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Volumn 315, Issue 1, 2014, Pages 55-64

Excessive hydrogen peroxide enhances the attachment of amyloid β1-42 in the lens epithelium of UPL rats, a hereditary model for cataracts

Author keywords

Amyloid ; Hydrogen peroxide; Lens; Lipid peroxide; UPL rat

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; DSF EYE DROP; EYE DROPS; GAMMA SECRETASE; HYDROGEN PEROXIDE; LIPID PEROXIDE; MESSENGER RNA; UNCLASSIFIED DRUG;

EID: 84890277301     PISSN: 0300483X     EISSN: 18793185     Source Type: Journal    
DOI: 10.1016/j.tox.2013.08.003     Document Type: Article
Times cited : (19)

References (56)
  • 1
    • 1642499152 scopus 로고    scopus 로고
    • Beta-amyloid peptides induce mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase
    • Abramov A.Y., Canevari L., Duchen M.R. Beta-amyloid peptides induce mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADPH oxidase. J. Neurosci. 2004, 24:565-575.
    • (2004) J. Neurosci. , vol.24 , pp. 565-575
    • Abramov, A.Y.1    Canevari, L.2    Duchen, M.R.3
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0036272650 scopus 로고    scopus 로고
    • Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley C.S., Canevari L., Land J.M., Clark J.B., Sharpe M.A. Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J. Neurochem. 2002, 80:91-100.
    • (2002) J. Neurochem. , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 7
    • 0031891785 scopus 로고    scopus 로고
    • Lenticular calcium, magnesium, and iron levels in diabetic rats and verapamil effect
    • Cekic O., Bardak Y. Lenticular calcium, magnesium, and iron levels in diabetic rats and verapamil effect. Ophthalmic Res. 1998, 30:107-112.
    • (1998) Ophthalmic Res. , vol.30 , pp. 107-112
    • Cekic, O.1    Bardak, Y.2
  • 8
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 1987, 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 9
    • 0034490572 scopus 로고    scopus 로고
    • Determination of calcium, sodium, potassium and magnesium concentrations in human senile cataractous lenses
    • Dilsiz N., Olcucu A., Atas M. Determination of calcium, sodium, potassium and magnesium concentrations in human senile cataractous lenses. Cell Biochem. Funct. 2000, 18:259-262.
    • (2000) Cell Biochem. Funct. , vol.18 , pp. 259-262
    • Dilsiz, N.1    Olcucu, A.2    Atas, M.3
  • 10
    • 0016743458 scopus 로고
    • Ion analyses of human cataractous lenses
    • Duncan G., Bushell A.R. Ion analyses of human cataractous lenses. Exp. Eye Res. 1975, 20:223-230.
    • (1975) Exp. Eye Res. , vol.20 , pp. 223-230
    • Duncan, G.1    Bushell, A.R.2
  • 12
    • 0025365741 scopus 로고
    • Role of site-specific, metal-catalyzed oxidation in lens aging and cataract: a hypothesis
    • Garland D. Role of site-specific, metal-catalyzed oxidation in lens aging and cataract: a hypothesis. Exp. Eye Res. 1990, 50:677-682.
    • (1990) Exp. Eye Res. , vol.50 , pp. 677-682
    • Garland, D.1
  • 14
    • 33747488423 scopus 로고    scopus 로고
    • Elevated neprilysin activity in vitreous of patients with proliferative diabetic retinopathy
    • Hara H., Oh-hashi K., Yoneda S., Shimazawa M., Inatani M., Tanihara H., Kiuchi K. Elevated neprilysin activity in vitreous of patients with proliferative diabetic retinopathy. Mol. Vis. 2006, 12:977-982.
    • (2006) Mol. Vis. , vol.12 , pp. 977-982
    • Hara, H.1    Oh-hashi, K.2    Yoneda, S.3    Shimazawa, M.4    Inatani, M.5    Tanihara, H.6    Kiuchi, K.7
  • 15
    • 84869217915 scopus 로고    scopus 로고
