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Volumn 41, Issue 3, 2000, Pages 832-843

Development and characterization of an H2O2-resistant immortal lens epithelial cell line

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTIOXIDANT; CATALASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; HYDROGEN PEROXIDE; THIOL; GLUTATHIONE; GLYCERALDEHYDE 3 PHOSPHATE; OXIDOREDUCTASE;

EID: 0033622105     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (33)

References (51)
  • 1
    • 0000145042 scopus 로고
    • The lens: Development, proteins, metabolism and cataract
    • Davson J, ed. Orlando: Academic Press
    • Harding JJ, Crabbe MJ. The lens: development, proteins, metabolism and cataract. In: Davson J, ed. The Eye. Orlando: Academic Press; 1984:1B.
    • (1984) The Eye
    • Harding, J.J.1    Crabbe, M.J.2
  • 4
    • 0032052922 scopus 로고    scopus 로고
    • Gene sharing in lens and cornea: Facts and implications
    • Piatigorsky J. Gene sharing in lens and cornea: facts and implications. Prog Retin Eye Res. 1998;17:145-174.
    • (1998) Prog Retin Eye Res. , vol.17 , pp. 145-174
    • Piatigorsky, J.1
  • 5
    • 0029151027 scopus 로고
    • Oxidative stress-induced cataract: Mechanism of action
    • Spector A. Oxidative stress-induced cataract: mechanism of action. FASEB J. 1995;9:1173-1182.
    • (1995) FASEB J. , vol.9 , pp. 1173-1182
    • Spector, A.1
  • 6
    • 0000324675 scopus 로고
    • Studies on the oxidation of cysteine to cystine in lens proteins during cataract formation
    • Dische Z, Zil H. Studies on the oxidation of cysteine to cystine in lens proteins during cataract formation. Am J Ophthalmol. 1951; 34:104-113.
    • (1951) Am J Ophthalmol. , vol.34 , pp. 104-113
    • Dische, Z.1    Zil, H.2
  • 7
    • 0002952307 scopus 로고
    • Protein modification in cataract: Possible oxidative mechanisms
    • Duncan G, ed. New York: Academic Press
    • Augusteyn RC. Protein modification in cataract: possible oxidative mechanisms. In: Duncan G, ed. Mechanisms of Cataract Formation in the Human Lens. New York: Academic Press; 1981:72-115.
    • (1981) Mechanisms of Cataract Formation in the Human Lens , pp. 72-115
    • Augusteyn, R.C.1
  • 9
    • 0019458386 scopus 로고
    • Evidence of increased lipid peroxidation in cataracts
    • Bhuyan KC, Bhuyan DK, Podos SM. Evidence of increased lipid peroxidation in cataracts. IRCS Med Sci. 1981;9:126-127.
    • (1981) IRCS Med Sci. , vol.9 , pp. 126-127
    • Bhuyan, K.C.1    Bhuyan, D.K.2    Podos, S.M.3
  • 10
    • 0022564971 scopus 로고
    • Free radical oxidation of lipids and thiol groups in formation of a cataract
    • Babizhaev MA, Deev AI. Free radical oxidation of lipids and thiol groups in formation of a cataract. Biofizika, 1986;31:109-114.
    • (1986) Biofizika , vol.31 , pp. 109-114
    • Babizhaev, M.A.1    Deev, A.I.2
  • 11
    • 0026008673 scopus 로고
    • Evidence of genotoxic damage in human cataractous lenses
    • Worgul BV, David J, Odrich S, et al. Evidence of genotoxic damage in human cataractous lenses. Mutagen. 1991;6:495-499.
    • (1991) Mutagen , vol.6 , pp. 495-499
    • Worgul, B.V.1    David, J.2    Odrich, S.3
  • 12
    • 0002711549 scopus 로고
    • The lens and oxidative stress
    • Sies H, ed. London: Academic Press
    • Spector A. The lens and oxidative stress. In: Sies H, ed. Oxidative Stress, Oxidants and Antioxidants. London: Academic Press; 1991:529-558.
    • (1991) Oxidative Stress, Oxidants and Antioxidants , pp. 529-558
    • Spector, A.1
  • 14
    • 0033120938 scopus 로고    scopus 로고
    • Hyperbaric oxygen in vivo accelerates the loss of cytoskeletal proteins and MIP26 in guinea pig lens nucleus
    • Padgaonkar VA, Lin LR, Leverenz VR, Rinke A, Reddy VN, Giblin FJ. Hyperbaric oxygen in vivo accelerates the loss of cytoskeletal proteins and MIP26 in guinea pig lens nucleus. Exp Eye Res. 1999;68:493-504.
