547-555, 2010.
DOI : 10.1016/j.tibs.2010.04.005

N. Zachara, O. Donnell, N. Cheung, W. Mercer, J. Marth et al., Dynamic O-GlcNAc Modification of Nucleocytoplasmic Proteins in Response to Stress: A SURVIVAL RESPONSE OF MAMMALIAN CELLS, Journal of Biological Chemistry, vol.279, issue.29, pp.30133-30142, 2004.
DOI : 10.1074/jbc.M403773200

L. Not, C. Brocks, L. Vamhidy, R. Marchase, and J. Chatham, Increased O-linked ??-N-acetylglucosamine levels on proteins improves survival, reduces inflammation and organ damage 24 hours after trauma-hemorrhage in rats, Critical Care Medicine, vol.38, issue.2, pp.562-571, 2010.
DOI : 10.1097/CCM.0b013e3181cb10b3

L. Zhou, S. Yang, S. Hu, I. Chaudry, R. Marchase et al., THE PROTECTIVE EFFECTS OF PUGNAC ON CARDIAC FUNCTION AFTER TRAUMA-HEMORRHAGE ARE MEDIATED VIA INCREASED PROTEIN O-GlcNAc LEVELS, Shock, vol.27, issue.4, pp.402-408, 2007.
DOI : 10.1097/01.shk.0000245031.31859.29

J. Liu, R. Marchase, and J. Chatham, Glutamine-induced protection of isolated rat heart from ischemia/reperfusion injury is mediated via the hexosamine biosynthesis pathway and increased protein O-GlcNAc levels, Journal of Molecular and Cellular Cardiology, vol.42, issue.1, pp.177-185, 2007.
DOI : 10.1016/j.yjmcc.2006.09.015

V. Champattanachai, R. Marchase, and J. Chatham, Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc, AJP: Cell Physiology, vol.292, issue.1, pp.178-187, 2007.
DOI : 10.1152/ajpcell.00162.2006

V. Champattanachai, R. Marchase, and J. Chatham, Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein O-GlcNAc and increased mitochondrial Bcl-2, AJP: Cell Physiology, vol.294, issue.6, pp.1509-1520, 2008.
DOI : 10.1152/ajpcell.00456.2007

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2800950

C. Slawson, R. Copeland, and G. Hart, O-GlcNAc signaling: a metabolic link between diabetes and cancer?, Trends in Biochemical Sciences, vol.35, issue.10, pp.547-555, 2010.
DOI : 10.1016/j.tibs.2010.04.005

B. Laczy, B. Hill, K. Wang, A. Paterson, and C. White, Protein O-GlcNAcylation: a new signaling paradigm for the cardiovascular system, AJP: Heart and Circulatory Physiology, vol.296, issue.1, 2009.
DOI : 10.1152/ajpheart.01056.2008

P. Huang, S. Ho, K. Wang, B. Roessler, and F. Zhang, Muscle-specific overexpression of NCOATGK, splice variant of O-GlcNAcase, induces skeletal muscle atrophy, AJP: Cell Physiology, vol.300, issue.3, pp.456-465, 2011.
DOI : 10.1152/ajpcell.00124.2010

C. Cieniewski-bernard, Y. Mounier, J. Michalski, and B. Bastide, O-GlcNAc level variations are associated with the development of skeletal muscle atrophy, Journal of Applied Physiology, vol.100, issue.5, pp.1499-1505, 2006.
DOI : 10.1152/japplphysiol.00865.2005

C. Cieniewski-bernard, B. Bastide, T. Lefebvre, J. Lemoine, and Y. Mounier, Identification of O-linked N-Acetylglucosamine Proteins in Rat Skeletal Muscle Using Two-dimensional Gel Electrophoresis and Mass Spectrometry, Molecular & Cellular Proteomics, vol.3, issue.6, pp.577-585, 2004.
DOI : 10.1074/mcp.M400024-MCP200

J. Hedou, C. Cieniewski-bernard, Y. Leroy, J. Michalski, and Y. Mounier, O-Linked N-Acetylglucosaminylation Is Involved in the Ca2+ Activation Properties of Rat Skeletal Muscle, Journal of Biological Chemistry, vol.282, issue.14, pp.10360-10369, 2007.
DOI : 10.1074/jbc.M606787200

URL : https://hal.archives-ouvertes.fr/hal-00250067

G. Ramirez-correa, J. W. Wang, Z. Zhong, Z. Gao, and W. , O-Linked GlcNAc Modification of Cardiac Myofilament Proteins: A Novel Regulator of Myocardial Contractile Function, Circulation Research, vol.103, issue.12, pp.1354-1358, 2008.
DOI : 10.1161/CIRCRESAHA.108.184978

J. Hedou, B. Bastide, A. Page, J. Michalski, and W. Morelle, -N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle, PROTEOMICS, vol.28, issue.8, pp.2139-2148, 2009.
DOI : 10.1002/pmic.200800617

URL : https://hal.archives-ouvertes.fr/hal-00408795

C. Cieniewski-bernard, V. Montel, L. Stevens, and B. Bastide, O-GlcNAcylation, an original modulator of contractile activity in striated muscle, Journal of Muscle Research and Cell Motility, vol.27, issue.4, pp.281-287, 2009.
DOI : 10.1007/s10974-010-9201-1

J. Jin, A. Chen, O. Ogut, and Q. Huang, Conformational modulation of slow skeletal muscle troponin T by an NH(2)-terminal metal-binding extension, 2000.

