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Volumn 52, Issue 7, 2011, Pages 4182-4191

Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA CRYSTALLIN; BETA CRYSTALLIN; CARBONYL REDUCTASE; DKFZP434A0627 PROTEIN; FILENSIN; GAMMA CRYSTALLIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LENS PROTEIN; PROTEIN SERINE THREONINE KINASE; RETINAL DEHYDROGENASE; UNCLASSIFIED DRUG; CRYSTALLIN; EYE PROTEIN;

EID: 80051950364     PISSN: 01460404     EISSN: 15525783     Source Type: Journal    
DOI: 10.1167/iovs.10-7094     Document Type: Article
Times cited : (48)

References (53)
  • 2
    • 0036841037 scopus 로고    scopus 로고
    • Incidence of age-related cataract over a 10-year interval: The Beaver Dam Eye Study
    • Klein BE, Klein R, Lee KE. Incidence of age-related cataract over a 10-year interval: the Beaver Dam Eye Study. Ophthalmology. 2002;109:2052-2057.
    • (2002) Ophthalmology. , vol.109 , pp. 2052-2057
    • Klein, B.E.1    Klein, R.2    Lee, K.E.3
  • 3
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA. 1992;89:10449-10453.
    • (1992) Proc Natl Acad Sci USA. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 4
    • 0027342592 scopus 로고
    • Proctor lecture. The function of alpha-crystallin
    • Horwitz J. Proctor lecture. The function of alpha-crystallin. Invest Ophthalmol Visual Sci. 1993;34:10-22.
    • (1993) Invest Ophthalmol Visual Sci. , vol.34 , pp. 10-22
    • Horwitz, J.1
  • 5
    • 0023721503 scopus 로고
    • Eye lens proteins and transparency: From light transmission theory to solution X-ray structural analysis
    • Tardieu A. Eye lens proteins and transparency: from light transmission theory to solution X-ray structural analysis. Annu Rev Biophys Biophys Chem. 1988;17:47-70.
    • (1988) Annu Rev Biophys Biophys Chem. , vol.17 , pp. 47-70
    • Tardieu, A.1
  • 6
    • 0028973109 scopus 로고
    • Evidence that alphacrystallin prevents non-specific protein aggregation in the intact eye lens
    • Rao PV, Huang QL, Horwitz J, Zigler JS Jr. Evidence that alphacrystallin prevents non-specific protein aggregation in the intact eye lens. Biochim Biophys Acta. 1995;1245:439-447.
    • (1995) Biochim Biophys Acta. , vol.1245 , pp. 439-447
    • Rao, P.V.1    Huang, Q.L.2    Horwitz, J.3    Zigler Jr., J.S.4
  • 7
    • 0036976370 scopus 로고    scopus 로고
    • Effect of long-term dietary manipulation on the aggregation of rat lens crystallins: Role of alpha-crystallin chaperone function
    • Reddy GB, Reddy PY, Vijayalakshmi A, Kumar MS, Suryanarayana P, Sesikeran B. Effect of long-term dietary manipulation on the aggregation of rat lens crystallins: role of alpha-crystallin chaperone function. Mol Vision. 2002;8:298-305.
    • (2002) Mol Vision. , vol.8 , pp. 298-305
    • Reddy, G.B.1    Reddy, P.Y.2    Vijayalakshmi, A.3    Kumar, M.S.4    Suryanarayana, P.5    Sesikeran, B.6
  • 8
    • 0029770039 scopus 로고    scopus 로고
    • Cloning, expression, and chaperone-like activity of human alphaA-crystallin
    • Andley UP, Mathur S, Griest TA, Petrash JM. Cloning, expression, and chaperone-like activity of human alphaA-crystallin. J Biol Chem. 1996;271:31973-31980.
    • (1996) J Biol Chem. , vol.271 , pp. 31973-31980
    • Andley, U.P.1    Mathur, S.2    Griest, T.A.3    Petrash, J.M.4
  • 10
    • 0034822088 scopus 로고    scopus 로고
    • Chaperone function of mutant versions of alpha A-and alpha B-crystallin prepared to pinpoint chaperone binding sites
    • Derham BK, van Boekel MA, Muchowski PJ, et al. Chaperone function of mutant versions of alpha A-and alpha B-crystallin prepared to pinpoint chaperone binding sites. Eur J Biochem. 2001;268:713-721.
