New insights: A role for O-GlcNAcylation in diabetic complications

References

• Akimoto Y, Kawakami H, Yamamoto K, et al. (2003). Elevated expression of O-GlcNAc-modified proteins and O-GlcNAc transferase in corneas of diabetic Goto-Kakizaki rats. Invest Ophthalmol Vis Sci 44:3802–9
   PubMed Web of Science ®Google Scholar
• Akimoto Y, Miura Y, Toda T, et al. (2011). Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4. Clin Proteomics 8:15
   PubMedGoogle Scholar
• American Diabetes Association. (2013). Economic costs of diabetes in the U.S. in 2012. Diabetes Care 36:1033–46
   PubMed Web of Science ®Google Scholar
• Andrali SS, Qian Q, Ozcan S. (2007). Glucose mediates the translocation of NeuroD1 by O-linked glycosylation. J Biol Chem 282:15589–96
   PubMed Web of Science ®Google Scholar
• Babu DA, Chakrabarti SK, Garmey JC, Mirmira RG. (2008). Pdx1 and BETA2/NeuroD1 participate in a transcriptional complex that mediates short-range DNA looping at the insulin gene. J Biol Chem 283:8164–72
   PubMed Web of Science ®Google Scholar
• Ball LE, Berkaw MN, Buse MG. (2006). Identification of the major site of O-linked beta-N-acetylglucosamine modification in the C terminus of insulin receptor substrate-1. Mol Cell Proteomics 5:313–23
   PubMed Web of Science ®Google Scholar
• Banerjee PS, Ma J, Hart GW. (2015). Diabetes-associated dysregulation of O-GlcNAcylation in rat cardiac mitochondria. Proc Natl Acad Sci USA, 112:6050–5
   PubMed Web of Science ®Google Scholar
• Boute N, Gribouval O, Roselli S, et al. (2000). NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome. Nat Genet 24:349–54
   PubMed Web of Science ®Google Scholar
• Brownlee M. (2001). Biochemistry and molecular cell biology of diabetic complications. Nature 414:813–20
   PubMed Web of Science ®Google Scholar
• Buse MG. (2006). Hexosamines, insulin resistance, and the complications of diabetes: current status. Am J Physiol Endocrinol Metab 290:E1–8
   PubMed Web of Science ®Google Scholar
• Butkinaree C, Park K, Hart GW. (2010). O-linked beta-N-acetylglucosamine (O-GlcNAc): extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim Biophys Acta 1800:96–106
   PubMed Web of Science ®Google Scholar
• Chen YQ, Su M, Walia RR, et al. (1998). Sp1 sites mediate activation of the plasminogen activator inhibitor-1 promoter by glucose in vascular smooth muscle cells. J Biol Chem 273:8225–31
   PubMed Web of Science ®Google Scholar
• Cheung WD, Sakabe K, Housley MP, et al. (2008). O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins. J Biol Chem 283:33935–41
   PubMed Web of Science ®Google Scholar
• Chou CF, Omary MB. (1993). Mitotic arrest-associated enhancement of O-linked glycosylation and phosphorylation of human keratins 8 and 18. J Biol Chem 268:4465–72
   PubMed Web of Science ®Google Scholar
• Chung EJ, Chun JN, Jung SA, et al. (2011). TGF-β-stimulated aberrant expression of class III β-tubulin via the ERK signaling pathway in cultured retinal pigment epithelial cells. Biochem Biophys Res Commun 415:367–72
   PubMed Web of Science ®Google Scholar
• Clark RJ, McDonough PM, Swanson E, et al. (2003). Diabetes and the accompanying hyperglycemia impairs cardiomyocyte calcium cycling through increased nuclear O-GlcNAcylation. J Biol Chem 278:44230–7
   PubMed Web of Science ®Google Scholar
• Cogan DG, Toussaint D, Kuwabara T. (1961). Retinal vascular patterns. IV. Diabetic retinopathy. Arch Ophthalmol 66:366–78
   PubMed Web of Science ®Google Scholar
• Comer FI, Hart GW. (1999). O-GlcNAc and the control of gene expression. Biochim Biophys Acta 1473:161–71
