Hyperglycemia-Induced Aberrant Cell Proliferation; A Metabolic Challenge Mediated by Protein O-GlcNAc Modification
Tóm tắt
Chronic hyperglycemia has been associated with an increased prevalence of pathological conditions including cardiovascular disease, cancer, or various disorders of the immune system. In some cases, these associations may be traced back to a common underlying cause, but more often, hyperglycemia and the disturbance in metabolic balance directly facilitate pathological changes in the regular cellular functions. One such cellular function crucial for every living organism is cell cycle regulation/mitotic activity. Although metabolic challenges have long been recognized to influence cell proliferation, the direct impact of diabetes on cell cycle regulatory elements is a relatively uncharted territory. Among other “nutrient sensing” mechanisms, protein O-linked β-N-acetylglucosamine (O-GlcNAc) modification emerged in recent years as a major contributor to the deleterious effects of hyperglycemia. An increasing amount of evidence suggest that O-GlcNAc may significantly influence the cell cycle and cellular proliferation. In our present review, we summarize the current data available on the direct impact of metabolic changes caused by hyperglycemia in pathological conditions associated with cell cycle disorders. We also review published experimental evidence supporting the hypothesis that O-GlcNAc modification may be one of the missing links between metabolic regulation and cellular proliferation.
Từ khóa
Tài liệu tham khảo
Jacob, 1961, Genetic regulatory mechanisms in the synthesis of proteins, J. Mol. Biol., 3, 318, 10.1016/S0022-2836(61)80072-7
Loomis, 1967, Glucose-lactose diauxie in Escherichia coli, J. Bacteriol., 93, 1397, 10.1128/jb.93.4.1397-1401.1967
Stoebel, 2008, The cost of expression of Escherichia coli lac operon proteins is in the process, not in the products, Genetics, 178, 1653, 10.1534/genetics.107.085399
World Health Organization (2019, July 11). Global Report on Diabetes. Available online: https://www.who.int/diabetes/global-report/en/.
Forouhi, 2014, Epidemiology of diabetes, Medicine (Abingdon), 42, 698
Deshpande, 2008, Epidemiology of diabetes and diabetes-related complications, Phys. Ther., 88, 1254, 10.2522/ptj.20080020
Giovannucci, 2010, Diabetes and cancer: A consensus report, Diabetes Care, 33, 1674, 10.2337/dc10-0666
Duan, 2014, Hyperglycemia, a Neglected Factor during Cancer Progression, Biomed Res. Int., 2014, 1, 10.1155/2014/461917
Varma, 2005, Hyperglycemia alters PI3k and Akt signaling and leads to endothelial cell proliferative dysfunction, Am. J. Physiol. Circ. Physiol., 289, H1744, 10.1152/ajpheart.01088.2004
Brem, 2007, Cellular and molecular basis of wound healing in diabetes, J. Clin. Investig., 117, 1219, 10.1172/JCI32169
Ohkuma, 2018, Sex differences in the association between diabetes and cancer: A systematic review and meta-analysis of 121 cohorts including 20 million individuals and one million events, Diabetologia, 61, 2140, 10.1007/s00125-018-4664-5
Schultz, 2013, Glucose Toxic Effects on Granulation Tissue Productive Cells: The Diabetics’ Impaired Healing, Biomed Res. Int., 2013, 1
Greenhalgh, D.G. (2003). Tissue Repair in Models of Diabetes Mellitus: A Review. Wound Healing, Humana Press.
Linderkamp, 1999, Impaired deformability of erythrocytes and neutrophils in children with newly diagnosed insulin-dependent diabetes mellitus, Diabetologia, 42, 865, 10.1007/s001250051239
Navarro, 2005, Role of inflammation in diabetic complications, Nephrol. Dial. Transplant., 20, 2601, 10.1093/ndt/gfi155
Munhoz, 2007, Neutrophil function and metabolism in individuals with diabetes mellitus, Braz. J. Med. Biol. Res., 40, 1037, 10.1590/S0100-879X2006005000143
Touch, 2017, T Cell Populations and Functions Are Altered in Human Obesity and Type 2 Diabetes, Curr. Diab. Rep., 17, 81, 10.1007/s11892-017-0900-5
Tokarz, 2018, The cell biology of systemic insulin function, J. Cell Biol., 217, 2273, 10.1083/jcb.201802095
(2018). Classification and Diagnosis of Diabetes: Standards of Medical Care in Diabetes—2018. Diabetes Care, 41, S13–S27.
Wilcox, 2016, Life and death of β cells in Type 1 diabetes: A comprehensive review, J. Autoimmun., 71, 51, 10.1016/j.jaut.2016.02.001
Kahn, 2003, The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of Type 2 diabetes, Diabetologia, 46, 3, 10.1007/s00125-002-1009-0
Kandimalla, 2017, Is Alzheimer’s disease a Type 3 Diabetes? A critical appraisal, Biochim. Biophys. Acta. Mol. Basis Dis., 1863, 1078, 10.1016/j.bbadis.2016.08.018
Arnold, 2018, Brain insulin resistance in type 2 diabetes and Alzheimer disease: Concepts and conundrums, Nat. Rev. Neurol., 14, 168, 10.1038/nrneurol.2017.185
Brownlee, 2001, Biochemistry and molecular cell biology of diabetic complications, Nature, 414, 813, 10.1038/414813a
Forbes, 2013, Mechanisms of Diabetic Complications, Physiol. Rev., 93, 137, 10.1152/physrev.00045.2011
Lopez, R., Arumugam, A., Joseph, R., Monga, K., Boopalan, T., Agullo, P., Gutierrez, C., Nandy, S., Subramani, R., and de la Rosa, J.M. (2013). Hyperglycemia Enhances the Proliferation of Non-Tumorigenic and Malignant Mammary Epithelial Cells through Increased leptin/IGF1R Signaling and Activation of AKT/mTOR. PLoS ONE, 8.