    • (2001) Eur J Biochem. , vol.268 , pp. 713-721
    • Derham, B.K.1    van Boekel, M.A.2    Muchowski, P.J.3
  • 12
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin
    • Muchowski PJ, Clark JI. ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin. Proc Natl Acad Sci USA. 1998;95:1004-1009.
    • (1998) Proc Natl Acad Sci USA. , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 13
    • 0030933472 scopus 로고    scopus 로고
    • Conformational and functional differences between recombinant human lens alphaA-and alphaB-crystallin
    • Sun TX, Das BK, Liang JJ. Conformational and functional differences between recombinant human lens alphaA-and alphaB-crystallin. J Biol Chem. 1997;272:6220-6225.
    • (1997) J Biol Chem. , vol.272 , pp. 6220-6225
    • Sun, T.X.1    Das, B.K.2    Liang, J.J.3
  • 14
    • 52049097263 scopus 로고    scopus 로고
    • Multi-crystallin complexes exist in the water-soluble high molecular weight protein fractions of aging normal and cataractous human lenses
    • Srivastava K, Chaves JM, Srivastava OP, Kirk M. Multi-crystallin complexes exist in the water-soluble high molecular weight protein fractions of aging normal and cataractous human lenses. Exp Eye Res. 2008;87:356-366.
    • (2008) Exp Eye Res. , vol.87 , pp. 356-366
    • Srivastava, K.1    Chaves, J.M.2    Srivastava, O.P.3    Kirk, M.4
  • 15
    • 1642524490 scopus 로고    scopus 로고
    • Characterization of covalent multimers of crystallins in aging human lenses
    • Srivastava OP, Kirk MC, Srivastava K. Characterization of covalent multimers of crystallins in aging human lenses. J Biol Chem. 2004;279:10901-10909.
    • (2004) J Biol Chem. , vol.279 , pp. 10901-10909
    • Srivastava, O.P.1    Kirk, M.C.2    Srivastava, K.3
  • 16
    • 0032128377 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry
    • Lampi KJ, Ma Z, Hanson SR, et al. Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry. Exp Eye Res. 1998;67:31-43.
    • (1998) Exp Eye Res. , vol.67 , pp. 31-43
    • Lampi, K.J.1    Ma, Z.2    Hanson, S.R.3
  • 17
    • 70349263467 scopus 로고    scopus 로고
    • Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry
    • Grey AC, Schey KL. Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry. Invest Ophthalmol Vis Sci. 2009;50:4319-4329.
    • (2009) Invest Ophthalmol Vis Sci. , vol.50 , pp. 4319-4329
    • Grey, A.C.1    Schey, K.L.2
  • 18
    • 34748888365 scopus 로고    scopus 로고
    • Proteomic analysis of water insoluble proteins from normal and cataractous human lenses
    • Harrington V, Srivastava OP, Kirk M. Proteomic analysis of water insoluble proteins from normal and cataractous human lenses. Mol Vis. 2007;13:1680-1694.
    • (2007) Mol Vis. , vol.13 , pp. 1680-1694
    • Harrington, V.1    Srivastava, O.P.2    Kirk, M.3
  • 19
    • 0014373922 scopus 로고
    • Color and solubility of the proteins of human cataracts
    • Pirie A. Color and solubility of the proteins of human cataracts. Invest Ophthalmol. 1968;7:634-750.
    • (1968) Invest Ophthalmol. , vol.7 , pp. 634-750
    • Pirie, A.1
  • 20
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • Rabilloud T. Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis. 1998;19:758-760.
    • (1998) Electrophoresis. , vol.19 , pp. 758-760
    • Rabilloud, T.1
  • 21
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg A, Weiss W, Dunn MJ. Current two-dimensional electrophoresis technology for proteomics. Proteomics. 2004;4:3665-3685.
    • (2004) Proteomics. , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 22
    • 0034630358 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients
    • Molloy MP. Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients. Anal Biochem. 2000;280: 1-10.
