{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T18:41:00Z","timestamp":1788892860766,"version":"build-2803163510"},"reference-count":73,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T00:00:00Z","timestamp":1782691200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000062","name":"NIDDK, National Institutes of Health, intramural research program grant","doi-asserted-by":"publisher","award":["DK060101-18"],"award-info":[{"award-number":["DK060101-18"]}],"id":[{"id":"10.13039\/100000062","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000062","name":"NIDDK, National Institutes of Health, intramural research program grant","doi-asserted-by":"publisher","award":["ZIA DK031116"],"award-info":[{"award-number":["ZIA DK031116"]}],"id":[{"id":"10.13039\/100000062","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Galectin-3 (Gal-3) is a \u03b2-galactoside-binding lectin implicated in metabolic inflammation, cardiovascular and renal dysfunction, neurodegenerative disorders, and obesity-related pathologies. Although Gal-3 is recognized as a clinically relevant biomarker, the mechanisms controlling its tissue expression and circulating abundance remain poorly defined. O-GlcNAcase (Oga; encoded by Mgea5), the enzyme that removes O-linked \u03b2-N-acetylglucosamine (O-GlcNAc) from proteins, regulates nutrient-sensitive signaling and transcriptional processes that overlap with Gal-3 associated disease pathways. To investigate the relationship between metabolic status and Gal-3 expression, male mice were fed a high-fat diet (HFD) for eight weeks to induce obesity. HFD-fed mice exhibited significant increases in body weight and fasting and fed blood glucose levels compared with lean controls, confirming metabolic dysregulation. ELISA revealed approximately threefold higher serum and plasma Gal-3 concentrations in obese mice, indicating enhanced Gal-3 production in diet-induced obesity. To determine whether Oga regulates Gal-3 expression, Oga wild-type (WT), heterozygous (HET), and knockout (KO) mice were analyzed. Circulating Gal-3 protein levels were significantly reduced in Oga KO mice, with intermediate levels in Oga HET animals. RT-qPCR revealed genotype-dependent modulation of Gal-3 (Lgals3) mRNA expression across multiple tissues, demonstrating tissue-specific regulation by Oga. These findings establish Oga as a critical regulator of Gal-3 expression and systemic abundance. The data reveal a mechanistic link between O-GlcNAc signaling enzyme Oga, and lectin-mediated metabolic inflammation, suggesting that Oga activity influences Gal-3 homeostasis and may affect its interpretation as a biomarker in metabolic disease.<\/jats:p>","DOI":"10.3390\/cells15131181","type":"journal-article","created":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T15:27:37Z","timestamp":1782746857000},"page":"1181","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Perturbing O-GlcNAcase Modulates the Expression and Distribution of Galectin-3"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4271-8171","authenticated-orcid":false,"given":"Mana Mohan","family":"Mukherjee","sequence":"first","affiliation":[{"name":"Cell Biochemistry Section, Laboratory of Cell and Molecular Biology, National Institute of Diabetes Digestive and Kidney Disease (NIDDK), National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Asmita","family":"Pramanik","sequence":"additional","affiliation":[{"name":"Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes Digestive and Kidney Disease (NIDDK), National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcella","family":"Kolodrubetz","sequence":"additional","affiliation":[{"name":"Cell Biochemistry Section, Laboratory of Cell and Molecular Biology, National Institute of Diabetes Digestive and Kidney Disease (NIDDK), National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Devin","family":"Biesbrock","sequence":"additional","affiliation":[{"name":"Cell Biochemistry Section, Laboratory of Cell and Molecular Biology, National Institute of Diabetes Digestive and Kidney Disease (NIDDK), National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8104-1493","authenticated-orcid":false,"given":"Kenneth A.","family":"Jacobson","sequence":"additional","affiliation":[{"name":"Molecular Recognition Section, Laboratory of Bioorganic Chemistry, National Institute of Diabetes Digestive and Kidney Disease (NIDDK), National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3154-9878","authenticated-orcid":false,"given":"John A.","family":"Hanover","sequence":"additional","affiliation":[{"name":"Cell Biochemistry Section, Laboratory of Cell and Molecular Biology, National Institute of Diabetes Digestive and Kidney Disease (NIDDK), National