   PubMed Web of Science ®Google Scholar
• Comer FI, Hart GW. (2001). Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. Biochemistry 40:7845–52
   PubMed Web of Science ®Google Scholar
• Cooper ME. (2001). Interaction of metabolic and haemodynamic factors in mediating experimental diabetic nephropathy. Diabetologia 44:1957–72
   PubMed Web of Science ®Google Scholar
• Copeland RJ, Bullen JW, Hart GW. (2008). Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity. Am J Physiol Endocrinol Metab 295:E17–28
   PubMed Web of Science ®Google Scholar
• Dauphinee SM, Ma M, Too CK. (2005). Role of O-linked beta-N-acetylglucosamine modification in the subcellular distribution of alpha4 phosphoprotein and Sp1 in rat lymphoma cells. J Cell Biochem 96:579–88
   PubMed Web of Science ®Google Scholar
• Degrell P, Cseh J, Mohas M, et al. (2009). Evidence of O-linked N-acetylglucosamine in diabetic nephropathy. Life Sci 84:389–93
   PubMed Web of Science ®Google Scholar
• Dentin R, Hedrick S, Xie J, et al. (2008). Hepatic glucose sensing via the CREB coactivator CRTC2. Science 319:1402–5
   PubMed Web of Science ®Google Scholar
• Donovan K, Alekseev O, Qi X, et al. (2014). O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells. Invest Ophthalmol Vis Sci 55:7862–73
   PubMed Web of Science ®Google Scholar
• Donoviel DB, Freed DD, Vogel H, et al. (2001). Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein with homology to NEPHRIN. Mol Cell Biol 21:4829–36
   PubMed Web of Science ®Google Scholar
• Du XL, Edelstein D, Rossetti L, et al. (2000). Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. Proc Natl Acad Sci USA 97:12222–6
   PubMed Web of Science ®Google Scholar
• Farook VS, Bogardus C, Prochazka M. (2002). Analysis of MGEA5 on 10q24.1-q24.3 encoding the beta-O-linked N-acetylglucosaminidase as a candidate gene for type 2 diabetes mellitus in Pima Indians. Mol Genet Metab 77:189–93
   PubMed Web of Science ®Google Scholar
• Forbes JM, Fukami K, Cooper ME. (2007). Diabetic nephropathy: where hemodynamics meets metabolism. Exp Clin Endocrinol Diabetes 115:69–84
   PubMed Web of Science ®Google Scholar
• Forsythe ME, Love DC, Lazarus BD, et al. (2006). Caenorhabditis elegans ortholog of a diabetes susceptibility locus: oga-1 (O-GlcNAcase) knockout impacts O-GlcNAc cycling, metabolism, and dauer. Proc Natl Acad Sci USA 103:11952–7
   PubMed Web of Science ®Google Scholar
• Fulop N, Mason MM, Dutta K, et al. (2007). Impact of Type 2 diabetes and aging on cardiomyocyte function and O-linked N-acetylglucosamine levels in the heart. Am J Physiol Cell Physiol 292:C1370–8
   PubMed Web of Science ®Google Scholar
• Gao Y, Miyazaki J, Hart GW. (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 415:155–63
   PubMed Web of Science ®Google Scholar
• Gao Y, Wells L, Comer FI, et al. (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 276:9838–45
   PubMed Web of Science ®Google Scholar
• Ginsberg HN. (2000). Insulin resistance and cardiovascular disease. J Clin Invest 106:453–8
   PubMed Web of Science ®Google Scholar
• Goldberg H, Whiteside C, Fantus IG. (2011). O-linked β-N-acetylglucosamine supports p38 MAPK activation by high glucose in glomerular mesangial cells. Am J Physiol Endocrinol Metab 301:E713–26
   PubMed Web of Science ®Google Scholar
• Goldberg HJ, Scholey J, Fantus IG. (2000). Glucosamine activates the plasminogen activator inhibitor 1 gene promoter through Sp1 DNA binding sites in glomerular mesangial cells. Diabetes 49:863–71