    • (2000) Anal Biochem. , vol.280 , pp. 1-10
    • Molloy, M.P.1
  • 24
    • 77954709516 scopus 로고    scopus 로고
    • Proteomic analysis of colonic mucosa in a rat model of irritable bowel syndrome
    • Ding Y, Lu B, Chen D, Meng L, Shen Y, Chen S. Proteomic analysis of colonic mucosa in a rat model of irritable bowel syndrome. Proteomics. 2010;10:2620-2630.
    • (2010) Proteomics. , vol.10 , pp. 2620-2630
    • Ding, Y.1    Lu, B.2    Chen, D.3    Meng, L.4    Shen, Y.5    Chen, S.6
  • 25
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y, Oda Y, Tabata T, et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics. 2005;4:1265-1272.
    • (2005) Mol Cell Proteomics. , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3
  • 26
    • 77952301017 scopus 로고    scopus 로고
    • Identification of crystallin modifications in the human lens cortex and nucleus using laser capture microdissection and CyDye labeling
    • Asomugha CO, Gupta R, Srivastava OP. Identification of crystallin modifications in the human lens cortex and nucleus using laser capture microdissection and CyDye labeling. Mol Vis. 2010;16: 476-494.
    • (2010) Mol Vis. , vol.16 , pp. 476-494
    • Asomugha, C.O.1    Gupta, R.2    Srivastava, O.P.3
  • 27
    • 0042665900 scopus 로고    scopus 로고
    • Multiplex proteomic analysis by two-dimensional differential in-gel electrophoresis
    • Knowles MR, Cervino S, Skynner HA, et al. Multiplex proteomic analysis by two-dimensional differential in-gel electrophoresis. Proteomics. 2003;3:1162-1171.
    • (2003) Proteomics. , vol.3 , pp. 1162-1171
    • Knowles, M.R.1    Cervino, S.2    Skynner, H.A.3
  • 28
    • 0028293240 scopus 로고
    • Characterization of the alpha-gamma and alpha-beta complex: Evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone
    • Boyle D, Takemoto L. Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone. Exp Eye Res. 1994;58: 9-15.
    • (1994) Exp Eye Res. , vol.58 , pp. 9-15
    • Boyle, D.1    Takemoto, L.2
  • 29
    • 0032986520 scopus 로고    scopus 로고
    • Alpha-crystallin as a molecular chaperone
    • Derham BK, Harding JJ. Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res. 1999;18:463-509.
    • (1999) Prog Retin Eye Res. , vol.18 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 30
    • 0033968166 scopus 로고    scopus 로고
    • Small heat-shock proteins and their potential role in human disease
    • Clark JI, Muchowski PJ. Small heat-shock proteins and their potential role in human disease. Curr Opin Struct Biol. 2000;10:52-59.
    • (2000) Curr Opin Struct Biol. , vol.10 , pp. 52-59
    • Clark, J.I.1    Muchowski, P.J.2
  • 31
    • 77952299727 scopus 로고    scopus 로고
    • Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats
    • Sakthivel M, Elanchezhian R, Thomas PA, Geraldine P. Alterations in lenticular proteins during ageing and selenite-induced cataractogenesis in Wistar rats. Mol Vis. 2010;16:445-453.
    • (2010) Mol Vis. , vol.16 , pp. 445-453
    • Sakthivel, M.1    Elanchezhian, R.2    Thomas, P.A.3    Geraldine, P.4
  • 32
    • 0026666722 scopus 로고
    • The ability of alpha crystallin to protect against heat-induced aggregation is age-dependent
    • Horwitz J, Emmons T, Takemoto L. The ability of alpha crystallin to protect against heat-induced aggregation is age-dependent. Curr Eye Res. 1992;11:817-822.
    • (1992) Curr Eye Res. , vol.11 , pp. 817-822
    • Horwitz, J.1    Emmons, T.2    Takemoto, L.3
  • 34
    • 0032078745 scopus 로고    scopus 로고
    • NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins
    • Carver JA, Lindner RA. NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins. Int J Biol Macromol. 1998;22:197-209.
