메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages

O-Glycosylation regulates ubiquitination and degradation of the anti-inflammatory protein A20 to accelerate atherosclerosis in diabetic ApoE-null mice

Author keywords

[No Author keywords available]

Indexed keywords

A20 PROTEIN; ADVANCED GLYCATION END PRODUCT RECEPTOR; APOLIPOPROTEIN E; GLUCOSAMINE; GLUCOSE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIPOPOLYSACCHARIDE; MESSENGER RNA; PROTEASOME; PROTEIN KINASE C BETA; PROTEIN KINASE C BETA2; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; ADVANCED GLYCOSYLATION END PRODUCT RECEPTOR; ADVANCED GLYCOSYLATION END-PRODUCT RECEPTOR; CYSTEINE PROTEINASE; IMMUNOGLOBULIN RECEPTOR; SIGNAL PEPTIDE; TNFAIP3 PROTEIN, MOUSE; UBIQUITIN;

EID: 78650142697     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0014240     Document Type: Article
Times cited : (69)

References (57)
  • 1
    • 2642524446 scopus 로고    scopus 로고
    • Atherosclerotic Vascular Disease Conference: Writing Group III: Pathophysiology
    • Faxon DP, Fuster V, Libby P, Beckman JA, Hiatt WR, et al. (2004) Atherosclerotic Vascular Disease Conference: Writing Group III: pathophysiology. Circulation 109: 2617-2625.
    • (2004) Circulation , vol.109 , pp. 2617-2625
    • Faxon, D.P.1    Fuster, V.2    Libby, P.3    Beckman, J.A.4    Hiatt, W.R.5
  • 2
    • 29144453326 scopus 로고    scopus 로고
    • Intensive diabetes treatment and cardiovascular disease in patients with type 1 diabetes
    • Nathan DM, Cleary PA, Backlund JY, Genuth SM, Lachin JM, et al. (2005) Intensive diabetes treatment and cardiovascular disease in patients with type 1 diabetes. N Engl J Med 353: 2643-2653.
    • (2005) N Engl J Med , vol.353 , pp. 2643-2653
    • Nathan, D.M.1    Cleary, P.A.2    Backlund, J.Y.3    Genuth, S.M.4    Lachin, J.M.5
  • 3
    • 0027395183 scopus 로고
    • Differential regulation of glucose transport and transporters by glucose in vascular endothelial and smooth muscle cells
    • Kaiser N, Sasson S, Feener EP, Boukobza-Vardi N, Higashi S, et al. (1993) Differential regulation of glucose transport and transporters by glucose in vascular endothelial and smooth muscle cells. Diabetes 42: 80-89.
    • (1993) Diabetes , vol.42 , pp. 80-89
    • Kaiser, N.1    Sasson, S.2    Feener, E.P.3    Boukobza-Vardi, N.4    Higashi, S.5
  • 4
    • 17844369493 scopus 로고    scopus 로고
    • Delayed autoregulation of glucose transport in vascular endothelial cells
    • Alpert E, Gruzman A, Riahi Y, Blejter R, Aharoni P, et al. (2005) Delayed autoregulation of glucose transport in vascular endothelial cells. Diabetologia 48: 752-755.
    • (2005) Diabetologia , vol.48 , pp. 752-755
    • Alpert, E.1    Gruzman, A.2    Riahi, Y.3    Blejter, R.4    Aharoni, P.5
  • 5
    • 0034643340 scopus 로고    scopus 로고
    • Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
    • Nishikawa T, Edelstein D, Du XL, Yamagishi D, Matsumura T, et al. (2000) Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage. Nature 404: 787-790.
    • (2000) Nature , vol.404 , pp. 787-790
    • Nishikawa, T.1    Edelstein, D.2    Du, X.L.3    Yamagishi, D.4    Matsumura, T.5
  • 6
    • 3042736838 scopus 로고    scopus 로고
    • Selective inhibition of protein kinase C b2 prevents acute effects of high glucose on vascular cell adhesion molecule-1 expression in human endothelial cells
    • Kouroedov A, Eto M, Joch H, Volpe M, Luscher TF, et al. (2004) Selective inhibition of protein kinase C b2 prevents acute effects of high glucose on vascular cell adhesion molecule-1 expression in human endothelial cells. Circulation 110: 91-96.