   PubMed Web of Science ®Google Scholar
• Goldberg HJ, Whiteside CI, Hart GW, Fantus IG. (2006). Posttranslational, reversible O-glycosylation is stimulated by high glucose and mediates plasminogen activator inhibitor-1 gene expression and Sp1 transcriptional activity in glomerular mesangial cells. Endocrinology 147:222–31
   PubMed Web of Science ®Google Scholar
• Gurel Z, Sieg KM, Shallow KD, et al. (2013). Retinal O-linked N-acetylglucosamine protein modifications: implications for postnatal retinal vascularization and the pathogenesis of diabetic retinopathy. Mol Vis 19:1047–59
   PubMed Web of Science ®Google Scholar
• Gurel Z, Zaro BW, Pratt MR, Sheibani N. (2014). Identification of O-GlcNAc modification targets in mouse retinal pericytes: implication of p53 in pathogenesis of diabetic retinopathy. PLoS One 9:e95561
   PubMed Web of Science ®Google Scholar
• Hanover JA, Yu S, Lubas WB, et al. (2003). Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene. Arch Biochem Biophys 409:287–97
   PubMed Web of Science ®Google Scholar
• Hardiville S, Hart GW. (2014). Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation. Cell Metab 20:208–13
   PubMed Web of Science ®Google Scholar
• Harris RD, Steffes MW, Bilous RW, et al. (1991). Global glomerular sclerosis and glomerular arteriolar hyalinosis in insulin dependent diabetes. Kidney Int 40:107–14
   PubMed Web of Science ®Google Scholar
• Hart GW. (2013). Nutrient regulation of immunity: O-GlcNAcylation regulates stimulus-specific NF-κB-dependent transcription. Sci Signal 6:pe26
   PubMed Web of Science ®Google Scholar
• Hart GW, Housley MP, Slawson C. (2007). Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. Nature 446:1017–22
   PubMed Web of Science ®Google Scholar
• Hart GW, Slawson C, Ramirez-Correa G, Lagerlof O. (2011). Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem 80:825–58
   PubMed Web of Science ®Google Scholar
• Hartweck LM, Scott CL, Olszewski NE. (2002). Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. have overlapping functions necessary for gamete and seed development. Genetics 161:1279–91
   PubMed Web of Science ®Google Scholar
• Heilig CW, Concepcion LA, Riser BL, et al. (1995). Overexpression of glucose transporters in rat mesangial cells cultured in a normal glucose milieu mimics the diabetic phenotype. J Clin Invest 96:1802–14
   PubMed Web of Science ®Google Scholar
• Hilgers RH, Xing D, Gong K, et al. (2012). Acute O-GlcNAcylation prevents inflammation-induced vascular dysfunction. Am J Physiol Heart Circ Physiol 303:H513–22
   PubMed Web of Science ®Google Scholar
• Holt GD, Hart GW. (1986). The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc. J Biol Chem 261:8049–57
   PubMed Web of Science ®Google Scholar
• Holt GD, Snow CM, Senior A, et al. (1987). Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J Cell Biol 104:1157–64
   PubMed Web of Science ®Google Scholar
• Housley MP, Rodgers JT, Udeshi ND, et al. (2008). O-GlcNAc regulates FoxO activation in response to glucose. J Biol Chem 283:16283–92
   PubMed Web of Science ®Google Scholar
• Housley MP, Udeshi ND, Rodgers JT, et al. (2009). A PGC-1alpha-O-GlcNAc transferase complex regulates FoxO transcription factor activity in response to glucose. J Biol Chem 284:5148–57
   PubMed Web of Science ®Google Scholar
• Hu Y, Belke D, Suarez J, et al. (2005). Adenovirus-mediated overexpression of O-GlcNAcase improves contractile function in the diabetic heart. Circ Res 96:1006–13
   PubMed Web of Science ®Google Scholar
