{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T21:55:25Z","timestamp":1791237325852,"version":"4.1.0"},"reference-count":28,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2016,2,2]],"date-time":"2016-02-02T00:00:00Z","timestamp":1454371200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Department of Biomedical, Surgical and Dental Sciences, University of Milan, Milan, Italy"},{"name":"Department of Medical Biotechnology and Translational Medicine, University of Milan, Milan, Italy"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[2016,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:sec><jats:label\/><jats:p>Skeletal muscle atrophy is a well\u2010known adverse effect of chronic treatment with glucocorticoids and it also occurs when stress conditions such as sepsis and cachexia increase the release of endogenous glucocorticoids. Although the mechanisms of action of these hormones have been elucidated, the possible molecular mechanisms causing atrophy are not yet fully understood. The involvement of the O\u2010GlcNAcylation process has recently been reported in disuse atrophy. O\u2010GlcNAcylation, a regulatory post\u2010translational modification of nuclear and cytoplasmic proteins consists in the attachment of O\u2010GlcNAc residues on cell proteins and is regulated by two enzymes: O\u2010GlcNAc\u2010transferase (OGT) and O\u2010GlcNAcase (OGA). O\u2010GlcNAcylation plays a crucial role in many cellular processes and it seems to be related to skeletal muscle physiological function. The aim of this study is to investigate the involvement of O\u2010GlcNAcylation in glucocorticoid\u2010induced atrophy by using an \u201cin vitro\u201d model, achieved by treatment of C2C12 with 10\u2009\u03bcM dexamethasone for 48\u2009h. In atrophic condition, we observed that O\u2010GlcNAc levels in cell proteins increased and concomitantly protein phosphorylation on serine and threonine residues decreased. Analysis of OGA expression at mRNA and protein levels showed a reduction in this enzyme in atrophic myotubes, whereas no significant changes of OGT expression were found. Furthermore, inhibition of OGA activity by Thiamet G induced atrophy marker expression. Our current findings suggest that O\u2010GlcNAcylation is involved in dexamethasone\u2010induced atrophy. In particular, we propose that the decrease in OGA content causes an excessive and mostly durable level of O\u2010GlcNAc residues on sarcomeric proteins that might modify their function and stability. J. Cell. Biochem. 117: 1833\u20131842, 2016. \u00a9 2016 Wiley Periodicals, Inc.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jcb.25483","type":"journal-article","created":{"date-parts":[[2016,1,5]],"date-time":"2016-01-05T14:07:05Z","timestamp":1452002825000},"page":"1833-1842","source":"Crossref","is-referenced-by-count":36,"title":["Dexamethasone\u2010Induced Skeletal Muscle Atrophy Increases O\u2010GlcNAcylation in C2C12 Cells"],"prefix":"10.1002","volume":"117","author":[{"given":"Luca","family":"Massaccesi","sequence":"first","affiliation":[{"name":"Department of Biomedical Surgical and Dental Sciences University of Milan Milan Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giancarlo","family":"Goi","sequence":"additional","affiliation":[{"name":"Department of Biomedical Surgical and Dental Sciences University of Milan Milan 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