Increased O-GlcNAcylation of NF-κB Enhances Retinal Ganglion Cell Death in Streptozotocin-induced Diabetic Retinopathy

REFERENCES

• Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001;414:813–820
   PubMed Web of Science ®Google Scholar
• Yau JW, Rogers SL, Kawasaki R, Lamoureux EL, Kowalski JW, Bek T, et al. Global prevalence and major risk factors of diabetic retinopathy. Diabetes Care 2012;35:556–564
   PubMed Web of Science ®Google Scholar
• Villarroel M, Ciudin A, Hernández C, Simó R. Neurodegeneration: an early event of diabetic retinopathy. World J Diabetes 2010;1:57–64
   PubMedGoogle Scholar
• Lieth E, Gardner TW, Barber AJ, Antonetti DA. Retinal neurodegeneration: early pathology in diabetes. Clin Exp Ophthalmol 2000;28:3–8
   PubMed Web of Science ®Google Scholar
• Torres CR, Hart GW. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc. J Biol Chem 1984;259:3308–3317
   PubMed Web of Science ®Google Scholar
• Nagel AK, Schilling M, Comte-Walters S, Berkaw MN, Ball LE. Identification of O-linked N-acetylglucosamine (O-GlcNAc)-modified osteoblast proteins by electron transfer dissociation tandem mass spectrometry reveals proteins critical for bone formation. Mol Cell Proteomics 2013;12:945–955
   PubMed Web of Science ®Google Scholar
• Hahne H, Sobotzki N, Nyberg T, Helm D, Borodkin VS, van Aalten DM, et al. Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry. J Proteome Res 2013;12:927–936
   PubMed Web of Science ®Google Scholar
• Zachara NE, Hart GW. 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 2004;1673:13–28
   PubMed Web of Science ®Google Scholar
• Capotosti F, Guernier S, Lammers F, Waridel P, Cai Y, Jin J, et al. O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1. Cell 2011;144:376–388
   PubMed Web of Science ®Google Scholar
• Love DC, Krause MW, Hanover JA. O-GlcNAc cycling: emerging roles in development and epigenetics. Semin Cell Dev Biol 2010;21:646–654
   PubMed Web of Science ®Google Scholar
• Ogawa M, Mizofuchi H, Kobayashi Y, Tsuzuki G, Yamamoto M, Wada S, et al. Terminal differentiation program of skeletal myogenesis is negatively regulated by O-GlcNAc glycosylation. Biochim Biophys Acta 2012;1820:24–32
   PubMed Web of Science ®Google Scholar
• Ogawa M, Sakakibara Y, Kamemura K. Requirement of decreased O-GlcNAc glycosylation of Mef2D for its recruitment to the myogenin promoter. Biochem Biophys Res Commun 2013;433:558–562
   PubMed Web of Science ®Google Scholar
• Yang X, Ongusaha PP, Miles PD, Havstad JC, Zhang F, So WV, et al. Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 2008;451:964–969
   PubMed Web of Science ®Google Scholar
• Hu Y, Belke D, Suarez J, Swanson E, Clark R, Hoshijima M, et al. Adenovirus-mediated overexpression of O-GlcNAcase improves contractile function in the diabetic heart. Circ Res 2005;96:1006–1013
   PubMed Web of Science ®Google Scholar
• Lima VV, Rigsby CS, Hardy DM, Webb RC, Tostes RC. O-GlcNAcylation: a novel post-translational mechanism to alter vascular cellular signaling in health and disease: focus on hypertension. J Am Soc Hypertens 2009;3:374–387
   PubMed Web of Science ®Google Scholar
• McLarty JL, Marsh SA, Chatham JC. Post-translational protein modification by O-linked N-acetyl-glucosamine: its role in mediating the adverse effects of diabetes on the heart. Life Sci 2013;92:621–627
   PubMed Web of Science ®Google Scholar
• Park MJ, Kim DI, Lim SK, Choi JH, Han HJ, Yoon KC, et al. High glucose-induced O-GlcNAcylated carbohydrate response element-binding protein (ChREBP) mediates mesangial cell lipogenesis and fibrosis: the possible role in the development of diabetic nephropathy. J Biol Chem 2014;289:13519–13530
   PubMed Web of Science ®Google Scholar
• Gurel Z, Sieg KM, Shallow KD, Sorenson CM, Sheibani N. Retinal O-linked N-acetylglucosamine protein modifications: implications for postnatal retinal vascularization and the pathogenesis of diabetic retinopathy. Mol Vis 2013;19:1047–1059
   PubMed Web of Science ®Google Scholar
• Semba RD, Huang H, Lutty GA, Van Eyk JE, Hart GW. The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy. Proteom Clin Appl 2014;8:218–231
   PubMed Web of Science ®Google Scholar