• Hu Y, Suarez J, Fricovsky E, et al. (2009). Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose. J Biol Chem 284:547–55
   PubMed Web of Science ®Google Scholar
• Iyer SP, Akimoto Y, Hart GW. (2003). Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase. J Biol Chem 278:5399–409
   PubMed Web of Science ®Google Scholar
• Jackson SP, Tjian R. (1988). O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation. Cell 55:125–33
   PubMed Web of Science ®Google Scholar
• Ji S, Kang JG, Park SY, et al. (2011). O-GlcNAcylation of tubulin inhibits its polymerization. Amino Acids 40:809–18
   PubMed Web of Science ®Google Scholar
• Keembiyehetty C, Love DC, Harwood KR, et al. (2015). Conditional knock-out reveals a requirement for O-linked N-Acetylglucosaminase (O-GlcNAcase) in metabolic homeostasis. J Biol Chem 290:7097–113
   PubMed Web of Science ®Google Scholar
• Kestila M, Lenkkeri U, Mannikko M, et al. (1998). Positionally cloned gene for a novel glomerular protein-nephrin-is mutated in congenital nephrotic syndrome. . Mol Cell 1:575–82
   PubMed Web of Science ®Google Scholar
• Konrad RJ, Kudlow JE. (2002). The role of O-linked protein glycosylation in beta-cell dysfunction. Int J Mol Med 10:535–9
   PubMed Web of Science ®Google Scholar
• Kreppel LK, Blomberg MA, Hart GW. (1997). Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J Biol Chem 272:9308–15
   PubMed Web of Science ®Google Scholar
• Kreppel LK, Hart GW. (1999). Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats. J Biol Chem 274:32015–22
   PubMed Web of Science ®Google Scholar
• Lazarus MB, Nam Y, Jiang J, et al. (2011). Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469:564–7
   PubMed Web of Science ®Google Scholar
• Lehman DM, Fu DJ, Freeman AB, et al. (2005). A single nucleotide polymorphism in MGEA5 encoding O-GlcNAc-selective N-acetyl-beta-D glucosaminidase is associated with type 2 diabetes in Mexican Americans. Diabetes 54:1214–21
   PubMed Web of Science ®Google Scholar
• Li JJ, Kwak SJ, Jung DS, et al. (2007). Podocyte biology in diabetic nephropathy. Kidney Int Suppl 106:S36–42
   PubMed Web of Science ®Google Scholar
• Love DC, Kochan J, Cathey RL, et al. (2003). Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase. J Cell Sci 116:647–54
   PubMed Web of Science ®Google Scholar
• Love DC, Krause MW, Hanover JA. (2010). O-GlcNAc cycling: emerging roles in development and epigenetics. Semin Cell Dev Biol 21:646–54
   PubMed Web of Science ®Google Scholar
• Lubas WA, Hanover JA. (2000). Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. J Biol Chem 275:10983–8
   PubMed Web of Science ®Google Scholar
• Luo B, Soesanto Y, McClain DA. (2008). Protein modification by O-linked GlcNAc reduces angiogenesis by inhibiting Akt activity in endothelial cells. Arterioscler Thromb Vasc Biol 28:651–7
   PubMed Web of Science ®Google Scholar
• Macauley MS, Shan X, Yuzwa SA, et al. (2010). Elevation of Global O-GlcNAc in rodents using a selective O-GlcNAcase inhibitor does not cause insulin resistance or perturb glucohomeostasis. Chem Biol 17:949–58
   PubMed Web of Science ®Google Scholar
• Magee GM, Bilous RW, Cardwell CR, et al. (2009). Is hyperfiltration associated with the future risk of developing diabetic nephropathy? A meta-analysis. Diabetologia 52:691–7
   PubMed Web of Science ®Google Scholar
• Makino A, Dai A, Han Y, et al. (2015). O-GlcNAcase overexpression reverses coronary endothelial cell dysfunction in type 1 diabetic mice. Am J Physiol Cell Physiol 309:C593–9