    • Induction of amyloid-β (1-42) in the retina and optic nerve head of chronic ocular hypertensive monkeys
    • Ito Y., Shimazawa M., Tsuruma K., Mayama C., Ishii K., Onoe H., Aihara M., Araie M., Hara H. Induction of amyloid-β (1-42) in the retina and optic nerve head of chronic ocular hypertensive monkeys. Mol. Vis. 2012, 18:2647-2657.
    • (2012) Mol. Vis. , vol.18 , pp. 2647-2657
    • Ito, Y.1    Shimazawa, M.2    Tsuruma, K.3    Mayama, C.4    Ishii, K.5    Onoe, H.6    Aihara, M.7    Araie, M.8    Hara, H.9
  • 16
    • 33749439072 scopus 로고
    • Medical-Aoi Publication Press, Tokyo, Japan, (Suishotai, in Japanese), S. Iwata (Ed.)
    • Iwata S. Crystalline Lens 1986, 355-360. Medical-Aoi Publication Press, Tokyo, Japan, (Suishotai, in Japanese). S. Iwata (Ed.).
    • (1986) Crystalline Lens , pp. 355-360
    • Iwata, S.1
  • 17
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie
    • Jarret J.T., Lansbury P.T. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie. Cell 1993, 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarret, J.T.1    Lansbury, P.T.2
  • 18
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • Jarret J.T., Berger E.P., Lansbury P.T. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarret, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 20
    • 0037013327 scopus 로고    scopus 로고
    • Intracellular amyloid-beta 1-42, but not extracellular soluble amyloid-beta peptides, induces neuronal apoptosis
    • Kienlen C.P., Miolet S., Tasiaux B., Octave J.N. Intracellular amyloid-beta 1-42, but not extracellular soluble amyloid-beta peptides, induces neuronal apoptosis. J. Biol. Chem. 2002, 277:15666-15670.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15666-15670
    • Kienlen, C.P.1    Miolet, S.2    Tasiaux, B.3    Octave, J.N.4
  • 22
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • Lorenzo A., Yankner B.A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:12243-12247.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 24
    • 0028173205 scopus 로고
    • Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments
    • Ma J., Yee A., Brewer H.B., Das S., Potter H. Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 1994, 372:92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer, H.B.3    Das, S.4    Potter, H.5
  • 25
    • 85056043014 scopus 로고    scopus 로고
    • The effect of hydrogen peroxide on sarco/endoplasmic and plasma membrane calcium ATPase gene expression in cultured human lens epithelial cells
    • Marian M.J., Mukhopadhyay P., Borchman D., Tang D., Paterson C.A. The effect of hydrogen peroxide on sarco/endoplasmic and plasma membrane calcium ATPase gene expression in cultured human lens epithelial cells. Open Ophthalmol. J. 2008, 2:123-129.
    • (2008) Open Ophthalmol. J. , vol.2 , pp. 123-129
    • Marian, M.J.1    Mukhopadhyay, P.2    Borchman, D.3    Tang, D.4    Paterson, C.A.5
  • 26
    • 0942276377 scopus 로고    scopus 로고
    • Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation
    • Meehan S., Berry Y., Luisi B., Dobson C.M., Carver J.A., MacPhee C.E. Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation. J. Biol. Chem. 2004, 279:3413-3419.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3413-3419
    • Meehan, S.1    Berry, Y.2    Luisi, B.3    Dobson, C.M.4    Carver, J.A.5    MacPhee, C.E.6
  • 27
    • 10844277858 scopus 로고    scopus 로고
    • Mice transgenic for Alzheimer disease beta-amyloid develop lens cataracts that are rescued by antioxidant treatment