    • (1999) Exp Eye Res. , vol.68 , pp. 493-504
    • Padgaonkar, V.A.1    Lin, L.R.2    Leverenz, V.R.3    Rinke, A.4    Reddy, V.N.5    Giblin, F.J.6
  • 15
    • 0028943903 scopus 로고
    • Nuclear light scattering, disulfide formation and membrane damage in lenses of older guinea pigs treated with hyperbaric oxygen
    • Giblin FJ, Padgaonkar VA, Leverenz VR, et al. Nuclear light scattering, disulfide formation and membrane damage in lenses of older guinea pigs treated with hyperbaric oxygen. Exp Eye Res. 1995;60:219-235.
    • (1995) Exp Eye Res. , vol.60 , pp. 219-235
    • Giblin, F.J.1    Padgaonkar, V.A.2    Leverenz, V.R.3
  • 16
    • 0019843761 scopus 로고
    • Hydrogen peroxide and human cataract
    • Spector A, Garner WH. Hydrogen peroxide and human cataract Exp Eye Res. 1981;33:673-681.
    • (1981) Exp Eye Res. , vol.33 , pp. 673-681
    • Spector, A.1    Garner, W.H.2
  • 17
    • 0001734528 scopus 로고
    • Peroxide concentration in normal and cataractous human lenses
    • Abstract nr 531
    • Bhuyan DK, Camras CB, Lakhani HK, Bhuyan KC. Peroxide concentration in normal and cataractous human lenses [ARVO Abstract]. Invest Ophthalmol Vis Sci. 1992;33(4):S798. Abstract nr 531.
    • (1992) Invest Ophthalmol Vis Sci. , vol.33 , Issue.4
    • Bhuyan, D.K.1    Camras, C.B.2    Lakhani, H.K.3    Bhuyan, K.C.4
  • 21
    • 0020077814 scopus 로고
    • Glutathione peroxidase from bovine lens: A selenoenzyme
    • Bergad PL, Rathbun WB, Linder W. Glutathione peroxidase from bovine lens: a selenoenzyme. Exp Eye Res. 1982;34:131-144.
    • (1982) Exp Eye Res. , vol.34 , pp. 131-144
    • Bergad, P.L.1    Rathbun, W.B.2    Linder, W.3
  • 22
    • 0015540238 scopus 로고
    • Heme occupancy of catalase in hemoglobin-free perfused rat liver and of isolated rat liver catalase
    • Sies H, Bücher T, Oshino N, Chance B. Heme occupancy of catalase in hemoglobin-free perfused rat liver and of isolated rat liver catalase. Arch Biochem Biophys. 1973;154:106-116.
    • (1973) Arch Biochem Biophys. , vol.154 , pp. 106-116
    • Sies, H.1    Bücher, T.2    Oshino, N.3    Chance, B.4
  • 23
    • 0032192105 scopus 로고    scopus 로고
    • The effect of photochemical stress upon the lenses of normal and glutathione peroxidase-1 knockout mice
    • Spector A, Kuszak JR, Ma W, Wang RR, Ho YS, Yang Y. The effect of photochemical stress upon the lenses of normal and glutathione peroxidase-1 knockout mice. Exp Eye Res. 1998;67:457-471.
    • (1998) Exp Eye Res. , vol.67 , pp. 457-471
    • Spector, A.1    Kuszak, J.R.2    Ma, W.3    Wang, R.R.4    Ho, Y.S.5    Yang, Y.6
  • 24
    • 4244156935 scopus 로고    scopus 로고
    • The effect of aging on the lenses of glutathione peroxidase-1 knockouts
    • Abstract nr 4623
    • Wang RR, Kuszak JR, Ma W, Yang Y, Spector A. The effect of aging on the lenses of glutathione peroxidase-1 knockouts [ARVO Abstract]. Invest Ophthalmol Vis Sci. 1999;40(4):S877. Abstract nr 4623.