Wolf, 2000, Cell cycle regulation in diabetic nephropathy, Kidney Int., 58, S59, 10.1046/j.1523-1755.2000.07710.x
Masson, 2006, Hyperglycemia and glucosamine-induced mesangial cell cycle arrest and hypertrophy: Common or independent mechanisms?, IUBMB Life (Int. Union Biochem. Mol. Biol. Life), 58, 381, 10.1080/15216540600755980
Li, 2018, Hyperglycemia Alters Astrocyte Metabolism and Inhibits Astrocyte Proliferation, Aging Dis., 9, 674, 10.14336/AD.2017.1208
McClelland, 2016, Glucose-Induced Oxidative Stress Reduces Proliferation in Embryonic Stem Cells via FOXO3A/β-Catenin-Dependent Transcription of p21cip1, Stem Cell Reports, 7, 55, 10.1016/j.stemcr.2016.06.006
Weiss, 2001, Hyperglycaemia in vitro alters the proliferation and mitochondrial activity of the choriocarcinoma cell lines BeWo, JAR and JEG-3 as models for human first-trimester trophoblast, Diabetologia, 44, 209, 10.1007/s001250051601
Todeschini, 2018, Hyperglycemia and aberrant O-GlcNAcylation: Contributions to tumor progression, J. Bioenerg. Biomembr., 50, 175, 10.1007/s10863-017-9740-x
Li, 2018, Hyperglycaemia-induced miR-301a promotes cell proliferation by repressing p21 and Smad4 in prostate cancer, Cancer Lett., 418, 211, 10.1016/j.canlet.2018.01.031
Kim, 2019, High Glucose with Insulin Induces Cell Cycle Progression and Activation of Oncogenic Signaling of Bladder Epithelial Cells Cotreated with Metformin and Pioglitazone, J. Diabetes Res., 2019, 2376512, 10.1155/2019/2376512
Fried, 1985, The effects of glucose and amino acids on tumor and host DNA synthesis, J. Surg. Res., 39, 461, 10.1016/0022-4804(85)90101-5
Watanabe, 1989, DNA synthesis, blood flow, and glucose utilization in experimental rat brain tumors, J. Neurosurg., 70, 86, 10.3171/jns.1989.70.1.0086
Jannière, L., Canceill, D., Suski, C., Kanga, S., Dalmais, B., Lestini, R., Monnier, A.F., Chapuis, J., Bolotin, A., and Titok, M. (2007). Genetic Evidence for a Link Between Glycolysis and DNA Replication. PLoS ONE, 2.
Takahashi, 2012, Astroglial Pentose Phosphate Pathway Rates in Response to High-Glucose Environments, ASN Neuro, 4, AN20120002, 10.1042/AN20120002
Romacho, 2016, Inflammation, glucose, and vascular cell damage: The role of the pentose phosphate pathway, Cardiovasc. Diabetol., 15, 82, 10.1186/s12933-016-0397-2
Solovjeva, 2009, Modulation of pentose phosphate pathway during cell cycle progression in human colon adenocarcinoma cell line HT29, Int. J. Cancer, 124, 2789, 10.1002/ijc.24262
Ma, 2017, Polo-like kinase 1 coordinates biosynthesis during cell cycle progression by directly activating pentose phosphate pathway, Nat. Commun., 8, 1506, 10.1038/s41467-017-01647-5
Stincone, 2015, The return of metabolism: Biochemistry and physiology of the pentose phosphate pathway, Biol. Rev., 90, 927, 10.1111/brv.12140
Burns, J., and Manda, G. (2017). Metabolic Pathways of the Warburg Effect in Health and Disease: Perspectives of Choice, Chain or Chance. Int. J. Mol. Sci., 18.
Peres, 2015, Cell cycle progression is regulated by intertwined redox oscillators, Theor. Biol. Med. Model., 12, 10, 10.1186/s12976-015-0005-2
Rietman, 2013, An integrated multidisciplinary model describing initiation of cancer and the Warburg hypothesis, Theor. Biol. Med. Model., 10, 39, 10.1186/1742-4682-10-39
Jones, 2015, Aerobic glycolysis: Beyond proliferation, Front. Immunol., 6, 227, 10.3389/fimmu.2015.00227
Korshunov, 1997, High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria, FEBS Lett., 416, 15, 10.1016/S0014-5793(97)01159-9
Giacco, 2010, Oxidative stress and diabetic complications, Circ. Res., 107, 1058, 10.1161/CIRCRESAHA.110.223545
Du, 2001, Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site, J. Clin. Investig., 108, 1341, 10.1172/JCI11235
Cuezva, 2014, The H+-ATP synthase: A gate to ROS-mediated cell death or cell survival, Biochim. Biophys. Acta Bioenerg., 1837, 1099, 10.1016/j.bbabio.2014.03.010
Szendroedi, J., Schmid, A.I., Chmelik, M., Toth, C., Brehm, A., Krssak, M., Nowotny, P., Wolzt, M., Waldhausl, W., and Roden, M. (2007). Muscle mitochondrial ATP synthesis and glucose transport/phosphorylation in type 2 diabetes. PLoS Med., 4.
Petersen, 2004, Impaired mitochondrial activity in the insulin-resistant offspring of patients with type 2 diabetes, N. Engl. J. Med., 350, 664, 10.1056/NEJMoa031314
Kwak, 2010, Mitochondrial metabolism and diabetes, J. Diabetes Investig., 1, 161, 10.1111/j.2040-1124.2010.00047.x
Rocha, 2016, Effect of Moderate Exercise on Mitochondrial Proteome in Heart Tissue of Spontaneous Hypertensive Rats, Am. J. Hypertens., 29, 696, 10.1093/ajh/hpv160
Farhat, 2015, Effect of exercise training on oxidative stress and mitochondrial function in rat heart and gastrocnemius muscle, Redox Rep., 20, 60, 10.1179/1351000214Y.0000000105
Havens, 2006, Regulation of late G1/S phase transition and APC Cdh1 by reactive oxygen species, Mol. Cell. Biol., 26, 4701, 10.1128/MCB.00303-06
Barni, 1996, Static cytofluorometry and fluorescence morphology of mitochondria and DNA in proliferating fibroblasts, Biotech. Histochem., 71, 66, 10.3109/10520299609117135
Buranasin, P., Mizutani, K., Iwasaki, K., Pawaputanon Na Mahasarakham, C., Kido, D., Takeda, K., and Izumi, Y. (2018). High glucose-induced oxidative stress impairs proliferation and migration of human gingival fibroblasts. PLoS ONE, 13.