    • Melov S., Wolf N., Strozyk D., Doctrow S.R., Bush A.I. Mice transgenic for Alzheimer disease beta-amyloid develop lens cataracts that are rescued by antioxidant treatment. Free Radic. Biol. Med. 2005, 38:258-561.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 258-561
    • Melov, S.1    Wolf, N.2    Strozyk, D.3    Doctrow, S.R.4    Bush, A.I.5
  • 30
    • 0037331807 scopus 로고    scopus 로고
    • Delay of cataract development in hereditary cataract UPL rats by disulfiram and aminoguanidine
    • Nabekura T., Koizumi Y., Nakao M., Tomohiro M., Inomata M., Ito Y. Delay of cataract development in hereditary cataract UPL rats by disulfiram and aminoguanidine. Exp. Eye Res. 2003, 76:169-174.
    • (2003) Exp. Eye Res. , vol.76 , pp. 169-174
    • Nabekura, T.1    Koizumi, Y.2    Nakao, M.3    Tomohiro, M.4    Inomata, M.5    Ito, Y.6
  • 31
    • 36049001151 scopus 로고    scopus 로고
    • Adverse effects of excessive nitric oxide on cytochrome c oxidase in lenses of hereditary cataract UPL rats
    • Nagai N., Ito Y. Adverse effects of excessive nitric oxide on cytochrome c oxidase in lenses of hereditary cataract UPL rats. Toxicology 2007, 242:7-15.
    • (2007) Toxicology , vol.242 , pp. 7-15
    • Nagai, N.1    Ito, Y.2
  • 32
    • 44349108345 scopus 로고    scopus 로고
    • Effect of disulfiram eye drops on lipid peroxide formation via excessive nitric oxide in lenses of hereditary cataract ICR/f rats
    • Nagai N., Ito Y., Takeuchi N. Effect of disulfiram eye drops on lipid peroxide formation via excessive nitric oxide in lenses of hereditary cataract ICR/f rats. Biol. Pharm. Bull. 2008, 31:981-985.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 981-985
    • Nagai, N.1    Ito, Y.2    Takeuchi, N.3
  • 33
    • 77950131689 scopus 로고    scopus 로고
    • Oxidative stress up-regulates presenilin 1 in lipid rafts in neuronal cells
    • Oda A., Tamaoka A., Araki W. Oxidative stress up-regulates presenilin 1 in lipid rafts in neuronal cells. J. Neurosci. Res. 2010, 88:1137-1145.
    • (2010) J. Neurosci. Res. , vol.88 , pp. 1137-1145
    • Oda, A.1    Tamaoka, A.2    Araki, W.3
  • 34
    • 0034996104 scopus 로고    scopus 로고
    • Mitochondrial function and Alzheimer's disease
    • Ojaimi J., Byrne E. Mitochondrial function and Alzheimer's disease. Biol. Signals Recept. 2001, 10:254-262.
    • (2001) Biol. Signals Recept. , vol.10 , pp. 254-262
    • Ojaimi, J.1    Byrne, E.2
  • 35
    • 0034745636 scopus 로고    scopus 로고
    • Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro
    • Parks J.K., Smith T.S., Trimmer P.A., Bennett J.P., Parker W.D. Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro. J. Neurochem. 2001, 76:1050-1056.
    • (2001) J. Neurochem. , vol.76 , pp. 1050-1056
    • Parks, J.K.1    Smith, T.S.2    Trimmer, P.A.3    Bennett, J.P.4    Parker, W.D.5
  • 37
    • 33644845279 scopus 로고    scopus 로고
    • Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease
    • Reddy P.H. Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease. J. Neurochem. 2006, 96:1-13.
    • (2006) J. Neurochem. , vol.96 , pp. 1-13
    • Reddy, P.H.1
  • 39
    • 33744906410 scopus 로고
    • Experimental studies on early lens changes after roentgen irradiation. II. Exchange and penetration of radioactive indicators (Na24, K42, I131, P32) in normal and irradiated lenses of rabbits
    • Sallman L.V., Locke B.D. Experimental studies on early lens changes after roentgen irradiation. II. Exchange and penetration of radioactive indicators (Na24, K42, I131, P32) in normal and irradiated lenses of rabbits. A.M.A. Arch. Ophthalmol. 1951, 45:431-444.