   PubMed Web of Science ®Google Scholar
• Marsh SA, Dell'Italia LJ, Chatham JC. (2008). Activation of the hexosamine biosynthesis pathway and protein O-GlcNAcylation modulate hypertrophic and cell signaling pathways in cardiomyocytes from diabetic mice. Amino Acids 40:819–28
   Web of Science ®Google Scholar
• Masson E, Wiernsperger N, Lagarde M, El Bawab S. (2005). Glucosamine induces cell-cycle arrest and hypertrophy of mesangial cells: implication of gangliosides. Biochem J 388:537–44
   PubMed Web of Science ®Google Scholar
• McClain DA, Lubas WA, Cooksey RC, et al. (2002). Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia. Proc Natl Acad Sci USA 99:10695–9
   PubMed Web of Science ®Google Scholar
• Na J, Sweetwyne MT, Park AS, et al. (2015). Diet-induced podocyte dysfunction in Drosophila and mammals. Cell Rep 12:636–47
   PubMed Web of Science ®Google Scholar
• Ozcan S, Andrali SS, Cantrell JE. (2010). Modulation of transcription factor function by O-GlcNAc modification. Biochim Biophys Acta 1799:353–64
   PubMed Web of Science ®Google Scholar
• Park K, Saudek CD, Hart GW. (2010). Increased expression of beta-N-acetylglucosaminidase in erythrocytes from individuals with pre-diabetes and diabetes. Diabetes 59:1845–50
   PubMed Web of Science ®Google Scholar
• Pathak S, Alonso J, Schimpl M, et al. (2015). The active site of O-GlcNAc transferase imposes constraints on substrate sequence. Nat Struct Mol Biol 22:744–50
   PubMed Web of Science ®Google Scholar
• Ramirez-Correa GA, Jin W, Wang Z, et al. (2008). O-linked GlcNAc modification of cardiac myofilament proteins: a novel regulator of myocardial contractile function. Circ Res 103:1354–8
   PubMed Web of Science ®Google Scholar
• Ramirez-Correa GA, Ma J, Slawson C, et al. (2015). Removal of abnormal myofilament O-GlcNAcylation restores Ca2 + sensitivity in diabetic cardiac muscle. Diabetes 64:3573–87
   PubMed Web of Science ®Google Scholar
• Ranuncolo SM, Ghosh S, Hanover JA, et al. (2012). Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo. J Biol Chem 287:23549–61
   PubMed Web of Science ®Google Scholar
• Remuzzi G, Macia M, Ruggenenti P. (2006). Prevention and treatment of diabetic renal disease in type 2 diabetes: the BENEDICT study. J Am Soc Nephrol 17:S90–7
   PubMedGoogle Scholar
• Roquemore EP, Chevrier MR, Cotter RJ, Hart GW. (1996). Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. Biochemistry 35:3578–86
   PubMed Web of Science ®Google Scholar
• Roquemore EP, Dell A, Morris HR, et al. (1992). Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine. J Biol Chem 267:555–63
   PubMed Web of Science ®Google Scholar
• Semba RD, Huang H, Lutty GA, et al. (2014). The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy. Proteomics Clin Appl 8:218–31
   PubMed Web of Science ®Google Scholar
• Shafi R, Iyer SP, Ellies LG, et al. (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 97:5735–9
   PubMed Web of Science ®Google Scholar
• Shao H, Wu C, Wells A. (2010). Phosphorylation of alpha-actinin 4 upon epidermal growth factor exposure regulates its interaction with actin. J Biol Chem 285:2591–600
   PubMed Web of Science ®Google Scholar
• Shaw AS, Miner JH. (2001). CD2-associated protein and the kidney. Curr Opin Nephrol Hypertens 10:19–22
   PubMed Web of Science ®Google Scholar
• Shih NY, Li J, Karpitskii V, et al. (1999). Congenital nephrotic syndrome in mice lacking CD2-associated protein. Science 286:312–15
   PubMed Web of Science ®Google Scholar