    • (2004) Circulation , vol.110 , pp. 91-96
    • Kouroedov, A.1    Eto, M.2    Joch, H.3    Volpe, M.4    Luscher, T.F.5
  • 7
    • 0347381138 scopus 로고    scopus 로고
    • Glycation, inflammation, and RAGE: A scaffold for the macrovascular complications of diabetes and beyond
    • Yan SF, Ramasamy R, Naka Y, Schmidt AM (2003) Glycation, inflammation, and RAGE: a scaffold for the macrovascular complications of diabetes and beyond. Circ Res 93: 1159-1169.
    • (2003) Circ Res , vol.93 , pp. 1159-1169
    • Yan, S.F.1    Ramasamy, R.2    Naka, Y.3    Schmidt, A.M.4
  • 8
    • 20044376702 scopus 로고    scopus 로고
    • The pathobiology of diabetic complications: A unifying mechanism
    • Brownlee M (2005) The pathobiology of diabetic complications: a unifying mechanism. Diabetes 54: 1615-1625.
    • (2005) Diabetes , vol.54 , pp. 1615-1625
    • Brownlee, M.1
  • 9
    • 0024280897 scopus 로고
    • O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation
    • Jackson SP, Tjian R (1988) O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation. Cell 55: 125-133.
    • (1988) Cell , vol.55 , pp. 125-133
    • Jackson, S.P.1    Tjian, R.2
  • 10
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • Wells L, Vosseller K, Hart GW (2001) Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 291: 2376-2378.
    • (2001) Science , vol.291 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 11
    • 3042613480 scopus 로고    scopus 로고
    • O-GlcNAc a sensor of cellular state: The role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress
    • Zachara NE, Hart GW (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: 13-28.
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 13-28
    • Zachara, N.E.1    Hart, G.W.2
  • 12
    • 0037117511 scopus 로고    scopus 로고
    • Elevated nucleocytoplasmic glycosylation by O-GlcNAc results in insulin resistance associated with defects in Akt activation in 3T3-L1 adipocytes
    • 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 U S A 99: 5313- 5318.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 5313-5318
    • Vosseller, K.1    Wells, L.2    Lane, M.D.3    Hart, G.W.4
  • 13
    • 0035180299 scopus 로고    scopus 로고
    • Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site
    • Du XL, Edelstein D, Dimmeler S, Ju Q, Sui C, et al. (2001) Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site. J Clin Invest 108: 1341-1348.
    • (2001) J Clin Invest , vol.108 , pp. 1341-1348
    • Du, X.L.1    Edelstein, D.2    Dimmeler, S.3    Ju, Q.4    Sui, C.5
  • 14
    • 0037162342 scopus 로고    scopus 로고
    • Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells
    • Federici M, Menghini R, Mauriello A, Hribal ML, Ferrelli F, et al. (2002) Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells. Circulation 106: 466-472.
    • (2002) Circulation , vol.106 , pp. 466-472
    • Federici, M.1    Menghini, R.2    Mauriello, A.3    Hribal, M.L.4    Ferrelli, F.5
  • 15
    • 34247116517 scopus 로고    scopus 로고
    • Glycosylation Mediates Up-regulation of a Potent Antiangiogenic and Proatherogenic Protein, Thrombospondin-1, by Glucose in Vascular Smooth Muscle Cells
    • Raman P, Krukovets I, Marinic TE, Bornstein P, Stenina OI (2007) Glycosylation Mediates Up-regulation of a Potent Antiangiogenic and Proatherogenic Protein, Thrombospondin-1, by Glucose in Vascular Smooth Muscle Cells. J Biol Chem 282: 5704-5714.