• Xu C, Liu G, Liu X, Wang F. O-GlcNAcylation under hypoxic conditions and its effects on the blood-retinal barrier in diabetic retinopathy. Int J Mol Med 2014;33:624–632
   PubMed Web of Science ®Google Scholar
• Kim YH, Kim YS, Kang SS, Cho GJ, Choi WS. Resveratrol inhibits neuronal apoptosis and elevated Ca2+/calmodulin-dependent protein kinase II activity in diabetic mouse retina. Diabetes 2010;59:1825–1835
   PubMed Web of Science ®Google Scholar
• Kim YH, Kim YS, Roh GS, Choi WS, Cho GJ. Resveratrol blocks diabetes-induced early vascular lesions and vascular endothelial growth factor induction in mouse retinas. Acta Ophthalmol 2012;90:e31–e37
   PubMed Web of Science ®Google Scholar
• Kim YH, Kim YS, Kang SS, Noh HS, Kim HJ, Cho GJ, Choi WS. Expression of 14-3-3 zeta and interaction with protein kinase C in the rat retina in early diabetes. Diabetologia 2005;48:1411–1415
   PubMed Web of Science ®Google Scholar
• Kim YH, Kim YS, Noh HS, Kang SS, Cheon EW, Park SK, et al. Changes in rhodopsin kinase and transducin in the rat retina in early-stage diabetes. Exp Eye Res 2005;80:753–760
   PubMed Web of Science ®Google Scholar
• Oshitari T, Hata N, Yamamoto S. Endoplasmic reticulum stress and diabetic retinopathy. Vasc Health Risk Manag 2008;4:115–122
   PubMedGoogle Scholar
• Marshall P, Lemieux C. Cleavage pattern of the homing endonuclease encoded by the fifth intron in the chloroplast large subunit rRNA-encoding gene of Chlamydomonas eugametos. Gene 1991;104:241–245
   PubMed Web of Science ®Google Scholar
• Hart GW, Slawson C, Ramirez-Correa G, Lagerlof O. Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu Rev Biochem 2011;80:825–858
   PubMed Web of Science ®Google Scholar
• Bond MR, Hanover JA. O-GlcNAc cycling: a link between metabolism and chronic disease. Annu Rev Nutr 2013;33:205–229
   PubMed Web of Science ®Google Scholar
• Slawson C, Copeland RJ, Hart GW. O-GlcNAc signaling: a metabolic link between diabetes and cancer? Trends Biochem Sci 2010;35:547–555
   PubMed Web of Science ®Google Scholar
• Ma J, Hart GW. Protein O-GlcNAcylation in diabetes and diabetic complications. Expert Rev Proteomics 2013;10:365–380
   PubMed Web of Science ®Google Scholar
• Dias WB, Hart GW. O-GlcNAc modification in diabetes and Alzheimer's disease. Mol Biosyst 2007;3:766–772
   PubMed Web of Science ®Google Scholar
• Roquemore EP, Chevrier MR, Cotter RJ, Hart GW. Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. Biochemistry 1996;35:3578–3586
   PubMed Web of Science ®Google Scholar
• Gurel Z, Zaro BW, Pratt MR, Sheibani N. Identification of O-GlcNAc modification targets in mouse retinal pericytes: implication of p53 in pathogenesis of diabetic retinopathy. PLoS One 2014;9:e95561
   PubMed Web of Science ®Google Scholar
• Baltimore D. NF-κB is 25. Nat Immunol 2011;12:683–685
   PubMed Web of Science ®Google Scholar
• Leidner J, Palkowitsch L, Marienfeld U, Fischer D, Marienfeld R. Identification of lysine residues critical for the transcriptional activity and polyubiquitination of the NF-kappaB family member RelB. Biochem J 2008;416:117–127
   PubMed Web of Science ®Google Scholar
• Zhao Y, Krishnamurthy B, Mollah Zu, Kay TW, Thomas HE. NF-κB in type 1 diabetes. Inflamm Allergy Drug Targets 2011;10:208–217
   PubMedGoogle Scholar
• Yang WH, Park SY, Nam HW, Kim do H, Kang JG, Kang ES, et al. NFkappaB activation is associated with its O-GlcNAcylation state under hyperglycemic conditions. Proc Natl Acad Sci USA 2008;105:17345–17350
   PubMed Web of Science ®Google Scholar
• Hegazy DM, O'Reilly DA, Yang BM, Hodgkinson AD, Millward BA, Demaine AG. NFkappaB polymorphisms and susceptibility to type 1 diabetes. Genes Immun 2001;2:304–308
   PubMed Web of Science ®Google Scholar
• Bierhaus A, Schiekofer S, Schwaninger M, Andrassy M, Humpert PM, Chen J, et al. Diabetes-associated sustained activation of the transcription factor nuclear factor-kappaB. Diabetes 2001;50:2792–2808
   PubMed Web of Science ®Google Scholar
• Glass CK, Saijo K, Winner B, Marchetto MC, Gage FH. Mechanisms underlying inflammation in neurodegeneration. Cell 2010;19:918–934
   Web of Science ®Google Scholar