Boonstra, 2004, Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells, Gene, 337, 1, 10.1016/j.gene.2004.04.032
Nowotny, 2015, Advanced glycation end products and oxidative stress in type 2 diabetes mellitus, Biomolecules, 5, 194, 10.3390/biom5010194
Black, 2012, Protein kinase C signaling and cell cycle regulation, Front. Immunol., 3, 423
Goldin, 2006, Advanced Glycation End Products, Circulation, 114, 597, 10.1161/CIRCULATIONAHA.106.621854
Wautier, 2001, Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE, Am. J. Physiol. Endocrinol. Metab., 280, E685, 10.1152/ajpendo.2001.280.5.E685
SCHMIDT, 2000, RAGE: A New Target for the Prevention and Treatment of the Vascular and Inflammatory Complications of Diabetes, Trends Endocrinol. Metab., 11, 368, 10.1016/S1043-2760(00)00311-8
Mendoza, 2011, The Ras-ERK and PI3K-mTOR pathways: Cross-talk and compensation, Trends Biochem. Sci., 36, 320, 10.1016/j.tibs.2011.03.006
Schmidt, 2007, Cell cycle related signaling in Neuro2a cells proceeds via the receptor for advanced glycation end products, J. Neural Transm., 114, 1413, 10.1007/s00702-007-0770-0
Xu, 2013, Knockdown of RAGE inhibits growth and invasion of gastric cancer cells, Eur. J. Histochem., 57, e36, 10.4081/ejh.2013.e36
Franke, 2009, Advanced glycation end products induce cell cycle arrest and proinflammatory changes in osteoarthritic fibroblast-like synovial cells, Arthritis Res. Ther., 11, R136, 10.1186/ar2807
Schwab, 2018, Polyol Pathway Links Glucose Metabolism to the Aggressiveness of Cancer Cells, Cancer Res., 78, 1604, 10.1158/0008-5472.CAN-17-2834
Criollo, 2007, Mitochondrial control of cell death induced by hyperosmotic stress, Apoptosis, 12, 3, 10.1007/s10495-006-0328-x
Lu, 2014, Sorbitol induces apoptosis of human colorectal cancer cells via p38 MAPK signal transduction, Oncol. Lett., 7, 1992, 10.3892/ol.2014.1994
Faust, 2012, Differential p38-dependent signalling in response to cellular stress and mitogenic stimulation in fibroblasts, Cell Commun. Signal., 10, 6, 10.1186/1478-811X-10-6
Thornton, 2009, Non-Classical P38 Map Kinase Functions: Cell Cycle Checkpoints and Survival, Int. J. Biol. Sci., 5, 44, 10.7150/ijbs.5.44
Hart, 2007, Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins, Nature, 446, 1017, 10.1038/nature05815
Nagy, 2007, Protein-associated O-GlcNAc, a multifunctional mechanism in cell signaling and its role in the pathogenesis of diabetes, stress and malignant diseases, Biochem. Med., 17, 162, 10.11613/BM.2007.015
Hart, 2011, Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease, Annu. Rev. Biochem., 80, 825, 10.1146/annurev-biochem-060608-102511
Li, 2013, Vaspin attenuates high glucose-induced vascular smooth muscle cells proliferation and chemokinesis by inhibiting the MAPK, PI3K/Akt, and NF-κB signaling pathways, Atherosclerosis, 228, 61, 10.1016/j.atherosclerosis.2013.02.013
Rugonyi, 2013, Hyperglycemia slows embryonic growth and suppresses cell cycle via cyclin D1 and p21, Diabetes, 62, 234, 10.2337/db12-0161
Loughlin, D.T., and Artlett, C.M. (2011). Modification of Collagen by 3-Deoxyglucosone Alters Wound Healing through Differential Regulation of p38 MAP Kinase. PLoS ONE, 6.
Saxton, 2017, mTOR Signaling in Growth, Metabolism, and Disease, Cell, 168, 960, 10.1016/j.cell.2017.02.004
Joven, 2014, Cell cycle regulation by the nutrient-sensing mammalian target of rapamycin (mTOR) pathway, Methods Mol. Biol., 1170, 113, 10.1007/978-1-4939-0888-2_7
Llanos, 2016, Stabilization of p21 by mTORC1/4E-BP1 predicts clinical outcome of head and neck cancers, Nat. Commun., 7, 10438, 10.1038/ncomms10438
Hidalgo, 2000, The rapamycin-sensitive signal transduction pathway as a target for cancer therapy, Oncogene, 19, 6680, 10.1038/sj.onc.1204091
Umezawa, 2017, AMPK: Therapeutic Target for Diabetes and Cancer Prevention, Curr. Pharm. Des., 23, 3629, 10.2174/0929867324666170713150440
Zi, 2018, Metformin and cancer: An existing drug for cancer prevention and therapy, Oncol. Lett., 15, 683
Wang, 2009, Wnt/β-catenin signaling pathway may regulate cell cycle and expression of cyclin A and cyclin E protein in hepatocellular carcinoma cells, Cell Cycle, 8, 1567, 10.4161/cc.8.10.8489
Rowlands, 2004, Beta-catenin and cyclin D1: Connecting development to breast cancer, Cell Cycle, 3, 145, 10.4161/cc.3.2.665
Korswagen, 2006, Regulation of the Wnt/β-catenin pathway by redox signaling, Dev. Cell, 10, 687, 10.1016/j.devcel.2006.05.007
Vallée, A., and Lecarpentier, Y. (2018). Crosstalk Between Peroxisome Proliferator-Activated Receptor Gamma and the Canonical WNT/β-Catenin Pathway in Chronic Inflammation and Oxidative Stress During Carcinogenesis. Front. Immunol., 9.
Liu, 2016, Chronic over-nutrition and dysregulation of GSK3 in diseases, Nutr. Metab. (Lond.), 13, 49, 10.1186/s12986-016-0108-8
Huang, 2018, The PI3K/AKT pathway in obesity and type 2 diabetes, Int. J. Biol. Sci., 14, 1483, 10.7150/ijbs.27173
Hou, 2014, Advanced glycation endproducts trigger autophagy in cadiomyocyte via RAGE/PI3K/AKT/mTOR pathway, Cardiovasc. Diabetol., 13, 78, 10.1186/1475-2840-13-78
Fakhruddin, 2017, Diabetes-Induced Reactive Oxygen Species: Mechanism of Their Generation and Role in Renal Injury, J. Diabetes Res., 2017, 1, 10.1155/2017/8379327
Loh, 2009, Reactive oxygen species enhance insulin sensitivity, Cell Metab., 10, 260, 10.1016/j.cmet.2009.08.009
Sasaguri, 2008, GSK-3beta regulates cyclin D1 expression: A new target for chemotherapy, Cell. Signal., 20, 581, 10.1016/j.cellsig.2007.10.018