    • (2007) J Biol Chem , vol.282 , pp. 5704-5714
    • Raman, P.1    Krukovets, I.2    Marinic, T.E.3    Bornstein, P.4    Stenina, O.I.5
  • 16
    • 0345060875 scopus 로고    scopus 로고
    • A20, a regulator of NFkB, maps to an atherosclerosis locus and differs between parental sensitive C57BL/6J and resistant FVB/N strains
    • Idel S, Dansky HM, Breslow JL (2003) A20, a regulator of NFkB, maps to an atherosclerosis locus and differs between parental sensitive C57BL/6J and resistant FVB/N strains. Proc Natl Acad Sci U S A 100: 14235-14240.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14235-14240
    • Idel, S.1    Dansky, H.M.2    Breslow, J.L.3
  • 17
    • 36749057932 scopus 로고    scopus 로고
    • The protective effect of A20 on atherosclerosis in apolipoprotein E-deficient mice is associated with reduced expression of NF-kappaB target genes
    • Wolfrum S, Teupser D, Tan M, Chen KY, Breslow JL (2007) The protective effect of A20 on atherosclerosis in apolipoprotein E-deficient mice is associated with reduced expression of NF-kappaB target genes. Proc Natl Acad Sci U S A 104: 18601-18606.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 18601-18606
    • Wolfrum, S.1    Teupser, D.2    Tan, M.3    Chen, K.Y.4    Breslow, J.L.5
  • 18
    • 33746578116 scopus 로고    scopus 로고
    • A20, a modulator of smooth muscle cell proliferation and apoptosis, prevents and induces regression of neointimal hyperplasia
    • Patel VI, Daniel S, Longo CR, Shrikhande GV, Scali ST, et al. (2006) A20, a modulator of smooth muscle cell proliferation and apoptosis, prevents and induces regression of neointimal hyperplasia. Faseb J 20: 1418-1430.
    • (2006) Faseb J , vol.20 , pp. 1418-1430
    • Patel, V.I.1    Daniel, S.2    Longo, C.R.3    Shrikhande, G.V.4    Scali, S.T.5
  • 19
    • 0029929722 scopus 로고    scopus 로고
    • A20 blocks endothelial cell activation through a NF-kB-dependent mechanism
    • Cooper JT, Stroka DM, Brostjan C, Palmetshofer A, Bach FH, et al. (1996) A20 blocks endothelial cell activation through a NF-kB-dependent mechanism. J Biol Chem 271: 18068-18073.
    • (1996) J Biol Chem , vol.271 , pp. 18068-18073
    • Cooper, J.T.1    Stroka, D.M.2    Brostjan, C.3    Palmetshofer, A.4    Bach, F.H.5
  • 20
    • 0042818084 scopus 로고    scopus 로고
    • A20 protects from CD40-CD40 ligand-mediated endothelial cell activation and apoptosis
    • Longo CR, Arvelo MB, Patel VI, Daniel S, Mahiou J, et al. (2003) A20 protects from CD40-CD40 ligand-mediated endothelial cell activation and apoptosis. Circulation 108: 1113-1118.
    • (2003) Circulation , vol.108 , pp. 1113-1118
    • Longo, C.R.1    Arvelo, M.B.2    Patel, V.I.3    Daniel, S.4    Mahiou, J.5
  • 21
    • 4944266955 scopus 로고    scopus 로고
    • A20 protects endothelial cells from TNF-, Fas-, and NK-mediated cell death by inhibiting caspase 8 activation
    • Daniel S, Arvelo MB, Patel VI, Longo CR, Shrikhande G, et al. (2004) A20 protects endothelial cells from TNF-, Fas-, and NK-mediated cell death by inhibiting caspase 8 activation. Blood 104: 2376-2384.
    • (2004) Blood , vol.104 , pp. 2376-2384
    • Daniel, S.1    Arvelo, M.B.2    Patel, V.I.3    Longo, C.R.4    Shrikhande, G.5
  • 22
    • 3943054838 scopus 로고    scopus 로고
    • Deubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling
    • Wertz IE, O'Rourke KM, Zhou H, Eby M, Aravind L, et al. (2004) Deubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. Nature 430: 694-699.