• Slawson C, Hart GW. (2011). O-GlcNAc signalling: implications for cancer cell biology. Nat Rev Cancer 11:678–84
   PubMed Web of Science ®Google Scholar
• Slawson C, Zachara NE, Vosseller K, et al. (2005). Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis. J Biol Chem 280:32944–56
   PubMed Web of Science ®Google Scholar
• Tan EP, Villar MT, E L, et al. (2014). Altering O-linked β-N-acetylglucosamine cycling disrupts mitochondrial function. J Biol Chem 289:14719–30
   PubMed Web of Science ®Google Scholar
• The Diabetes Control and Complications Trial Research Group. (1993). The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus. N Engl J Med 329:977–86
   PubMed Web of Science ®Google Scholar
• Toleman C, Paterson AJ, Whisenhunt TR, Kudlow JE. (2004). Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. J Biol Chem 279:53665–73
   PubMed Web of Science ®Google Scholar
• Torres CR, Hart GW. (1984). Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem 259:3308–17
   PubMed Web of Science ®Google Scholar
• UK Prospective Diabetes Study (UKPDS) Group. (1998). Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33). Lancet 352:837–53
   PubMed Web of Science ®Google Scholar
• Vosseller K, Wells L, Lane MD, Hart GW. (2002). Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes. Proc Natl Acad Sci USA 99:5313–18
   PubMed Web of Science ®Google Scholar
• Walgren JL, Vincent TS, Schey KL, Buse MG. (2003). High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin. Am J Physiol Endocrinol Metab 284:E424–34
   PubMed Web of Science ®Google Scholar
• Wang Z, Park K, Comer F, et al. (2009). Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes. Diabetes 58:309–17
   PubMed Web of Science ®Google Scholar
• Wei M, Gaskill SP, Haffner SM, Stern MP. (1998). Effects of diabetes and level of glycemia on all-cause and cardiovascular mortality. The San Antonio Heart Study. Diabetes Care 21:1167–72
   PubMed Web of Science ®Google Scholar
• Whelan SA, Dias WB, Thiruneelakantapillai L, et al. (2010). Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes. J Biol Chem 285:5204–11
   PubMed Web of Science ®Google Scholar
• Whelan SA, Hart GW. (2006). Identification of O-GlcNAc sites on proteins. Meth Enzymol 415:113–33
   PubMed Web of Science ®Google Scholar
• Wilson PW, D'Agostino RB, Levy D, et al. (1998). Prediction of coronary heart disease using risk factor categories. Circulation 97:1837–47
   PubMed Web of Science ®Google Scholar
• Witmer AN, Vrensen GF, Van Noorden CJ, Schlingemann RO. (2003). Vascular endothelial growth factors and angiogenesis in eye disease. Prog Retin Eye Res 22:1–29
   PubMed Web of Science ®Google Scholar
• Wolf G. (2000). Cell cycle regulation in diabetic nephropathy. Kidney Int Suppl 77:S59–66
   PubMedGoogle Scholar
• Wolf G, Ziyadeh FN. (1999). Molecular mechanisms of diabetic renal hypertrophy. Kidney Int 56:393–405
   PubMed Web of Science ®Google Scholar
• Yang X, Ongusaha PP, Miles PD, et al. (2008). Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 451:964–9
   PubMed Web of Science ®Google Scholar
• Yau JW, Rogers SL, Kawasaki R, et al. (2012). Global prevalence and major risk factors of diabetic retinopathy. Diabetes Care 35:556–64
   PubMed Web of Science ®Google Scholar
• Zeidan Q, Wang Z, De Maio A, Hart GW. (2010). O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins. Mol Biol Cell 21:1922–36
   PubMed Web of Science ®Google Scholar
• Zhang X, Bennett V. (1996). Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier. J Biol Chem 271:31391–8
   PubMed Web of Science ®Google Scholar