Jope, 2007, Glycogen synthase kinase-3 (GSK3): Inflammation, diseases, and therapeutics, Neurochem. Res., 32, 577, 10.1007/s11064-006-9128-5
Walz, 2017, Molecular Pathways: Revisiting Glycogen Synthase Kinase-3β as a Target for the Treatment of Cancer, Clin. Cancer Res., 23, 1891, 10.1158/1078-0432.CCR-15-2240
Saengboonmee, 2016, High glucose enhances progression of cholangiocarcinoma cells via STAT3 activation, Sci. Rep., 6, 18995, 10.1038/srep18995
Masur, 2011, Diabetogenic glucose and insulin concentrations modulate transcriptome and protein levels involved in tumour cell migration, adhesion and proliferation, Br. J. Cancer, 104, 345, 10.1038/sj.bjc.6606050
Onodera, 2014, Increased sugar uptake promotes oncogenesis via EPAC/RAP1 and O-GlcNAc pathways, J. Clin. Investig., 124, 367, 10.1172/JCI63146
Shikata, 2013, Diabetes mellitus and cancer risk: Review of the epidemiological evidence, Cancer Sci., 104, 9, 10.1111/cas.12043
Wang, 2012, Increased risk of hepatocellular carcinoma in patients with diabetes mellitus: A systematic review and meta-analysis of cohort studies, Int. J. Cancer, 130, 1639, 10.1002/ijc.26165
Ben, 2011, The relationship between new-onset diabetes mellitus and pancreatic cancer risk: A case-control study, Eur. J. Cancer, 47, 248, 10.1016/j.ejca.2010.07.010
Ben, 2011, Diabetes mellitus and risk of pancreatic cancer: A meta-analysis of cohort studies, Eur. J. Cancer, 47, 1928, 10.1016/j.ejca.2011.03.003
Larsson, 2007, Diabetes mellitus and risk of breast cancer: A meta-analysis, Int. J. Cancer, 121, 856, 10.1002/ijc.22717
Larsson, 2011, Diabetes mellitus and incidence of kidney cancer: A meta-analysis of cohort studies, Diabetologia, 54, 1013, 10.1007/s00125-011-2051-6
Jiang, 2011, Diabetes mellitus and incidence and mortality of colorectal cancer: A systematic review and meta-analysis of cohort studies, Eur. J. Epidemiol., 26, 863, 10.1007/s10654-011-9617-y
Mitri, 2008, Diabetes and risk of Non-Hodgkin’s lymphoma: A meta-analysis of observational studies, Diabetes Care, 31, 2391, 10.2337/dc08-1034
Zhao, 2016, Diabetes mellitus and prognosis in women with breast cancer: A systematic review and meta-analysis, Medicine (Baltimore), 95, e5602, 10.1097/MD.0000000000005602
Loponte, 2017, Hyperglycemia exacerbates colon cancer malignancy through hexosamine biosynthetic pathway, Oncogenesis, 6, e306, 10.1038/oncsis.2017.2
Lucena, 2016, Epithelial Mesenchymal Transition Induces Aberrant Glycosylation through Hexosamine Biosynthetic Pathway Activation, J. Biol. Chem., 291, 12917, 10.1074/jbc.M116.729236
Aurer, 2007, Aberrant glycosylation of Igg heavy chain in multiple myeloma, Coll. Antropol., 31, 247
Holst, 2013, Investigations on aberrant glycosylation of glycosphingolipids in colorectal cancer tissues using liquid chromatography and matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF-MS), Mol. Cell. Proteomics, 12, 3081, 10.1074/mcp.M113.030387
Vavasseur, 1994, O-glycan biosynthesis in human colorectal adenoma cells during progression to cancer, Eur. J. Biochem., 222, 415, 10.1111/j.1432-1033.1994.tb18880.x
Qiu, 2008, Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot, J. Proteome Res., 7, 1693, 10.1021/pr700706s
Holst, 2015, Glycosylation characteristics of colorectal cancer, Adv. Cancer Res., 126, 203, 10.1016/bs.acr.2014.11.004
Laskar, 2018, Anti-Diabetic Drugs: Cure or Risk Factors for Cancer?, Pathol. Oncol. Res., 24, 745, 10.1007/s12253-018-0402-z
Zhang, 2011, Reduced risk of colorectal cancer with metformin therapy in patients with type 2 diabetes: A meta-analysis, Diabetes Care, 34, 2323, 10.2337/dc11-0512
Algire, 2010, Metformin blocks the stimulative effect of a high-energy diet on colon carcinoma growth in vivo and is associated with reduced expression of fatty acid synthase, Endocr. Relat. Cancer, 17, 351, 10.1677/ERC-09-0252
Buzzai, 2007, Systemic treatment with the antidiabetic drug metformin selectively impairs p53-deficient tumor cell growth, Cancer Res., 67, 6745, 10.1158/0008-5472.CAN-06-4447
Zhou, 2017, The anti-diabetic drug exenatide, a glucagon-like peptide-1 receptor agonist, counteracts hepatocarcinogenesis through cAMP-PKA-EGFR-STAT3 axis, Oncogene, 36, 4135, 10.1038/onc.2017.38
Geerlings, 1999, Immune dysfunction in patients with diabetes mellitus (DM), FEMS Immunol. Med. Microbiol., 26, 259, 10.1111/j.1574-695X.1999.tb01397.x
Moutschen, 1992, Impaired immune responses in diabetes mellitus: Analysis of the factors and mechanisms involved. Relevance to the increased susceptibility of diabetic patients to specific infections, Diabete Metab., 18, 187
Zhou, 2018, Role of Adaptive and Innate Immunity in Type 2 Diabetes Mellitus, J. Diabetes Res., 2018, 1
Nagareddy, 2013, Hyperglycemia promotes myelopoiesis and impairs the resolution of atherosclerosis, Cell Metab., 17, 695, 10.1016/j.cmet.2013.04.001
Tencerová, M., Kračmerová, J., Krauzová, E., Mališová, L., Kováčová, Z., Wedellová, Z., Šiklová, M., Štich, V., and Rossmeislová, L. (2015). Experimental Hyperglycemia Induces an Increase of Monocyte and T-Lymphocyte Content in Adipose Tissue of Healthy Obese Women. PLoS ONE, 10.
Swamy, 2016, Glucose and glutamine fuel protein O-GlcNAcylation to control T cell self-renewal and malignancy, Nat. Immunol., 17, 712, 10.1038/ni.3439
(2019, July 31). Press Release: The Nobel Prize in Physiology or Medicine 2018. Available online: https://www.nobelprize.org/prizes/medicine/2018/press-release/.