    • (1999) Invest Ophthalmol Vis Sci. , vol.40 , Issue.4
    • Wang, R.R.1    Kuszak, J.R.2    Ma, W.3    Yang, Y.4    Spector, A.5
  • 25
    • 0013640492 scopus 로고    scopus 로고
    • Glutathione peroxidase deficiency leads to increased light scattering and changes in morphology in the nucleus of lenses of gene knockout mice
    • Abstract nr 929
    • Reddy VN, Giblin FJ, Lin LR, Dang L, Unakar N, Ho YS. Glutathione peroxidase deficiency leads to increased light scattering and changes in morphology in the nucleus of lenses of gene knockout mice [ARVO Abstract]. Invest Ophthalmol Vis Sci. 1998;39(4): S196. Abstract nr 929.
    • (1998) Invest Ophthalmol Vis Sci. , vol.39 , Issue.4
    • Reddy, V.N.1    Giblin, F.J.2    Lin, L.R.3    Dang, L.4    Unakar, N.5    Ho, Y.S.6
  • 26
    • 0032436022 scopus 로고    scopus 로고
    • The effect of catalase amplification on immortal lens epithelial cell lines
    • Yang Y, Spector A, Ma W, Wang RR, Larsen K, Kleiman NJ. The effect of catalase amplification on immortal lens epithelial cell lines. Exp Eye Res. 1998;67:647-656.
    • (1998) Exp Eye Res. , vol.67 , pp. 647-656
    • Yang, Y.1    Spector, A.2    Ma, W.3    Wang, R.R.4    Larsen, K.5    Kleiman, N.J.6
  • 27
    • 4244195219 scopus 로고    scopus 로고
    • Characteristics of catalase transgenics controlled by a lens specific promoter
    • Abstract nr 4622
    • Ma W, Yang Y, Wang RR, Spector A. Characteristics of catalase transgenics controlled by a lens specific promoter [ARVO Abstract]. Invest Ophthalmol Vis Sci. 1999;40(4):S877. Abstract nr 4622.
    • (1999) Invest Ophthalmol Vis Sci. , vol.40 , Issue.4
    • Ma, W.1    Yang, Y.2    Wang, R.R.3    Spector, A.4
  • 30
    • 0023895652 scopus 로고
    • Influence of the activity of glutathione reductase on the response of cultured lens epithelial cells from young and old rabbits to hydrogen peroxide
    • Reddan JR, Giblin FJ, Dziedzic DC, McCready JP, Schrimscher L, Reddy VN. Influence of the activity of glutathione reductase on the response of cultured lens epithelial cells from young and old rabbits to hydrogen peroxide. Exp Eye Res. 1988;46:209-221.
    • (1988) Exp Eye Res. , vol.46 , pp. 209-221
    • Reddan, J.R.1    Giblin, F.J.2    Dziedzic, D.C.3    McCready, J.P.4    Schrimscher, L.5    Reddy, V.N.6
  • 31
    • 0020390362 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from yeast
    • Byers LD. Glyceraldehyde-3-phosphate dehydrogenase from yeast. Methods Enzymol. 1982;89:326-335.
    • (1982) Methods Enzymol. , vol.89 , pp. 326-335
    • Byers, L.D.1
  • 32
    • 0021288878 scopus 로고
    • Superoxide dismutase assay
    • Flohé L, Otting F. Superoxide dismutase assay. Methods Enzymol. 1984;105:93-104.
    • (1984) Methods Enzymol. , vol.105 , pp. 93-104
    • Flohé, L.1    Otting, F.2
  • 33
    • 0019741605 scopus 로고
    • Assays for differentiation of glutathione-S-transferase
    • Habig WH, Jakoby WB. Assays for differentiation of glutathione-S-transferase. Methods Enzymol. 1981;77:398-405.
    • (1981) Methods Enzymol. , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 35
    • 0025021892 scopus 로고
    • Hydrogen peroxide-induced DNA damage in bovine lens epithelial cells
    • Kleiman NJ, Wang RR, Spector A. Hydrogen peroxide-induced DNA damage in bovine lens epithelial cells. Mutat Res. 1990;240: 35-45.
    • (1990) Mutat Res. , vol.240 , pp. 35-45
    • Kleiman, N.J.1    Wang, R.R.2    Spector, A.3
  • 36
    • 0028317163 scopus 로고
    • SDS polyacrylamide gel electrophoresis of proteins
    • Walker JM, ed. Totowa, NJ: Humana Press
    • Smith BJ. SDS polyacrylamide gel electrophoresis of proteins. In: Walker JM, ed. Methods of Molecular Biology Vol. Basic Protein and Peptide Protocols. Vol. 32. Totowa, NJ: Humana Press; 1994: 23-34.
