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Volumn 387, Issue 1, 2009, Pages 70-76

Increased O-GlcNAc causes disrupted lens fiber cell differentiation and cataracts

Author keywords

Diabetes; Glycosylation; NCOAT; Proteasome; Transgenic mice

Indexed keywords

DOXYCYCLINE; GAMMA CRYSTALLIN; GREEN FLUORESCENT PROTEIN; N ACETYLGLUCOSAMINE; PROTEASOME;

EID: 67651048549     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.06.132     Document Type: Article
Times cited : (11)

References (26)
  • 2
    • 4043127599 scopus 로고    scopus 로고
    • Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses
    • Harrington V., McCall S., Huynh S., Srivastava K., and Srivastava O.P. Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses. Mol. Vis. 10 (2004) 476-489
    • (2004) Mol. Vis. , vol.10 , pp. 476-489
    • Harrington, V.1    McCall, S.2    Huynh, S.3    Srivastava, K.4    Srivastava, O.P.5
  • 3
    • 18044388716 scopus 로고    scopus 로고
    • Age-related nuclear cataract-oxidation is the key
    • Truscott R.J. Age-related nuclear cataract-oxidation is the key. Exp. Eye Res. 80 (2005) 709-725
    • (2005) Exp. Eye Res. , vol.80 , pp. 709-725
    • Truscott, R.J.1
  • 4
    • 2942610705 scopus 로고    scopus 로고
    • Age-dependent protein modifications and declining proteasome activity in the human lens
    • Viteri G., Carrard G., Birlouez-Aragon I., Silva E., and Friguet B. Age-dependent protein modifications and declining proteasome activity in the human lens. Arch. Biochem. Biophys. 427 (2004) 197-203
    • (2004) Arch. Biochem. Biophys. , vol.427 , pp. 197-203
    • Viteri, G.1    Carrard, G.2    Birlouez-Aragon, I.3    Silva, E.4    Friguet, B.5
  • 5
    • 0032144578 scopus 로고    scopus 로고
    • Proteolytic cleavage of N-Succ-Leu-Leu-Val-Tyr-AMC by the proteasome in lens epithelium from clear and cataractous human lenses
    • Andersson M., SjOstrand J., and Karlsson J. Proteolytic cleavage of N-Succ-Leu-Leu-Val-Tyr-AMC by the proteasome in lens epithelium from clear and cataractous human lenses. Exp. Eye Res. 67 (1998) 231-236
    • (1998) Exp. Eye Res. , vol.67 , pp. 231-236
    • Andersson, M.1    SjOstrand, J.2    Karlsson, J.3
  • 6
    • 0037524357 scopus 로고    scopus 로고
    • O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar
    • Wells L., and Hart G.W. O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar. FEBS Lett. 546 (2003) 154-158
    • (2003) FEBS Lett. , vol.546 , pp. 154-158
    • Wells, L.1    Hart, G.W.2
  • 7
    • 0034854157 scopus 로고    scopus 로고
    • Glycan-dependent signaling: O-linked N-acetylglucosamine
    • Hanover J.A. Glycan-dependent signaling: O-linked N-acetylglucosamine. FASEB J. 15 (2001) 1865-1876
    • (2001) FASEB J. , vol.15 , pp. 1865-1876
    • Hanover, J.A.1
  • 8
    • 0030944105 scopus 로고    scopus 로고
    • O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • Lubas W.A., Frank D.W., Krause M., and Hanover J.A. O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272 (1997) 9316-9324
    • (1997) J. Biol. Chem. , vol.272 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.A.4
  • 9
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins: cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
    • Kreppel L.K., Blomberg M.A., and Hart G.W. Dynamic glycosylation of nuclear and cytosolic proteins: cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272 (1997) 9308-9315
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 10
    • 0035971182 scopus 로고    scopus 로고
    • Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain
    • Gao Y., Wells L., Comer F.I., Parker G.J., and Hart G.W. 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 (2001) 9838-9845
    • (2001) J. Biol. Chem. , vol.276 , pp. 9838-9845
    • Gao, Y.1    Wells, L.2    Comer, F.I.3    Parker, G.J.4    Hart, G.W.5
  • 11
    • 11144246904 scopus 로고    scopus 로고
    • Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities
    • Toleman C., Paterson A.J., Whisenhunt T.R., and Kudlow J.E. Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. J. Biol. Chem. 279 (2004) 53665-53673
    • (2004) J. Biol. Chem. , vol.279 , pp. 53665-53673
    • Toleman, C.1    Paterson, A.J.2    Whisenhunt, T.R.3    Kudlow, J.E.4