Curran, 2010, PD-1 and CTLA-4 combination blockade expands infiltrating T cells and reduces regulatory T and myeloid cells within B16 melanoma tumors, Proc. Natl. Acad. Sci. USA, 107, 4275, 10.1073/pnas.0915174107
Gershkovitz, 2017, Hyperglycemia Impairs Neutrophil Mobilization Leading to Enhanced Metastatic Seeding, Cell Rep., 21, 2384, 10.1016/j.celrep.2017.11.010
Conroy, 2016, V Obesity-associated cancer: An immunological perspective, Proc. Nutr. Soc., 75, 125, 10.1017/S0029665115004176
Tsentidis, 2016, Higher levels of s-RANKL and osteoprotegerin in children and adolescents with type 1 diabetes mellitus may indicate increased osteoclast signaling and predisposition to lower bone mass: A multivariate cross-sectional analysis, Osteoporos. Int., 27, 1631, 10.1007/s00198-015-3422-5
2000, Study of craniofacial morphology and skeletal maturation in juvenile diabetics (Type I), Am. J. Orthod. Dentofac. Orthop., 118, 189, 10.1067/mod.2000.105235
Sterky, 1967, Growth pattern in juvenile diabetes, Acta Paediatr. Scand., 177, 80, 10.1111/j.1651-2227.1967.tb05231.x
Sundararaghavan, 2017, Diabetes and bone health: Latest evidence and clinical implications, Ther. Adv. Musculoskelet. Dis., 9, 67, 10.1177/1759720X16687480
DeShields, 2018, Comparison of osteoporosis in US adults with type 1 and type 2 diabetes mellitus, J. Endocrinol. Investig., 41, 1051, 10.1007/s40618-018-0828-x
Weber, 2015, Type 1 diabetes is associated with an increased risk of fracture across the life span: A population-based cohort study using The Health Improvement Network (THIN), Diabetes Care, 38, 1913, 10.2337/dc15-0783
Rathinavelu, 2018, Molecular Modulation of Osteoblasts and Osteoclasts in Type 2 Diabetes, J. Diabetes Res., 2018, 1, 10.1155/2018/6354787
Siqueira, 2011, FOXO1 modulates osteoblast differentiation, Bone, 48, 1043, 10.1016/j.bone.2011.01.019
Preshaw, 2012, Periodontitis and diabetes: A two-way relationship, Diabetologia, 55, 21, 10.1007/s00125-011-2342-y
1993, Periodontal disease. The sixth complication of diabetes mellitus, Diabetes Care, 16, 329, 10.2337/diacare.16.1.329
Taylor, 1998, Glycemic control and alveolar bone loss progression in type 2 diabetes, Ann. Periodontol., 3, 30, 10.1902/annals.1998.3.1.30
Li, 2010, Periodontal ligament remodeling and alveolar bone resorption during orthodontic tooth movement in rats with diabetes, Diabetes Technol. Ther., 12, 65, 10.1089/dia.2009.0085
Arita, 2016, Effects of diabetes on tooth movement and root resorption after orthodontic force application in rats, Orthod. Craniofac. Res., 19, 83, 10.1111/ocr.12117
Braga, 2011, Effect of diabetes on orthodontic tooth movement in a mouse model, Eur. J. Oral Sci., 119, 7, 10.1111/j.1600-0722.2010.00793.x
Ohgi, 1996, Glucose modulates growth of gingival fibroblasts and periodontal ligament cells: Correlation with expression of basic fibroblast growth factor, J. Periodontal Res., 31, 579, 10.1111/j.1600-0765.1996.tb00523.x
Li, 2016, High glucose improves healing of periodontal wound by inhibiting proliferation and osteogenetic differentiation of human PDL cells, Int. Wound J., 13, 39, 10.1111/iwj.12218
Kato, 2016, High Glucose Concentrations Suppress the Proliferation of Human Periodontal Ligament Stem Cells and Their Differentiation Into Osteoblasts, J. Periodontol., 87, e44, 10.1902/jop.2015.150474
Zhang, R., Liang, Q., Kang, W., and Ge, S. (2019). Metformin facilitates the proliferation, migration and osteogenic differentiation of periodontal ligament stem cells in vitro. Cell Biol. Int.
Alavi, 2014, Diabetic foot ulcers: Part I. Pathophysiology and prevention, J. Am. Acad. Dermatol., 70, e1, 10.1016/j.jaad.2013.07.048
Dinh, 2012, Mechanisms involved in the development and healing of diabetic foot ulceration, Diabetes, 61, 2937, 10.2337/db12-0227
Davis, 2019, Targeting epigenetic mechanisms in diabetic wound healing, Transl. Res., 204, 39, 10.1016/j.trsl.2018.10.001
Yevdokimova, 2003, High glucose-induced alterations of extracellular matrix of human skin fibroblasts are not dependent on TSP-1-TGFbeta1 pathway, J. Diabetes Complicat., 17, 355, 10.1016/S1056-8727(02)00225-8
Hehenberger, 1997, High glucose-induced growth factor resistance in human fibroblasts can be reversed by antioxidants and protein kinase C-inhibitors, Cell Biochem. Funct., 15, 197, 10.1002/(SICI)1099-0844(199709)15:3<197::AID-CBF740>3.0.CO;2-7
Goldstein, 1979, Diabetes mellitus and genetic prediabetes. Decreased replicative capacity of cultured skin fibroblasts, J. Clin. Investig., 63, 358, 10.1172/JCI109311
Luthra, 2002, Effects of basic fibroblast growth factor (FGF-2) on proliferation of human skin fibroblasts in type II diabetes mellitus, Exp. Clin. Endocrinol. Diabetes, 110, 176, 10.1055/s-2002-32149
Rowe, 1977, Abnormalities in proliferation and protein synthesis in skin fibroblast cultures from patients with diabetes mellitus, Diabetes, 26, 284, 10.2337/diab.26.4.284
Lerman, 2003, Cellular dysfunction in the diabetic fibroblast: Impairment in migration, vascular endothelial growth factor production, and response to hypoxia, Am. J. Pathol., 162, 303, 10.1016/S0002-9440(10)63821-7
Pirola, 2010, Epigenetic phenomena linked to diabetic complications, Nat. Rev. Endocrinol., 6, 665, 10.1038/nrendo.2010.188
Saito, 2012, Diabetes alters subsets of endothelial progenitor cells that reside in blood, bone marrow, and spleen, Am. J. Physiol. Cell Physiol., 302, C892, 10.1152/ajpcell.00380.2011
Loomans, 2004, Endothelial progenitor cell dysfunction: A novel concept in the pathogenesis of vascular complications of type 1 diabetes, Diabetes, 53, 195, 10.2337/diabetes.53.1.195
Tamarat, 2004, Impairment in ischemia-induced neovascularization in diabetes: Bone marrow mononuclear cell dysfunction and therapeutic potential of placenta growth factor treatment, Am. J. Pathol., 164, 457, 10.1016/S0002-9440(10)63136-7
Shen, 2010, Advanced glycation endproducts increase EPC apoptosis and decrease nitric oxide release via MAPK pathways, Biomed. Pharmacother., 64, 35, 10.1016/j.biopha.2009.03.002
Hink, 2001, Mechanisms underlying endothelial dysfunction in diabetes mellitus, Circ. Res., 88, E14, 10.1161/01.RES.88.2.e14
Jain, 2011, Effect of hyperglycemia and neuropeptides on interleukin-8 expression and angiogenesis in dermal microvascular endothelial cells, J. Vasc. Surg., 53, 1654, 10.1016/j.jvs.2011.02.019
Levin, 2008, Variability and risk factors for kidney disease progression and death following attainment of stage 4 CKD in a referred cohort, Am. J. Kidney Dis., 52, 661, 10.1053/j.ajkd.2008.06.023
Chang, 2018, The role of IL-20 in chronic kidney disease and diabetic nephropathy: Pathogenic and therapeutic implications, J. Leukoc. Biol., 104, 919, 10.1002/JLB.MR1217-489R
Masson, 2005, Glucosamine induces cell-cycle arrest and hypertrophy of mesangial cells: Implication of gangliosides, Biochem. J., 388, 537, 10.1042/BJ20041506
Yano, 2009, High ambient glucose induces angiotensin-independent AT-1 receptor activation, leading to increases in proliferation and extracellular matrix accumulation in MES-13 mesangial cells, Biochem. J., 423, 129, 10.1042/BJ20082277
Lan, 2013, Andrographolide suppresses high glucose-induced fibronectin expression in mesangial cells via inhibiting the AP-1 pathway, J. Cell. Biochem., 114, 2562, 10.1002/jcb.24601
Wolf, 2001, High glucose-induced hypertrophy of mesangial cells requires p27(Kip1), an inhibitor of cyclin-dependent kinases, Am. J. Pathol., 158, 1091, 10.1016/S0002-9440(10)64056-4
Nahman, 1992, Effects of high glucose on cellular proliferation and fibronectin production by cultured human mesangial cells, Kidney Int., 41, 396, 10.1038/ki.1992.55
Li, 2019, Betaine alleviates high glucose-induced mesangial cell proliferation by inhibiting cell proliferation and extracellular matrix deposition via the AKT/ERK1/2/p38 MAPK pathway, Mol. Med. Rep., 20, 1754
Wolf, 1992, High glucose-induced proliferation in mesangial cells is reversed by autocrine TGF-beta, Kidney Int., 42, 647, 10.1038/ki.1992.330
Zachara, N., Akimoto, Y., and Hart, G.W. (2015). The O-GlcNAc Modification, Cold Spring Harbor Laboratory Press. [3rd ed.].