    • (1998) Int J Biol Macromol. , vol.22 , pp. 197-209
    • Carver, J.A.1    Lindner, R.A.2
  • 35
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone alpha-crystallin with unfolding alphalactalbumin: A structural and kinetic spectroscopic study
    • Carver JA, Lindner RA, Lyon C, et al. The interaction of the molecular chaperone alpha-crystallin with unfolding alphalactalbumin: a structural and kinetic spectroscopic study. J Mol Biol. 2002;318:815-827.
    • (2002) J Mol Biol. , vol.318 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3
  • 36
    • 0042121150 scopus 로고    scopus 로고
    • Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate
    • Zhang Z, Smith DL, Smith JB. Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate. Exp Eye Res. 2003;77:259-272.
    • (2003) Exp Eye Res. , vol.77 , pp. 259-272
    • Zhang, Z.1    Smith, D.L.2    Smith, J.B.3
  • 37
    • 59349092370 scopus 로고    scopus 로고
    • Deamidation alters interactions of beta-crystallins in hetero-oligomers
    • Takata T, Woodbury LG, Lampi KJ. Deamidation alters interactions of beta-crystallins in hetero-oligomers. Mol Vis. 2009;15:241-249.
    • (2009) Mol Vis. , vol.15 , pp. 241-249
    • Takata, T.1    Woodbury, L.G.2    Lampi, K.J.3
  • 38
    • 35648932100 scopus 로고    scopus 로고
    • Post-translational modifications in the nuclear region of young, aged, and cataract human lenses
    • Hains PG, Truscott RJ. Post-translational modifications in the nuclear region of young, aged, and cataract human lenses. J Proteome Res. 2007;6:3935-3943.
    • (2007) J Proteome Res. , vol.6 , pp. 3935-3943
    • Hains, P.G.1    Truscott, R.J.2
  • 39
    • 77953276375 scopus 로고    scopus 로고
    • Age-dependent deamidation of lifelong proteins in the human lens
    • Hains PG, Truscott RJ. Age-dependent deamidation of lifelong proteins in the human lens. Invest Ophthalmol Vis Sci. 2010;51: 3107-3114.
    • (2010) Invest Ophthalmol Vis Sci. , vol.51 , pp. 3107-3114
    • Hains, P.G.1    Truscott, R.J.2
  • 40
    • 77954760090 scopus 로고    scopus 로고
    • Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone
    • Acosta-Sampson L, King J. Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone. J Mol Biol. 2010;401:134-152.
    • (2010) J Mol Biol. , vol.401 , pp. 134-152
    • Acosta-Sampson, L.1    King, J.2
  • 41
    • 2942619847 scopus 로고
    • Enzyme activity patterns in clear human lenses and in different types of human senile cataract
    • Friedburg D. Enzyme activity patterns in clear human lenses and in different types of human senile cataract. Ciba Foundation Symposium. 1973;19:117-133.
    • (1973) Ciba Foundation Symposium. , vol.19 , pp. 117-133
    • Friedburg, D.1
  • 42
    • 33749447728 scopus 로고    scopus 로고
    • Thioredoxin, thioredoxin reductase, and alpha-crystallin revive inactivated glyceraldehyde 3-phosphate dehydrogenase in human aged and cataract lens extracts
    • Yan H, Lou MF, Fernando MR, Harding JJ. Thioredoxin, thioredoxin reductase, and alpha-crystallin revive inactivated glyceraldehyde 3-phosphate dehydrogenase in human aged and cataract lens extracts. Mol Vis. 2006;12:1153-1159.
    • (2006) Mol Vis. , vol.12 , pp. 1153-1159
    • Yan, H.1    Lou, M.F.2    Fernando, M.R.3    Harding, J.J.4
  • 43
    • 5644275139 scopus 로고    scopus 로고
    • Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function
    • Biswas A, Das KP. Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function. J Biol Chem. 2004;279:42648-42657.
    • (2004) J Biol Chem. , vol.279 , pp. 42648-42657
    • Biswas, A.1    Das, K.P.2
  • 44
    • 34548476945 scopus 로고    scopus 로고
    • Multiple and additive functions of ALDH3A1 and ALDH1A1: Cataract phenotype and ocular oxidative damage in Aldh3a1(-/-)/Aldh1a1(-/-) knock-out mice
    • Lassen N, Bateman JB, Estey T, et al. Multiple and additive functions of ALDH3A1 and ALDH1A1: cataract phenotype and ocular oxidative damage in Aldh3a1(-/-)/Aldh1a1(-/-) knock-out mice. J Biol Chem. 2007;282:25668-25676.