  • 12
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F., Su K., Yang X., Bowe D.B., Paterson A.J., and Kudlow J.E. O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 115 (2003) 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    Kudlow, J.E.6
  • 13
    • 0037304213 scopus 로고    scopus 로고
    • High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin
    • Walgren J.L., Vincent T.S., Schey K.L., and Buse M.G. High glucose and insulin promote O-GlcNAc modification of proteins, including alpha-tubulin. Am. J. Physiol. Endocrinol. Metab. 284 (2003) E424-E434
    • (2003) Am. J. Physiol. Endocrinol. Metab. , vol.284
    • Walgren, J.L.1    Vincent, T.S.2    Schey, K.L.3    Buse, M.G.4
  • 14
    • 0034646330 scopus 로고    scopus 로고
    • Glucose stimulates protein modification by O-linked GlcNAc in pancreatic beta cells: linkage of O-linked GlcNAc to beta cell death
    • Liu K., Paterson A.J., Chin E., and Kudlow J.E. 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 (2000) 2820-2825
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2820-2825
    • Liu, K.1    Paterson, A.J.2    Chin, E.3    Kudlow, J.E.4
  • 15
    • 33846488647 scopus 로고    scopus 로고
    • Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats
    • Akimoto Y., Hart G.W., Wells L., Vosseller K., Yamamoto K., Munetomo E., Ohara-Imaizumi M., Nishiwaki C., Nagamatsu S., Hirano H., and Kawakami H. Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats. Glycobiology 17 (2007) 127-140
    • (2007) Glycobiology , vol.17 , pp. 127-140
    • Akimoto, Y.1    Hart, G.W.2    Wells, L.3    Vosseller, K.4    Yamamoto, K.5    Munetomo, E.6    Ohara-Imaizumi, M.7    Nishiwaki, C.8    Nagamatsu, S.9    Hirano, H.10    Kawakami, H.11
  • 16
    • 0031943723 scopus 로고    scopus 로고
    • Insulin and glucosamine infusions increase O-linked N-acetyl-glucosamine in skeletal muscle proteins in vivo
    • Yki-Jarvinen H., Virkamaki A., Daniels M.C., McClain D., and Gottschalk W.K. Insulin and glucosamine infusions increase O-linked N-acetyl-glucosamine in skeletal muscle proteins in vivo. Metabolism 47 (1998) 449-455
    • (1998) Metabolism , vol.47 , pp. 449-455
    • Yki-Jarvinen, H.1    Virkamaki, A.2    Daniels, M.C.3    McClain, D.4    Gottschalk, W.K.5
  • 17
    • 0027390387 scopus 로고
    • Bovine lens epithelial cells have a ubiquitin-dependent proteolysis system
    • Huang L.L., Jahngen-Hodge J., and Taylor A. Bovine lens epithelial cells have a ubiquitin-dependent proteolysis system. Biochim. Biophys. Acta 1175 (1993) 181-187
    • (1993) Biochim. Biophys. Acta , vol.1175 , pp. 181-187
    • Huang, L.L.1    Jahngen-Hodge, J.2    Taylor, A.3
  • 18
    • 0037402905 scopus 로고    scopus 로고
    • Lens fibers have a fully functional ubiquitin-proteasome pathway
    • Pereira P., Shang F., Hobbs M., Girao H., and Taylor A. Lens fibers have a fully functional ubiquitin-proteasome pathway. Exp. Eye Res. 76 (2003) 623-631
    • (2003) Exp. Eye Res. , vol.76 , pp. 623-631
    • Pereira, P.1    Shang, F.2    Hobbs, M.3    Girao, H.4    Taylor, A.5
  • 20
  • 23
    • 0030907389 scopus 로고    scopus 로고
    • Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility
    • Han I., and Kudlow J.E. Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility. Mol. Cell. Biol. 17 (1997) 2550-2558
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2550-2558
    • Han, I.1    Kudlow, J.E.2
  • 25
    • 18244396127 scopus 로고    scopus 로고
    • Subcellular redistribution of components of the ubiquitin-proteasome pathway during lens differentiation and maturation
    • Girao H., Pereira P., Taylor A., and Shang F. Subcellular redistribution of components of the ubiquitin-proteasome pathway during lens differentiation and maturation. Invest. Ophthalmol. Vis. Sci. 46 (2005) 1386-1392
    • (2005) Invest. Ophthalmol. Vis. Sci. , vol.46 , pp. 1386-1392
    • Girao, H.1    Pereira, P.2    Taylor, A.3    Shang, F.4
  • 26
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor J.P., Hardy J., and Fischbeck K.H. Toxic proteins in neurodegenerative disease. Science 296 (2002) 1991-1995
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.