Marshall, 1991, Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance, J. Biol. Chem., 266, 4706, 10.1016/S0021-9258(19)67706-9
Groves, 2017, Fatty acid synthase inhibits the O-GlcNAcase during oxidative stress, J. Biol. Chem., 292, 6493, 10.1074/jbc.M116.760785
Love, 2010, O-GlcNAc cycling: Emerging roles in development and epigenetics, Semin. Cell Dev. Biol., 21, 646, 10.1016/j.semcdb.2010.05.001
Hawkins, 1997, Role of the glucosamine pathway in fat-induced insulin resistance, J. Clin. Investig., 99, 2173, 10.1172/JCI119390
Weigert, 2003, Palmitate-induced activation of the hexosamine pathway in human myotubes: Increased expression of glutamine:fructose-6-phosphate aminotransferase, Diabetes, 52, 650, 10.2337/diabetes.52.3.650
Robinson, 1993, Pre-exposure to glucosamine induces insulin resistance of glucose transport and glycogen synthesis in isolated rat skeletal muscles. Study of mechanisms in muscle and in rat-1 fibroblasts overexpressing the human insulin receptor, Diabetes, 42, 1333, 10.2337/diab.42.9.1333
McClain, 2002, Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia, Proc. Natl. Acad. Sci. USA, 99, 10695, 10.1073/pnas.152346899
Hebert, 1996, Overexpression of glutamine:fructose-6-phosphate amidotransferase in transgenic mice leads to insulin resistance, J. Clin. Investig., 98, 930, 10.1172/JCI118876
Slawson, 2005, Perturbations in O-linked β-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis, J. Biol. Chem., 280, 32944, 10.1074/jbc.M503396200
Fisi, V., Kátai, E., Orbán, J., Dossena, S., Miseta, A., and Nagy, T. (2018). O-Linked N-Acetylglucosamine Transiently Elevates in HeLa Cells during Mitosis. Molecules, 23.
Delporte, 2014, Cell cycle-dependent O-GlcNAc modification of tobacco histones and their interaction with the tobacco lectin, Plant Physiol. Biochem. PPB, 83, 151, 10.1016/j.plaphy.2014.07.021
Drougat, 2012, Serum-stimulated cell cycle entry promotes ncOGT synthesis required for cyclin D expression, Oncogenesis, 1, e36, 10.1038/oncsis.2012.36
Sakabe, 2010, Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code, Proc. Natl. Acad. Sci. USA, 107, 19915, 10.1073/pnas.1009023107
Forma, 2014, The potential role of O-GlcNAc modification in cancer epigenetics, Cell. Mol. Biol. Lett., 19, 438, 10.2478/s11658-014-0204-6
Qie, 2016, Cyclin D1, cancer progression, and opportunities in cancer treatment, J. Mol. Med. (Berl.), 94, 1313, 10.1007/s00109-016-1475-3
Jiang, 2016, Elevated O-GlcNAcylation promotes gastric cancer cells proliferation by modulating cell cycle related proteins and ERK 1/2 signaling, Oncotarget, 7, 61390, 10.18632/oncotarget.11359
Sayat, 2008, O-GlcNAc-glycosylation of beta-catenin regulates its nuclear localization and transcriptional activity, Exp. Cell Res., 314, 2774, 10.1016/j.yexcr.2008.05.017
Jeon, 2013, Glucosamine-induced reduction of integrin β4 and plectin complex stimulates migration and proliferation in mouse embryonic stem cells, Stem Cells Dev., 22, 2975, 10.1089/scd.2013.0158
Fardini, 2013, O-GlcNAcylation: A New Cancer Hallmark?, Front. Endocrinol. (Lausanne), 4, 99, 10.3389/fendo.2013.00099
Wang, Z., Udeshi, N.D., Slawson, C., Compton, P.D., Sakabe, K., Cheung, W.D., Shabanowitz, J., Hunt, D.F., and Hart, G.W. (2010). Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Sci. Signal., 3.
Sur, 2016, Phosphatases and kinases regulating CDC25 activity in the cell cycle: Clinical implications of CDC25 overexpression and potential treatment strategies, Mol. Cell. Biochem., 416, 33, 10.1007/s11010-016-2693-2
Degenhardt, 2010, Targeting Polo-like kinase in cancer therapy, Clin. Cancer Res., 16, 384, 10.1158/1078-0432.CCR-09-1380
Colicino, 2018, Regulating a key mitotic regulator, polo-like kinase 1 (PLK1), Cytoskeleton (Hoboken), 75, 481, 10.1002/cm.21504
Lanza, 2016, Reduced O-GlcNAcase expression promotes mitotic errors and spindle defects, Cell Cycle, 15, 1363, 10.1080/15384101.2016.1167297
Slawson, 2008, A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin, Mol. Biol. Cell, 19, 4130, 10.1091/mbc.e07-11-1146
Tan, 2013, O-linked N-acetylglucosamine cycling regulates mitotic spindle organization, J. Biol. Chem., 288, 27085, 10.1074/jbc.M113.470187
Magescas, 2017, Spindle pole cohesion requires glycosylation-mediated localization of NuMA, Sci. Rep., 7, 1474, 10.1038/s41598-017-01614-6
Sakabe, 2010, O-GlcNAc transferase regulates mitotic chromatin dynamics, J. Biol. Chem., 285, 34460, 10.1074/jbc.M110.158170
Leturcq, 2018, O-GlcNAc transferase associates with the MCM2-7 complex and its silencing destabilizes MCM-MCM interactions, Cell. Mol. Life Sci., 75, 4321, 10.1007/s00018-018-2874-0
Tian, 2016, O-GlcNAcylation Antagonizes Phosphorylation of CDH1 (CDC20 Homologue 1), J. Biol. Chem., 291, 12136, 10.1074/jbc.M116.717850
Ozcan, 2010, Modulation of transcription factor function by O-GlcNAc modification, Biochim. Biophys. Acta, 1799, 353, 10.1016/j.bbagrm.2010.02.005
Donovan, 2014, O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells, Investig. Ophthalmol. Vis. Sci., 55, 7862, 10.1167/iovs.14-14048
Wells, 2011, The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc, Amino Acids, 40, 877, 10.1007/s00726-010-0709-x
Qiu, 2017, Modification of p27 with O-linked N-acetylglucosamine regulates cell proliferation in hepatocellular carcinoma, Mol. Carcinog., 56, 258, 10.1002/mc.22490
Wang, L., Chen, S., Zhang, Z., Zhang, J., Mao, S., Zheng, J., Xuan, Y., Liu, M., Cai, K., and Zhang, W. (2018). Suppressed OGT expression inhibits cell proliferation while inducing cell apoptosis in bladder cancer. BMC Cancer, 18.