Institutes of Health, Bethesda, MD 20892, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,6,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1038\/nrm.2017.22","article-title":"Protein O-GlcNAcylation: Emerging mechanisms and functions","volume":"18","author":"Yang","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1242\/jcs.053678","article-title":"The intersections between O-GlcNAcylation and phosphorylation: Implications for multiple signaling pathways","volume":"123","author":"Zeidan","year":"2010","journal-title":"J. Cell Sci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1083\/jcb.201501101","article-title":"A little sugar goes a long way: The cell biology of O-GlcNAc","volume":"208","author":"Bond","year":"2015","journal-title":"J. Cell Biol."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Mannino, M.P., and Hart, G.W. (2022). The Beginner\u2019s Guide to O-GlcNAc: From Nutrient Sensitive Pathway Regulation to Its Impact on the Immune System. Front. Immunol., 13.","DOI":"10.3389\/fimmu.2022.828648"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1038\/s41597-021-00810-4","article-title":"The human O-GlcNAcome database and meta-analysis","volume":"8","author":"Berendt","year":"2021","journal-title":"Sci. Data"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1096\/fj.01-0094rev","article-title":"Glycan-dependent signaling: O-linked N-acetylglucosamine","volume":"15","author":"Hanover","year":"2001","journal-title":"FASEB J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"re13","DOI":"10.1126\/stke.3122005re13","article-title":"The Hexosamine Signaling Pathway: Deciphering the \u201cO-GlcNAc Code\u201d","volume":"2005","author":"Love","year":"2005","journal-title":"Sci. STKE"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1152\/physrev.00043.2019","article-title":"Role of O-Linked N-Acetylglucosamine Protein Modification in Cellular (Patho)Physiology","volume":"101","author":"Chatham","year":"2021","journal-title":"Physiol. Rev."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1038\/nature12537","article-title":"Diabetic hyperglycaemia activates CaMKII and arrhythmias by O-linked glycosylation","volume":"502","author":"Erickson","year":"2013","journal-title":"Nature"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"e80","DOI":"10.1161\/CIRCRESAHA.119.316288","article-title":"Hyperglycemia Acutely Increases Cytosolic Reactive Oxygen Species via O-linked GlcNAcylation and CaMKII Activation in Mouse Ventricular Myocytes","volume":"126","author":"Lu","year":"2020","journal-title":"Circ. Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1038\/s41467-017-01654-6","article-title":"O-GlcNAcylation of SIRT1 enhances its deacetylase activity and promotes cytoprotection under stress","volume":"8","author":"Han","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"34440","DOI":"10.1074\/jbc.R114.595439","article-title":"O-GlcNAc and the epigenetic regulation of gene expression","volume":"289","author":"Lewis","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"19915","DOI":"10.1073\/pnas.1009023107","article-title":"Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code","volume":"107","author":"Sakabe","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1016\/j.chembiol.2010.12.001","article-title":"Epigenetics gets sweeter: O-GlcNAc joins the \u201chistone code\u201d","volume":"17","author":"Hanover","year":"2010","journal-title":"Chem. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/j.semcdb.2010.05.001","article-title":"O-GlcNAc cycling: Emerging roles in development and epigenetics","volume":"21","author":"Love","year":"2010","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.bbagen.2009.07.017","article-title":"The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine","volume":"1800","author":"Hanover","year":"2010","journal-title":"Biochim. Et Biophys. Acta (BBA)\u2014Gen. Subj."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Konzman, D., Abramowitz, L.K., Steenackers, A., Mukherjee, M.M., Na, H.J., and Hanover, J.A. (2020). O-GlcNAc: Regulator of Signaling and Epigenetics Linked to X-linked Intellectual Disability. Front. Genet., 11.","DOI":"10.3389\/fgene.2020.605263"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"105677","DOI":"10.1016\/j.jbc.2024.105677","article-title":"Emerging roles of O-GlcNAcylation in protein trafficking and secretion","volume":"300","author":"Zhang","year":"2024","journal-title":"J. Biol. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Mukherjee, M.M., Bond, M.R., Abramowitz, L.K., Biesbrock, D., Woodroofe, C.C., Kim, E.J., Swenson, R.E., and Hanover, J.A. (2023). Tools and tactics to define specificity of metabolic chemical reporters. Front. Mol. Biosci., 10.","DOI":"10.3389\/fmolb.2023.1286690"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1038\/s41589-024-01756-5","article-title":"Selective bioorthogonal probe for N-glycan hybrid structures","volume":"21","author":"Mukherjee","year":"2025","journal-title":"Nat. Chem. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1038\/s42004-025-01685-x","article-title":"A dual fluorescent-Raman bioorthogonal probe for specific biosynthetic labeling of intracellular gangliosides","volume":"8","author":"Mukherjee","year":"2025","journal-title":"Commun. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.tibs.2010.04.005","article-title":"O-GlcNAc signaling: A metabolic link between diabetes and cancer?","volume":"35","author":"Slawson","year":"2010","journal-title":"Trends Biochem. Sci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.pharmthera.2013.11.005","article-title":"O-GlcNAc and the cardiovascular system","volume":"142","author":"Dassanayaka","year":"2014","journal-title":"Pharmacol. Ther."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1038\/nrc3114","article-title":"O-GlcNAc signalling: Implications for cancer cell biology","volume":"11","author":"Slawson","year":"2011","journal-title":"Nat. Rev. Cancer"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1016\/j.molcel.2014.04.026","article-title":"O-GlcNAcylation regulates cancer metabolism and survival stress signaling via regulation of the HIF-1 pathway","volume":"54","author":"Ferrer","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1038\/s41467-017-02795-4","article-title":"AMPK activation counteracts cardiac hypertrophy by reducing O-GlcNAcylation","volume":"9","author":"Gelinas","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1534\/genetics.111.126490","article-title":"O-Linked-N-Acetylglucosamine Cycling and Insulin Signaling Are Required for the Glucose Stress Response in Caenorhabditis elegans","volume":"188","author":"Mondoux","year":"2011","journal-title":"Genetics"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"38684","DOI":"10.1074\/jbc.M110.155192","article-title":"Blocking O-Linked GlcNAc Cycling in Drosophila Insulin-producing Cells Perturbs Glucose-Insulin Homeostasis","volume":"285","author":"Sekine","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_29","first-page":"339","article-title":"You are what you eat: O-: Linked N-acetylglucosamine in disease, development and epigenetics","volume":"18","author":"Hanover","year":"2015","journal-title":"Curr. Opin. Clin. Nutr. Metab. Care"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Mukherjee, M.M., Biesbrock, D., and Hanover, J.A. (2025). Galectin-3: Integrator of Signaling via Hexosamine Flux. Biomolecules, 15.","DOI":"10.20944\/preprints202505.1654.v1"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.sbi.2007.09.002","article-title":"Functions of cell surface galectin-glycoprotein lattices","volume":"17","author":"Rabinovich","year":"2007","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Sciacchitano, S., Lavra, L., Morgante, A., Ulivieri, A., Magi, F., De Francesco, G.P., Bellotti, C., Salehi, L.B., and Ricci, A. (2018). Galectin-3: One Molecule for an Alphabet of Diseases, from A to Z. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19020379"},{"key":"ref_33","first-page":"599","article-title":"Galectin-3 as a novel biomarker for disease diagnosis and a target for therapy (Review)","volume":"41","author":"Dong","year":"2018","journal-title":"Int. J. Mol. Med."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.numecd.2008.06.006","article-title":"Do advanced glycation end products contribute to the development of long-term diabetic complications?","volume":"18","author":"Pugliese","year":"2008","journal-title":"Nutr. Metab. Cardiovasc. Dis."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"S264","DOI":"10.1097\/01.ASN.0000077402.95720.B4","article-title":"Role of Galectin-3 in Diabetic Nephropathy","volume":"14","author":"Iacobini","year":"2003","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"101743","DOI":"10.1016\/j.jbc.2022.101743","article-title":"Nutrient-responsive O-GlcNAcylation dynamically modulates the secretion of glycan-binding protein galectin 3","volume":"298","author":"Mathew","year":"2022","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"6691","DOI":"10.21873\/anticanres.13037","article-title":"Effects of Global O-GlcNAcylation on Galectin Gene-expression Profiles in Human Cancer Cell Lines","volume":"38","author":"Sherazi","year":"2018","journal-title":"Anticancer Res."