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhou, H.3    Eby, M.4    Aravind, L.5
  • 23
    • 77649225756 scopus 로고    scopus 로고
    • Inhibition of NF-{kappa}B Signaling by A20 Through Disruption of Ubiquitin Enzyme Complexes
    • Shembade N, Ma A, Harhaj EW (2010) Inhibition of NF-{kappa}B Signaling by A20 Through Disruption of Ubiquitin Enzyme Complexes. Science 327: 1135-1139.
    • (2010) Science , vol.327 , pp. 1135-1139
    • Shembade, N.1    Ma, A.2    Harhaj, E.W.3
  • 24
    • 61949220270 scopus 로고    scopus 로고
    • The ubiquitinediting enzyme A20 requires RNF11 to downregulate NF-kappaB signalling
    • Shembade N, Parvatiyar K, Harhaj NS, Harhaj EW (2009) The ubiquitinediting enzyme A20 requires RNF11 to downregulate NF-kappaB signalling. Embo J 28: 513-522.
    • (2009) Embo J , vol.28 , pp. 513-522
    • Shembade, N.1    Parvatiyar, K.2    Harhaj, N.S.3    Harhaj, E.W.4
  • 25
    • 0025179989 scopus 로고
    • The A20 cDNA induced by tumor necrosis factor alpha encodes a novel type of zinc finger protein
    • Opipari AJ, Boguski MS, Dixit VM (1990) The A20 cDNA induced by tumor necrosis factor alpha encodes a novel type of zinc finger protein. J Biol Chem 265: 14705-14708.
    • (1990) J Biol Chem , vol.265 , pp. 14705-14708
    • Opipari, A.J.1    Boguski, M.S.2    Dixit, V.M.3
  • 26
    • 84934442545 scopus 로고    scopus 로고
    • Characterization of site-specific N-glycosylation
    • Medzihradszky KF (2008) Characterization of site-specific N-glycosylation. Methods Mol Biol 446: 293-316.
    • (2008) Methods Mol Biol , vol.446 , pp. 293-316
    • Medzihradszky, K.F.1
  • 27
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosylation across the human proteome and the correlation to protein function
    • Gupta R, Brunak S (2002) Prediction of glycosylation across the human proteome and the correlation to protein function. Pacific Symposium on Biocomputing 7: 310-322.
    • (2002) Pacific Symposium on Biocomputing , vol.7 , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 28
    • 0018980970 scopus 로고
    • Sugarlectin interactions: How does wheat-germ agglutinin bind sialoglycoconjugates?
    • Monsigny M, Roche AC, Sene C, Maget-Dana R, Delmotte F (1980) Sugarlectin interactions: how does wheat-germ agglutinin bind sialoglycoconjugates? Eur J Biochem 104: 147-153.
    • (1980) Eur J Biochem , vol.104 , pp. 147-153
    • Monsigny, M.1    Roche, A.C.2    Sene, C.3    Maget-Dana, R.4    Delmotte, F.5
  • 29
    • 4644303568 scopus 로고    scopus 로고
    • Nucleocytoplasmic glycosylation, O-GlcNAc: Identification and site mapping
    • Zachara NE, Cheung WD, Hart GW (2004) Nucleocytoplasmic glycosylation, O-GlcNAc: identification and site mapping. Methods Mol Biol 284: 175-194.
    • (2004) Methods Mol Biol , vol.284 , pp. 175-194
    • Zachara, N.E.1    Cheung, W.D.2    Hart, G.W.3
  • 30
    • 35648958721 scopus 로고    scopus 로고
    • IKK{beta} phosphorylates the K63 deubiquitinase A20 to cause feedback inhibition of the NF{kappa}B pathway
    • Hutti JE, Turk BE, Asara JM, Ma A, Cantley LC, et al. (2007) IKK{beta} phosphorylates the K63 deubiquitinase A20 to cause feedback inhibition of the NF{kappa}B pathway. Mol Cell Biol.
    • (2007) Mol Cell Biol
    • Hutti, J.E.1    Turk, B.E.2    Asara, J.M.3    Ma, A.4    Cantley, L.C.5
  • 31
    • 0041315638 scopus 로고    scopus 로고
    • The receptor RAGE as a progression factor amplifying arachidonate-dependent inflammatory and proteolytic response in human atherosclerotic plaques: Role of glycemic control
    • Cipollone F, Iezzi A, Fazia M, Zucchelli M, Pini B, et al. (2003) The receptor RAGE as a progression factor amplifying arachidonate-dependent inflammatory and proteolytic response in human atherosclerotic plaques: role of glycemic control. Circulation 108: 1070-1077.