E. Arias, J. Kim, and G. Cartee, Prolonged Incubation in PUGNAc Results in Increased Protein O-Linked Glycosylation and Insulin Resistance in Rat Skeletal Muscle, Diabetes, vol.53, issue.4, pp.921-930, 2004.
DOI : 10.2337/diabetes.53.4.921

P. Stace, D. Marchington, A. Kerbey, and P. Randle, Long term culture of rat soleus muscle in vitro, FEBS Letters, vol.245, issue.1-2, pp.91-94, 1990.
DOI : 10.1016/0014-5793(90)81058-V

Y. Mounier, X. Holy, and L. Stevens, Compared properties of the contractile system of skinned slow and fast rat muscle fibres, Pfl???gers Archiv European Journal of Physiology, vol.187, issue.2, pp.136-141, 1989.
DOI : 10.1007/BF00370583

A. Fabiato, [31] Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands, Methods Enzymol, vol.157, pp.378-417, 1988.
DOI : 10.1016/0076-6879(88)57093-3

M. Delp and C. Duan, Composition and size of type I, IIA, IID/X, and IIB fibers and citrate synthase activity of rat muscle, J Appl Physiol, vol.80, pp.261-270, 1996.

F. Comer, K. Vosseller, L. Wells, M. Accavitti, and G. Hart, Characterization of a Mouse Monoclonal Antibody Specific for O-Linked N-Acetylglucosamine, Analytical Biochemistry, vol.293, issue.2, pp.169-177, 2001.
DOI : 10.1006/abio.2001.5132

N. Zachara, Detection and Analysis of (O-linked ??-N-Acetylglucosamine)-Modified Proteins, Methods Mol Biol, vol.464, pp.227-254, 2009.
DOI : 10.1007/978-1-60327-461-6_13

C. Snow, A. Senior, and L. Gerace, Monoclonal antibodies identify a group of nuclear pore complex glycoproteins, The Journal of Cell Biology, vol.104, issue.5, pp.1143-1156, 1987.
DOI : 10.1083/jcb.104.5.1143

R. Talmadge and R. Roy, Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms, J Appl Physiol, vol.75, pp.2337-2340, 1993.

B. Bastide, P. Kischel, J. Puterflam, L. Stevens, and D. Pette, Expression and functional implications of troponin T isoforms in soleus muscle fibers of rat after unloading, Pfl??gers Archiv, vol.444, issue.3, pp.345-352, 2002.
DOI : 10.1007/s00424-002-0833-x

P. Kischel, B. Bastide, M. Muller, F. Dubail, and F. Offredi, Expression and functional properties of four slow skeletal troponin T isoforms in rat muscles, AJP: Cell Physiology, vol.289, issue.2, pp.437-443, 2005.
DOI : 10.1152/ajpcell.00365.2004

K. Stubbs, M. Macauley, and D. Vocadlo, A Selective Inhibitor Gal-PUGNAc of Human Lysosomal ??-Hexosaminidases Modulates Levels of the Ganglioside???GM2 in Neuroblastoma Cells, Angewandte Chemie International Edition, vol.14, issue.7, pp.1300-1303, 2009.
DOI : 10.1002/anie.200804583

A. Mehdy, W. Morelle, C. Rosnoblet, D. Legrand, and T. Lefebvre, PUGNAc treatment leads to an unusual accumulation of free oligosaccharides in CHO cells, Journal of Biochemistry, vol.151, issue.4, pp.439-446, 2012.
DOI : 10.1093/jb/mvs012

E. Arias and G. Cartee, Relationship between protein O-linked glycosylation and insulin-stimulated glucose transport in rat skeletal muscle following calorie restriction or exposure to O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate, Acta Physiologica Scandinavica, vol.47, issue.3, pp.281-289, 2005.
DOI : 10.1007/s000180300017

A. Persechini, J. Stull, and R. Cooke, The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers, J Biol Chem, vol.260, pp.7951-7954, 1985.

G. Stephenson and D. Stephenson, Endogenous MLC2 phosphorylation and Ca2+-activated force in mechanically skinned skeletal muscle fibres of the rat, Pfl???gers Archiv European Journal of Physiology, vol.168, issue.1, pp.30-38, 1993.
DOI : 10.1007/BF00375099

H. Sweeney, B. Bowman, and J. Stull, Myosin light chain phosphorylation in vertebrate striated muscle: regulation and function, Am J Physiol, vol.264, pp.1085-1095, 1993.

D. Szczesna, J. Zhao, M. Jones, G. Zhi, and J. Stull, sensitivity of skeletal muscle contraction, Journal of Applied Physiology, vol.92, issue.4, pp.1661-1670, 2002.
DOI : 10.1152/japplphysiol.00858.2001