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"McTague, A., Tazhitdinova, R., and Timoshenko, A.V. (2022). O-GlcNAc-Mediated Regulation of Galectin Expression and Secretion in Human Promyelocytic HL-60 Cells Undergoing Neutrophilic Differentiation. Biomolecules, 12.","DOI":"10.3390\/biom12121763"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Gatie, M.I., Spice, D.M., Garha, A., McTague, A., Ahmer, M., Timoshenko, A.V., and Kelly, G.M. (2022). O-GlcNAcylation and Regulation of Galectin-3 in Extraembryonic Endoderm Differentiation. Biomolecules, 12.","DOI":"10.3390\/biom12050623"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1186\/s12014-021-09317-x","article-title":"O-GlcNAcylation protein disruption by Thiamet G promotes changes on the GBM U87-MG cells secretome molecular signature","volume":"18","author":"Menezes","year":"2021","journal-title":"Clin. Proteom."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"9618092","DOI":"10.1155\/2016\/9618092","article-title":"Role of Galectin-3 in Obesity and Impaired Glucose Homeostasis","volume":"2016","author":"Menini","year":"2016","journal-title":"Oxid. Med. Cell Longev."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1007\/s11154-021-09704-7","article-title":"Emerging roles of Galectin-3 in diabetes and diabetes complications: A snapshot","volume":"23","author":"Li","year":"2022","journal-title":"Rev. Endocr. Metab. Disord."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.1515\/cclm-2014-0187","article-title":"Galectin-3 in diabetic patients","volume":"52","author":"Pugliese","year":"2014","journal-title":"Clin. Chem. Lab. Med."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1093\/glycob\/cwu111","article-title":"Galectin-3: An emerging all-out player in metabolic disorders and their complications","volume":"25","author":"Pugliese","year":"2015","journal-title":"Glycobiology"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1210\/jc.2009-1619","article-title":"Serum galectin-3 is elevated in obesity and negatively correlates with glycosylated hemoglobin in type 2 diabetes","volume":"95","author":"Weigert","year":"2010","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1007\/s40618-014-0222-2","article-title":"Increased levels of galectin-3 were associated with prediabetes and diabetes: New risk factor?","volume":"38","author":"Yilmaz","year":"2015","journal-title":"J. Endocrinol. Investig."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1186\/1758-5996-6-106","article-title":"Low serum galectin-3 concentrations are associated with insulin resistance in patients with type 2 diabetes mellitus","volume":"6","author":"Ohkura","year":"2014","journal-title":"Diabetol. Metab. Syndr."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/j.cell.2016.10.025","article-title":"Hematopoietic-Derived Galectin-3 Causes Cellular and Systemic Insulin Resistance","volume":"167","author":"Li","year":"2016","journal-title":"Cell"},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Jiang, Q., Zhao, Q., Chen, Y., Ma, C., Peng, X., Wu, X., Liu, X., Wang, R., Hou, S., and Kong, L. (2024). Galectin-3 impairs calcium transients and beta-cell function. Nat. Commun., 15.","DOI":"10.1038\/s41467-024-47959-1"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Storman, M., Przyby\u0142kowski, A., and Czupryniak, L. (2025). Cross-Sectional Study of Serum Galectin-3 Levels in Patients with Type 2 Diabetes and Colorectal Polyps. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26167662"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"107632","DOI":"10.1016\/j.celrep.2020.107632","article-title":"Nutrient-Driven O-GlcNAcylation Controls DNA Damage Repair Signaling and Stem\/Progenitor Cell Homeostasis","volume":"31","author":"Na","year":"2020","journal-title":"Cell Rep."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"11952","DOI":"10.1073\/pnas.0601931103","article-title":"Caenorhabditis elegans ortholog of a diabetes susceptibility locus: oga-1 (O-GlcNAcase) knockout impacts O-GlcNAc cycling, metabolism, and dauer","volume":"103","author":"Forsythe","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"10695","DOI":"10.1073\/pnas.152346899","article-title":"Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia","volume":"99","author":"McClain","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"5313","DOI":"10.1073\/pnas.072072399","article-title":"Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes","volume":"99","author":"Vosseller","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Ansari, S.A., and Emerald, B.S. (2019). The Role of Insulin Resistance and Protein O-GlcNAcylation in Neurodegeneration. Front. Neurosci., 13.","DOI":"10.3389\/fnins.2019.00473"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"7097","DOI":"10.1074\/jbc.M114.617779","article-title":"Conditional knock-out reveals a requirement for O-linked N-Acetylglucosaminase (O-GlcNAcase) in metabolic homeostasis","volume":"290","author":"Keembiyehetty","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Ben Ahmed, A., Lemaire, Q., Scache, J., Mariller, C., Lefebvre, T., and Vercoutter-Edouart, A.