    • (1951) A.M.A. Arch. Ophthalmol. , vol.45 , pp. 431-444
    • Sallman, L.V.1    Locke, B.D.2
  • 41
    • 47749147258 scopus 로고    scopus 로고
    • Hydrogen peroxide promotes Abeta production through JNK-dependent activation of gamma-secretase
    • Shen C., Chen Y., Liu H., Zhang K., Zhang T., Lin A., Jing N. Hydrogen peroxide promotes Abeta production through JNK-dependent activation of gamma-secretase. J. Biol. Chem. 2008, 283:17721-17730.
    • (2008) J. Biol. Chem. , vol.283 , pp. 17721-17730
    • Shen, C.1    Chen, Y.2    Liu, H.3    Zhang, K.4    Zhang, T.5    Lin, A.6    Jing, N.7
  • 44
    • 17144425021 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, endoplasmic reticulum stress, and apoptosis in Alzheimer's disease
    • Takuma K., Yan S.S., Stern D.M., Yamada K. Mitochondrial dysfunction, endoplasmic reticulum stress, and apoptosis in Alzheimer's disease. J. Pharm. Sci. 2005, 97:312-326.
    • (2005) J. Pharm. Sci. , vol.97 , pp. 312-326
    • Takuma, K.1    Yan, S.S.2    Stern, D.M.3    Yamada, K.4
  • 49
    • 0030837684 scopus 로고    scopus 로고
    • Immunohistochemical study of calpain-mediated alpha-crystallin proteolysis in the UPL rat hereditary cataract
    • Tomohiro M., Aida Y., Inomata M., Ito Y., Mizuno A., Sakuma S. Immunohistochemical study of calpain-mediated alpha-crystallin proteolysis in the UPL rat hereditary cataract. Jpn. J. Ophthalmol. 1997, 41:121-129.
    • (1997) Jpn. J. Ophthalmol. , vol.41 , pp. 121-129
    • Tomohiro, M.1    Aida, Y.2    Inomata, M.3    Ito, Y.4    Mizuno, A.5    Sakuma, S.6
  • 52
    • 57649225077 scopus 로고    scopus 로고
    • Translational control of BACE1 may go awry in Alzheimer's disease
    • Wong P.C. Translational control of BACE1 may go awry in Alzheimer's disease. Neuron 2008, 60:941-943.
    • (2008) Neuron , vol.60 , pp. 941-943
    • Wong, P.C.1
  • 53
    • 0026616976 scopus 로고
    • + exchange mechanism in vesicles isolated from apical membranes of lens epithelium of spiny dogfish (Squalus acanthias) and bovine eye
    • + exchange mechanism in vesicles isolated from apical membranes of lens epithelium of spiny dogfish (Squalus acanthias) and bovine eye. Exp. Eye Res. 1992, 55:243-250.
    • (1992) Exp. Eye Res. , vol.55 , pp. 243-250
    • Ye, J.1    Zadunaisky, J.A.2
  • 54
    • 0037112194 scopus 로고    scopus 로고
    • Amyloid-beta induces Smac release via AP-1/Bim activation in cerebral endothelial cells
    • Yin K.J., Lee J.M., Chen S.D., Xu J., Hsu C.Y. Amyloid-beta induces Smac release via AP-1/Bim activation in cerebral endothelial cells. J. Neurosci. 2002, 22:9764-9770.
    • (2002) J. Neurosci. , vol.22 , pp. 9764-9770
    • Yin, K.J.1    Lee, J.M.2    Chen, S.D.3    Xu, J.4    Hsu, C.Y.5
  • 55
    • 0037017399 scopus 로고    scopus 로고
    • Selective cytotoxicity of intracellular amyloid beta peptide1-42 through p53 and Bax in cultured primary human
    • Zhang Y., McLaughlin R., Goodyer C., LeBlanc A. Selective cytotoxicity of intracellular amyloid beta peptide1-42 through p53 and Bax in cultured primary human. J. Cell Biol. 2002, 156:519-529.
    • (2002) J. Cell Biol. , vol.156 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    LeBlanc, A.4
  • 56
    • 33847724188 scopus 로고    scopus 로고
    • The amyloid precursor protein: beyond amyloid
    • Zheng H., Koo E.H. The amyloid precursor protein: beyond amyloid. Mol. Neurodegener. 2006, 3:1-5.
    • (2006) Mol. Neurodegener. , vol.3 , pp. 1-5
    • Zheng, H.1    Koo, E.H.2


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