Dias, 2007, O-GlcNAc modification in diabetes and Alzheimer’s disease, Mol. Biosyst., 3, 766, 10.1039/b704905f
Banerjee, 2016, Roles of O-GlcNAc in chronic diseases of aging, Mol. Aspects Med., 51, 1, 10.1016/j.mam.2016.05.005
Hanover, 2018, O-GlcNAc in cancer: An Oncometabolism-fueled vicious cycle, J. Bioenerg. Biomembr., 50, 155, 10.1007/s10863-018-9751-2
Chatham, 2010, Protein O-GlcNAcylation: A critical regulator of the cellular response to stress, Curr. Signal Transduct. Ther., 5, 49, 10.2174/157436210790226492
Hanover, 1999, Elevated O-linked N-acetylglucosamine metabolism in pancreatic beta-cells, Arch. Biochem. Biophys., 362, 38, 10.1006/abbi.1998.1016
Gao, 2003, The transcription factor PDX-1 is post-translationally modified by O-linked N-acetylglucosamine and this modification is correlated with its DNA binding activity and insulin secretion in min6 beta-cells, Arch. Biochem. Biophys., 415, 155, 10.1016/S0003-9861(03)00234-0
Durning, 2016, O-Linked β- N -acetylglucosamine (O-GlcNAc) Acts as a Glucose Sensor to Epigenetically Regulate the Insulin Gene in Pancreatic Beta Cells, J. Biol. Chem., 291, 2107, 10.1074/jbc.M115.693580
Filhoulaud, 2009, The hexosamine biosynthesis pathway is essential for pancreatic beta cell development, J. Biol. Chem., 284, 24583, 10.1074/jbc.M109.025288
Guillemain, 2007, Glucose is necessary for embryonic pancreatic endocrine cell differentiation, J. Biol. Chem., 282, 15228, 10.1074/jbc.M610986200
Vanderford, 2007, Glucose induces MafA expression in pancreatic beta cell lines via the hexosamine biosynthetic pathway, J. Biol. Chem., 282, 1577, 10.1074/jbc.M605064200
Liu, 2000, Glucose stimulates protein modification by O-linked GlcNAc in pancreatic beta cells: Linkage of O-linked GlcNAc to beta cell death, Proc. Natl. Acad. Sci. USA, 97, 2820, 10.1073/pnas.97.6.2820
Zachara, 2004, O-GlcNAc a sensor of cellular state: The role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress, Biochim. Biophys. Acta, 1673, 13, 10.1016/j.bbagen.2004.03.016
Carvalho, 2014, O-GlcNAcylation: The Sweet Side of the Cancer, Front. Oncol., 4, 132
Lynch, 2011, O-GlcNAc transferase: A sweet new cancer target, Cell Cycle, 10, 1712, 10.4161/cc.10.11.15561
Khalaila, 2018, O-GlcNAcylation affects β-catenin and E-cadherin expression, cell motility and tumorigenicity of colorectal cancer, Exp. Cell Res., 364, 42, 10.1016/j.yexcr.2018.01.024
Madan, 2016, Changes in O-Linked N-Acetylglucosamine (O-GlcNAc) Homeostasis Activate the p53 Pathway in Ovarian Cancer Cells, J. Biol. Chem., 291, 18897, 10.1074/jbc.M116.734533
Gu, 2014, O-GlcNAcylation is increased in prostate cancer tissues and enhances malignancy of prostate cancer cells, Mol. Med. Rep., 10, 897, 10.3892/mmr.2014.2269
Li, 2017, O-GlcNAcylation modulates Bmi-1 protein stability and potential oncogenic function in prostate cancer, Oncogene, 36, 6293, 10.1038/onc.2017.223
Ma, 2013, Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-κB activity in pancreatic cancer cells, J. Biol. Chem., 288, 15121, 10.1074/jbc.M113.470047
Shin, 2018, O -GlcNAcylation of the Tumor Suppressor FOXO3 Triggers Aberrant Cancer Cell Growth, Cancer Res., 78, 1214, 10.1158/0008-5472.CAN-17-3512
Sharma, N.S., Gupta, V.K., Dauer, P., Kesh, K., Hadad, R., Giri, B., Chandra, A., Dudeja, V., Slawson, C., and Banerjee, S. (2018). O-GlcNAc modification of oncogenic transcription factor Sox2 promotes protein stability and regulates self-renewal in pancreatic cancer. bioRxiv, 345223.