-S. (2023). O-GlcNAc Dynamics: The Sweet Side of Protein Trafficking Regulation in Mammalian Cells. Cells, 12.","DOI":"10.3390\/cells12101396"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1038\/ncb3066","article-title":"O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation","volume":"16","author":"Guo","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"57186","DOI":"10.18632\/oncotarget.11083","article-title":"O-GlcNAcylation of ATG4B positively regulates autophagy by increasing its hydroxylase activity","volume":"7","author":"Jo","year":"2016","journal-title":"Oncotarget"},{"key":"ref_60","unstructured":"Bond, M.R., St Amand, M.M., Kolodrubetz, M.C., Shiloach, J., and Hanover, J. (2016). O-GlcNAcase Knockout Disrupts Mammalian Cell Autophagy, Oxford Univ Press Inc."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"39649","DOI":"10.1074\/jbc.M608069200","article-title":"Importin-mediated nuclear translocation of galectin-3","volume":"281","author":"Nakahara","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1038\/nsmb833","article-title":"The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha","volume":"11","author":"Jinek","year":"2004","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.ejcb.2015.05.004","article-title":"Recycling of galectin-3 in epithelial cells","volume":"94","author":"Honig","year":"2015","journal-title":"Eur. J. Cell. Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1242\/jcs.110.10.1169","article-title":"Plasma membrane targetting, vesicular budding and release of galectin 3 from the cytoplasm of mammalian cells during secretion","volume":"110","author":"Mehul","year":"1997","journal-title":"J. Cell Sci."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1760","DOI":"10.1161\/ATVBAHA.111.241877","article-title":"Glycation and Insulin Resistance","volume":"32","author":"Song","year":"2012","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"107120","DOI":"10.1016\/j.phrs.2024.107120","article-title":"Functional significance of O-linked N-acetylglucosamine protein modification in regulating autophagy","volume":"202","author":"Zhu","year":"2024","journal-title":"Pharmacol. Res."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Cork, G.K., Thompson, J., and Slawson, C. (2018). Real Talk: The Inter-play Between the mTOR, AMPK, and Hexosamine Biosynthetic Pathways in Cell Signaling. Front. Endocrinol., 9.","DOI":"10.3389\/fendo.2018.00522"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"e183033","DOI":"10.1172\/jci.insight.183033","article-title":"Loss of O-GlcNAcylation modulates mTORC1 and autophagy in \u03b2 cells, driving diabetes 2 progression","volume":"9","author":"Jo","year":"2024","journal-title":"JCI Insight"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1101\/gad.305441.117","article-title":"Calcium-dependent O-GlcNAc signaling drives liver autophagy in adaptation to starvation","volume":"31","author":"Ruan","year":"2017","journal-title":"Genes Dev."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1126\/science.1204592","article-title":"TFEB Links Autophagy to Lysosomal Biogenesis","volume":"332","author":"Settembre","year":"2011","journal-title":"Science"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"4252","DOI":"10.7150\/ijbs.112672","article-title":"Coupling of glucose metabolism with mitophagy via O-GlcNAcylation of PINK1","volume":"21","author":"Xu","year":"2025","journal-title":"Int. J. Biol. Sci."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Fahie, K.M.M., Papanicolaou, K.N., and Zachara, N.E. (2022). Integration of O-GlcNAc into Stress Response Pathways. Cells, 11.","DOI":"10.3390\/cells11213509"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Mueller, T., Ouyang, X., Johnson, M.S., Qian, W.-J., Chatham, J.C., Darley-Usmar, V., and Zhang, J. (2021). New Insights Into the Biology of Protein O-GlcNAcylation: Approaches and Observations. Front. Aging, 1.","DOI":"10.3389\/fragi.2020.620382"}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/15\/13\/1181\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,6]],"date-time":"2026-07-06T08:35:50Z","timestamp":1783326950000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/15\/13\/1181"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,29]]},"references-count":73,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["cells15131181"],"URL":"https:\/\/doi.org\/10.3390\/cells15131181","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,29]]}}}