    • (2003) Circulation , vol.108 , pp. 1070-1077
    • Cipollone, F.1    Iezzi, A.2    Fazia, M.3    Zucchelli, M.4    Pini, B.5
  • 32
    • 0033603241 scopus 로고    scopus 로고
    • RAGE mediates a novel proinflammatory axis: A central cell surface receptor for S100/ calgranulin polypeptides
    • Hofmann MA, Drury S, Fu C, Qu W, Taguchi A, et al. (1999) RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/ calgranulin polypeptides. Cell 97: 889-901.
    • (1999) Cell , vol.97 , pp. 889-901
    • Hofmann, M.A.1    Drury, S.2    Fu, C.3    Qu, W.4    Taguchi, A.5
  • 33
    • 0031717894 scopus 로고    scopus 로고
    • Suppression of accelerated diabetic atherosclerosis by the soluble receptor for advanced glycation endproducts
    • Park L, Raman KG, Lee KJ, Lu Y, Ferran LJ, Jr., et al. (1998) Suppression of accelerated diabetic atherosclerosis by the soluble receptor for advanced glycation endproducts. Nat Med 4: 1025-1031.
    • (1998) Nat Med , vol.4 , pp. 1025-1031
    • Park, L.1    Raman, K.G.2    Lee, K.J.3    Lu, Y.4    Ferran Jr., L.J.5
  • 34
    • 0033941219 scopus 로고    scopus 로고
    • Tumour necrosis factor-alpha plasma level in patients with type 1 diabetes mellitus and its association with glycaemic control and cardiovascular risk factors
    • Lechleitner M, Koch T, Herold M, Dzien A, Hoppichler F (2000) Tumour necrosis factor-alpha plasma level in patients with type 1 diabetes mellitus and its association with glycaemic control and cardiovascular risk factors. J Intern Med 248: 67-76.
    • (2000) J Intern Med , vol.248 , pp. 67-76
    • Lechleitner, M.1    Koch, T.2    Herold, M.3    Dzien, A.4    Hoppichler, F.5
  • 35
    • 0026959405 scopus 로고
    • Serum levels of tumor necrosis factor in insulin-dependent diabetic patients
    • Foss MC, Foss NT, Paccola GM, Silva CL (1992) Serum levels of tumor necrosis factor in insulin-dependent diabetic patients. Braz J Med Biol Res 25: 239-242.
    • (1992) Braz J Med Biol Res , vol.25 , pp. 239-242
    • Foss, M.C.1    Foss, N.T.2    Paccola, G.M.3    Silva, C.L.4
  • 37
    • 45149118855 scopus 로고    scopus 로고
    • Intensive glycemic control in the ACCORD and ADVANCE trials
    • Dluhy RG, McMahon GT (2008) Intensive glycemic control in the ACCORD and ADVANCE trials. N Engl J Med 358: 2630-2633.
    • (2008) N Engl J Med , vol.358 , pp. 2630-2633
    • Dluhy, R.G.1    McMahon, G.T.2
  • 38
    • 77954654472 scopus 로고    scopus 로고
    • Effects of medical therapies on retinopathy progression in type 2 diabetes
    • Chew EY, Ambrosius WT, Davis MD, Danis RP, Gangaputra S, et al. (2010) Effects of medical therapies on retinopathy progression in type 2 diabetes. N Engl J Med 363: 233-244.
    • (2010) N Engl J Med , vol.363 , pp. 233-244
    • Chew, E.Y.1    Ambrosius, W.T.2    Davis, M.D.3    Danis, R.P.4    Gangaputra, S.5
  • 39
    • 0026465540 scopus 로고
    • The Epstein-Barr virus LMP1 gene product induces A20 zinc finger protein expression by activating NF-kB
    • Laherty CD, Hu HM, Opipari AW, Wang F, Dixit VM (1992) The Epstein-Barr virus LMP1 gene product induces A20 zinc finger protein expression by activating NF-kB. J BiolChem 267: 24157-24160.