Kanwal, 2013, O-GlcNAcylation-Inducing Treatments Inhibit Estrogen Receptor α Expression and Confer Resistance to 4-OH-Tamoxifen in Human Breast Cancer-Derived MCF-7 Cells, PLoS ONE, 8, 1, 10.1371/journal.pone.0069150
Mi, 2011, O-GlcNAcylation is a novel regulator of lung and colon cancer malignancy, Biochim. Biophys. Acta, 1812, 514, 10.1016/j.bbadis.2011.01.009
Shi, 2010, Aberrant O-GlcNAcylation characterizes chronic lymphocytic leukemia, Leukemia, 24, 1588, 10.1038/leu.2010.152
Asthana, 2018, Hexosamine Biosynthetic Pathway Inhibition Leads to AML Cell Differentiation and Cell Death, Mol. Cancer Ther., 17, 2226, 10.1158/1535-7163.MCT-18-0426
Ali, 2017, O-GlcNAcylation of NF-κB Promotes Lung Metastasis of Cervical Cancer Cells via Upregulation of CXCR4 Expression, Mol. Cells, 40, 476, 10.14348/molcells.2017.2309
Lima, 2018, O-GlcNAc Modification During Pregnancy: Focus on Placental Environment, Front. Physiol., 9, 1263, 10.3389/fphys.2018.01263
Gao, 2001, Dynamic O-glycosylation of nuclear and cytosolic proteins: Cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain, J. Biol. Chem., 276, 9838, 10.1074/jbc.M010420200
Shafi, 2000, The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny, Proc. Natl. Acad. Sci. USA, 97, 5735, 10.1073/pnas.100471497
Yang, 2012, O-GlcNAcase is essential for embryonic development and maintenance of genomic stability, Aging Cell, 11, 439, 10.1111/j.1474-9726.2012.00801.x
Lefebvre, 2004, Modulation of O-GlcNAc glycosylation during xenopus oocyte maturation, J. Cell. Biochem., 93, 999, 10.1002/jcb.20242
Dehennaut, 2007, O-linked N-acetylglucosaminyltransferase inhibition prevents G2/M transition in Xenopus laevis oocytes, J. Biol. Chem., 282, 12527, 10.1074/jbc.M700444200
Dehennaut, 2008, Microinjection of recombinant O-GlcNAc transferase potentiates Xenopus oocytes M-phase entry, Biochem. Biophys. Res. Commun., 369, 539, 10.1016/j.bbrc.2008.02.063
Zhou, 2019, Disruption of O-GlcNAc homeostasis during mammalian oocyte meiotic maturation impacts fertilization, Mol. Reprod. Dev., 86, 543, 10.1002/mrd.23131
Moley, 1991, Effect of diabetes mellitus on mouse pre-implantation embryo development, J. Reprod. Fertil., 93, 325, 10.1530/jrf.0.0930325
Pantaleon, 2010, Toxic effects of hyperglycemia are mediated by the hexosamine signaling pathway and o-linked glycosylation in early mouse embryos, Biol. Reprod., 82, 751, 10.1095/biolreprod.109.076661
Andres, 2017, Chemical Modulation of Protein O-GlcNAcylation via OGT Inhibition Promotes Human Neural Cell Differentiation, ACS Chem. Biol., 12, 2030, 10.1021/acschembio.7b00232
Shi, 2013, Ten-eleven translocation 1 (Tet1) is regulated by O-linked N-acetylglucosamine transferase (Ogt) for target gene repression in mouse embryonic stem cells, J. Biol. Chem., 288, 20776, 10.1074/jbc.M113.460386
Kim, 2017, Impact of protein O-GlcNAcylation on neural tube malformation in diabetic embryopathy, Sci. Rep., 7, 11107, 10.1038/s41598-017-11655-6
Parween, 2017, Higher O-GlcNAc Levels Are Associated with Defects in Progenitor Proliferation and Premature Neuronal Differentiation during in-Vitro Human Embryonic Cortical Neurogenesis, Front. Cell. Neurosci., 11, 415, 10.3389/fncel.2017.00415
Lynch, 2012, Critical role of O-Linked β-N-acetylglucosamine transferase in prostate cancer invasion, angiogenesis, and metastasis, J. Biol. Chem., 287, 11070, 10.1074/jbc.M111.302547
Zibrova, 2017, GFAT1 phosphorylation by AMPK promotes VEGF-induced angiogenesis, Biochem. J., 474, 983, 10.1042/BCJ20160980
Luo, 2008, Protein modification by O-linked GlcNAc reduces angiogenesis by inhibiting Akt activity in endothelial cells, Arterioscler. Thromb. Vasc. Biol., 28, 651, 10.1161/ATVBAHA.107.159533
Huang, 2017, High-glucose environment induced intracellular O-GlcNAc glycosylation and reduced galectin-7 expression in keratinocytes: Implications on impaired diabetic wound healing, J. Dermatol. Sci., 87, 168, 10.1016/j.jdermsci.2017.04.014
Frykberg, 2015, Challenges in the Treatment of Chronic Wounds, Adv. Wound Care, 4, 560, 10.1089/wound.2015.0635
Runager, 2014, Targeting O-glycosyltransferase (OGT) to promote healing of diabetic skin wounds, J. Biol. Chem., 289, 5462, 10.1074/jbc.M113.513952
Waltenberger, 2000, Vascular endothelial growth factor-A-induced chemotaxis of monocytes is attenuated in patients with diabetes mellitus: A potential predictor for the individual capacity to develop collaterals, Circulation, 102, 185, 10.1161/01.CIR.102.2.185
Baudoin, 2014, O-GlcNAcylation and Inflammation: A Vast Territory to Explore, Front. Endocrinol. (Lausanne), 5, 235
Shukla, 2018, Too sweet to resist: Control of immune cell function by O-GlcNAcylation, Cell. Immunol., 333, 85, 10.1016/j.cellimm.2018.05.010
Machacek, 2019, Elevated O-GlcNAcylation enhances pro-inflammatory Th17 function by altering the intracellular lipid microenvironment, J. Biol. Chem., 294, 8973, 10.1074/jbc.RA119.008373
Wu, 2017, O-GlcNAcylation is required for B cell homeostasis and antibody responses, Nat. Commun., 8, 1854, 10.1038/s41467-017-01677-z
Aguilar, 2017, Profiling of Protein O-GlcNAcylation in Murine CD8+ Effector- and Memory-like T Cells, ACS Chem. Biol., 12, 3031, 10.1021/acschembio.7b00869
Golks, 2008, The O-linked N-acetylglucosamine modification in cellular signalling and the immune system. Protein modifications: Beyond the usual suspects review series, EMBO Rep., 9, 748, 10.1038/embor.2008.129
Springhorn, 2012, Exploring leukocyte O-GlcNAcylation as a novel diagnostic tool for the earlier detection of type 2 diabetes mellitus, J. Clin. Endocrinol. Metab., 97, 4640, 10.1210/jc.2012-2229
Myslicki, 2014, O-GlcNAc modification is associated with insulin sensitivity in the whole blood of healthy young adult males, Diabetol. Metab. Syndr., 6, 96, 10.1186/1758-5996-6-96
Zhang, 2017, Bitterness in sugar: O-GlcNAcylation aggravates pre-B acute lymphocytic leukemia through glycolysis via the PI3K/Akt/c-Myc pathway, Am. J. Cancer Res., 7, 1337
Ballotari, P., Vicentini, M., Manicardi, V., Gallo, M., Chiatamone Ranieri, S., Greci, M., and Rossi, G.P. (2017). Diabetes and risk of cancer incidence: Results from a population-based cohort study in northern Italy. BMC Cancer, 17.
Hsueh, 2001, Control of Vascular Cell Proliferation and Migration by PPAR: A new approach to the macrovascular complications of diabetes, Diabetes Care, 24, 392, 10.2337/diacare.24.2.392
Ferrer, 2014, O-GlcNAcylation regulates cancer metabolism and survival stress signaling via regulation of the HIF-1 pathway, Mol. Cell, 54, 820, 10.1016/j.molcel.2014.04.026
Slawson, 2011, O-GlcNAc signalling: Implications for cancer cell biology, Nat. Rev. Cancer, 11, 678, 10.1038/nrc3114
Liu, 2017, Discovery of a Low Toxicity O-GlcNAc Transferase (OGT) Inhibitor by Structure-based Virtual Screening of Natural Products, Sci. Rep., 7, 12334, 10.1038/s41598-017-12522-0
Liu, 2018, Metabolic Inhibitors of O-GlcNAc Transferase That Act In Vivo Implicate Decreased O-GlcNAc Levels in Leptin-Mediated Nutrient Sensing, Angew. Chem. Int. Ed., 57, 7644, 10.1002/anie.201803254