    • (2007) J Biol Chem. , vol.282 , pp. 25668-25676
    • Lassen, N.1    Bateman, J.B.2    Estey, T.3
  • 45
    • 0036892305 scopus 로고    scopus 로고
    • Discovery of novel targets of quinoline drugs in the human purine binding proteome
    • Graves PR, Kwiek JJ, Fadden P, et al. Discovery of novel targets of quinoline drugs in the human purine binding proteome. Mol Pharmacol. 2002;62:1364-1372.
    • (2002) Mol Pharmacol. , vol.62 , pp. 1364-1372
    • Graves, P.R.1    Kwiek, J.J.2    Fadden, P.3
  • 46
    • 0017701178 scopus 로고
    • Lens opacities associated with lipidosis-like ultrastructural alterations in rats treated with chloroquine, chlorphentermine, or iprindole
    • Drenckhahn D, Lullmann-Rauch R. Lens opacities associated with lipidosis-like ultrastructural alterations in rats treated with chloroquine, chlorphentermine, or iprindole. Exp Eye Res. 1977;24:621-632.
    • (1977) Exp Eye Res. , vol.24 , pp. 621-632
    • Drenckhahn, D.1    Lullmann-Rauch, R.2
  • 47
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperone and the cytoskeleton
    • Liang P, Macrae TH. Molecular chaperone and the cytoskeleton. J Cell Sci. 1997;110:1431-1440.
    • (1997) J Cell Sci. , vol.110 , pp. 1431-1440
    • Liang, P.1    Macrae, T.H.2
  • 48
    • 0036366525 scopus 로고    scopus 로고
    • Cytoskeletal competence requires protein chaperones
    • Quinlan R. Cytoskeletal competence requires protein chaperones. Prog Mol Subcell Biol. 2002;28:219-233.
    • (2002) Prog Mol Subcell Biol. , vol.28 , pp. 219-233
    • Quinlan, R.1
  • 49
    • 0032587169 scopus 로고    scopus 로고
    • AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress
    • Muchowski PJ, Valdez MM, Clark JI. AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress. Invest Ophthalmol Vis Sci. 1999;40:951-958.
    • (1999) Invest Ophthalmol Vis Sci. , vol.40 , pp. 951-958
    • Muchowski, P.J.1    Valdez, M.M.2    Clark, J.I.3
  • 50
    • 0028831015 scopus 로고
    • In vitro studies on the assembly properties of the lens proteins CP 49, CP 115: Coassembly with alpha crystalline but not with vimentin
    • Carter JM, Hutcheson AM, Quinlan RA. In vitro studies on the assembly properties of the lens proteins CP 49, CP 115: coassembly with alpha crystalline but not with vimentin. Exp Eye Res. 1995;60:181-192.
    • (1995) Exp Eye Res. , vol.60 , pp. 181-192
    • Carter, J.M.1    Hutcheson, A.M.2    Quinlan, R.A.3
  • 51
    • 0019495032 scopus 로고
    • Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase
    • Wermuth B. Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase. J Biol Chem. 1981;266:1206-1213.
    • (1981) J Biol Chem. , vol.266 , pp. 1206-1213
    • Wermuth, B.1
  • 52
    • 0034783977 scopus 로고    scopus 로고
    • 2001 assessment of nutritional influences on risk for cataract
    • Taylor A, Hobbs M. 2001 assessment of nutritional influences on risk for cataract. Nutrition. 2001;17:845-857.
    • (2001) Nutrition. , vol.17 , pp. 845-857
    • Taylor, A.1    Hobbs, M.2
  • 53
    • 0042198801 scopus 로고    scopus 로고
    • Redox regulation in the lens
    • Lou MF. Redox regulation in the lens. Prog Retin Eye Res. 2003;22:657-682.
    • (2003) Prog Retin Eye Res. , vol.22 , pp. 657-682
    • Lou, M.F.1


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