    • (1992) J BiolChem , vol.267 , pp. 24157-24160
    • Laherty, C.D.1    Hu, H.M.2    Opipari, A.W.3    Wang, F.4    Dixit, V.M.5
  • 40
    • 0034710891 scopus 로고    scopus 로고
    • Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation
    • Du XL, Edelstein D, Rossetti L, Fantus IG, Goldberg H, 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 U S A 97: 12222-12226.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 12222-12226
    • Du, X.L.1    Edelstein, D.2    Rossetti, L.3    Fantus, I.G.4    Goldberg, H.5
  • 41
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68: 1015-1068.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 43
    • 2342539803 scopus 로고    scopus 로고
    • O-GlcNAc modification: A nutritional sensor that modulates proteasome function
    • Zachara NE, Hart GW (2004) O-GlcNAc modification: a nutritional sensor that modulates proteasome function. Trends Cell Biol 14: 218-221.
    • (2004) Trends Cell Biol , vol.14 , pp. 218-221
    • Zachara, N.E.1    Hart, G.W.2
  • 44
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility
    • Han I, Kudlow JE (1997) Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol Cell Biol 17: 2550-2558.
    • (1997) Mol Cell Biol , vol.17 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 45
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, et al. (2003) O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 115: 715-725.
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5
  • 46
    • 0033591451 scopus 로고    scopus 로고
    • An N-terminal region of Sp1 targets its proteasome-dependent degradation in vitro
    • Su K, Roos MD, Yang X, Han I, Paterson AJ, et al. (1999) An N-terminal region of Sp1 targets its proteasome-dependent degradation in vitro. J Biol Chem 274: 15194-15202.
    • (1999) J Biol Chem , vol.274 , pp. 15194-15202
    • Su, K.1    Roos, M.D.2    Yang, X.3    Han, I.4    Paterson, A.J.5
  • 47
    • 77949769388 scopus 로고    scopus 로고
    • O-linked beta-N-acetylglucosamine (OGlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
    • Butkinaree C, Park K, Hart GW (2009) O-linked beta-N-acetylglucosamine (OGlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress. Biochim Biophys Acta 1800: 96-106.
    • (2009) Biochim Biophys Acta , vol.1800 , pp. 96-106
    • Butkinaree, C.1    Park, K.2    Hart, G.W.3
  • 48
    • 0028908348 scopus 로고
    • Advanced protein glycosylation in diabetes
    • Brownlee M (1995) Advanced protein glycosylation in diabetes. Ann Rev Med 46: 223-234.
    • (1995) Ann Rev Med , vol.46 , pp. 223-234
    • Brownlee, M.1
  • 49
    • 33847058785 scopus 로고    scopus 로고
    • Tag Polymorphisms at the A20 (TNFAIP3) Locus Are Associated With Lower Gene Expression and Increased Risk of Coronary Artery Disease in Type 2 Diabetes
    • Boonyasrisawat W, Eberle D, Bacci S, Zhang YY, Nolan D, et al. (2007) Tag Polymorphisms at the A20 (TNFAIP3) Locus Are Associated With Lower Gene Expression and Increased Risk of Coronary Artery Disease in Type 2 Diabetes. Diabetes 56: 499-505.
    • (2007) Diabetes , vol.56 , pp. 499-505
    • Boonyasrisawat, W.1    Eberle, D.2    Bacci, S.3    Zhang, Y.Y.4    Nolan, D.5
  • 50
    • 0036231781 scopus 로고    scopus 로고
    • Flux through the hexosamine pathway is a determinant of nuclear factor kappaB- dependent promoter activation
    • James LR, Tang D, Ingram A, Ly H, Thai K, et al. (2002) Flux through the hexosamine pathway is a determinant of nuclear factor kappaB- dependent promoter activation. Diabetes 51: 1146-1156.