    • (1994) Methods of Molecular Biology Vol. Basic Protein and Peptide Protocols , vol.32 , pp. 23-34
    • Smith, B.J.1
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0028282965 scopus 로고
    • The chaperone activity of bovine α-crystallin: Interaction with other lens crystallins in native and denatured states
    • Wang K. Spector A. The chaperone activity of bovine α-crystallin: interaction with other lens crystallins in native and denatured states. J Biol Chem. 1994;269:13601-13608.
    • (1994) J Biol Chem. , vol.269 , pp. 13601-13608
    • Wang, K.1    Spector, A.2
  • 40
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel WJ, Billed TM, Stults JT, Wong SC, Grimley C, Watanabe C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci USA. 1993;90:5011-5015.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billed, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6
  • 41
    • 0027608882 scopus 로고
    • Use of mass spectrometric molecular weight information to identify proteins in sequence databases
    • Mann M, Hojrup P, Roepstorff P. Use of mass spectrometric molecular weight information to identify proteins in sequence databases. Biol Mass Spectrom. 1993;22:338-345.
    • (1993) Biol Mass Spectrom. , vol.22 , pp. 338-345
    • Mann, M.1    Hojrup, P.2    Roepstorff, P.3
  • 42
    • 0022339289 scopus 로고
    • Role of hydrogen peroxide in riboflavin-sensitized photodynamic damage to cultured rat lenses
    • Jernigan HM Jr. Role of hydrogen peroxide in riboflavin-sensitized photodynamic damage to cultured rat lenses. Exp Eye Res. 1985; 41:121-129.
    • (1985) Exp Eye Res. , vol.41 , pp. 121-129
    • Jernigan H.M., Jr.1
  • 44
    • 0030797051 scopus 로고    scopus 로고
    • Formation, prevention and repair of DNA damage by iron/hydrogen peroxide
    • Henle ES, Linn S. Formation, prevention and repair of DNA damage by iron/hydrogen peroxide. J Biol Cbem. 1997;272:19095-19098.
    • (1997) J Biol Cbem. , vol.272 , pp. 19095-19098
    • Henle, E.S.1    Linn, S.2
  • 45
    • 0020529486 scopus 로고
    • Inducible repair of oxidative damage in Escherichia coli
    • Demple B, Halbrook J. Inducible repair of oxidative damage in Escherichia coli. Nature. 1983;304:466-468.
    • (1983) Nature , vol.304 , pp. 466-468
    • Demple, B.1    Halbrook, J.2
  • 46
    • 0013664788 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat shock proteins in Salmonella typhimurium
    • Christman MF, Morgan RW, Jacobson FS, Ames BN. Positive control of a regulon for defenses against oxidative stress and some heat shock proteins in Salmonella typhimurium. Mutat Res. 1984;141:145-147.
    • (1984) Mutat Res. , vol.141 , pp. 145-147
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.N.4
  • 47
    • 0023818989 scopus 로고
    • 2-resistant variants of Chinese hamster nbroblasts demon strate increases in catalase activity
    • 2-resistant variants of Chinese hamster nbroblasts demon strate increases in catalase activity. Radic Res. 1988;114:114-124.
    • (1988) Radic Res. , vol.114 , pp. 114-124
    • Spitz, D.R.1    Li, G.C.2    McCormick, M.L.3    Sun, Y.4    Oberley, L.W.5
  • 49
    • 0029588591 scopus 로고
    • Contribution of increased glutathione content to mechanisms of oxidative stress resistance in hydrogen peroxide resistant hamster fibroblasts
    • Spitz DR, Kinter MT, Roberts RJ. Contribution of increased glutathione content to mechanisms of oxidative stress resistance in hydrogen peroxide resistant hamster fibroblasts J Cell Physiol. 1995;165:600-609.
    • (1995) J Cell Physiol. , vol.165 , pp. 600-609
    • Spitz, D.R.1    Kinter, M.T.2    Roberts, R.J.3
  • 51
    • 0028943903 scopus 로고
    • Nuclear light scattering disulfide formation and membrane damage in lenses of older guinea pigs treated with hyperbaric oxygen
    • Giblin FJ, Padgaonkar V, Leverenz VR, et al. Nuclear light scattering disulfide formation and membrane damage in lenses of older guinea pigs treated with hyperbaric oxygen. Exp Eye Res. 1995; 60:219-235.
    • (1995) Exp Eye Res. , vol.60 , pp. 219-235
    • Giblin, F.J.1    Padgaonkar, V.2    Leverenz, V.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.