    • (2002) Diabetes , vol.51 , pp. 1146-1156
    • James, L.R.1    Tang, D.2    Ingram, A.3    Ly, H.4    Thai, K.5
  • 51
    • 0030921166 scopus 로고    scopus 로고
    • Protective genes expressed in endothelial cells: A regulatory response to injury
    • Bach FH, Hancock WW, Ferran C (1997) Protective genes expressed in endothelial cells: a regulatory response to injury. Immunol Today 18: 483-486.
    • (1997) Immunol Today , vol.18 , pp. 483-486
    • Bach, F.H.1    Hancock, W.W.2    Ferran, C.3
  • 52
    • 0041358574 scopus 로고    scopus 로고
    • A novel potential therapy for diabetic nephropathy and vascular complications: Protein kinase C beta inhibition
    • Tuttle KR, Anderson PW (2003) A novel potential therapy for diabetic nephropathy and vascular complications: protein kinase C beta inhibition. Am J Kidney Dis 42: 456-465.
    • (2003) Am J Kidney Dis , vol.42 , pp. 456-465
    • Tuttle, K.R.1    Anderson, P.W.2
  • 53
    • 33644842187 scopus 로고    scopus 로고
    • Inhibition of PKC beta by oral administration of ruboxistaurin is well tolerated and ameliorates diabetes-induced retinal hemodynamic abnormalities in patients
    • Aiello LP, Clermont A, Arora V, Davis MD, Sheetz MJ, et al. (2006) Inhibition of PKC beta by oral administration of ruboxistaurin is well tolerated and ameliorates diabetes-induced retinal hemodynamic abnormalities in patients. Invest Ophthalmol Vis Sci 47: 86-92.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 86-92
    • Aiello, L.P.1    Clermont, A.2    Arora, V.3    Davis, M.D.4    Sheetz, M.J.5
  • 54
    • 0034682796 scopus 로고    scopus 로고
    • The receptor for advanced glycation end products is induced by the glycation products themselves and tumor necrosis factor-alpha through nuclear factorkappa B, and by 17beta-estradiol through Sp-1 in human vascular endothelial cells
    • Tanaka N, Yonekura H, Yamagishi S, Fujimori H, Yamamoto Y, et al. (2000) The receptor for advanced glycation end products is induced by the glycation products themselves and tumor necrosis factor-alpha through nuclear factorkappa B, and by 17beta-estradiol through Sp-1 in human vascular endothelial cells. J Biol Chem 275: 25781-25790.
    • (2000) J Biol Chem , vol.275 , pp. 25781-25790
    • Tanaka, N.1    Yonekura, H.2    Yamagishi, S.3    Fujimori, H.4    Yamamoto, Y.5
  • 55
    • 1842434301 scopus 로고    scopus 로고
    • Tight glycemic control in diabetic coronary artery bypass graft patients improves perioperative outcomes and decreases recurrent ischemic events
    • Lazar HL, Chipkin SR, Fitzgerald CA, Bao Y, Cabral H, et al. (2004) Tight glycemic control in diabetic coronary artery bypass graft patients improves perioperative outcomes and decreases recurrent ischemic events. Circulation 109: 1497-1502.
    • (2004) Circulation , vol.109 , pp. 1497-1502
    • Lazar, H.L.1    Chipkin, S.R.2    Fitzgerald, C.A.3    Bao, Y.4    Cabral, H.5
  • 56
    • 1842866397 scopus 로고    scopus 로고
    • Neointimal proliferation within carotid stents is more pronounced in diabetic patients with initial poor glycaemic state
    • Willfort-Ehringer A, Ahmadi R, Gessl A, Gschwandtner ME, Haumer A, et al. (2004) Neointimal proliferation within carotid stents is more pronounced in diabetic patients with initial poor glycaemic state. Diabetologia 47: 400-406.
    • (2004) Diabetologia , vol.47 , pp. 400-406
    • Willfort-Ehringer, A.1    Ahmadi, R.2    Gessl, A.3    Gschwandtner, M.E.4    Haumer, A.5
  • 57
    • 0021280147 scopus 로고
    • Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc
    • 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: 3308-3317.
    • (1984) J Biol Chem , vol.259 , pp. 3308-3317
    • Torres, C.R.1    Hart, G.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.