메뉴 건너뛰기




Volumn 28, Issue 5, 2000, Pages 754-766

Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene

Author keywords

Free radicals; Glutathione peroxidase; Hydrogen peroxide; Knockout mice; Mitochondria; Oxidative phosphorylation; Oxidative stress

Indexed keywords

BETA GALACTOSIDASE; ENZYME ANTIBODY; GLUTATHIONE PEROXIDASE; LIPID PEROXIDE; MITOCHONDRIAL ENZYME; REACTIVE OXYGEN METABOLITE;

EID: 0034062554     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(00)00161-1     Document Type: Article
Times cited : (207)

References (49)
  • 1
    • 0032524667 scopus 로고    scopus 로고
    • Regulation of the pereability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex I
    • Fontaine E., Eriksson O., Ichas F., Bernardi P. Regulation of the pereability transition pore in skeletal muscle mitochondria. Modulation by electron flow through the respiratory chain complex I. J. Biol. Chem. 273:1998;12662-12668.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12662-12668
    • Fontaine, E.1    Eriksson, O.2    Ichas, F.3    Bernardi, P.4
  • 2
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., Sies H., Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59:1979;527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 7
    • 0032561328 scopus 로고    scopus 로고
    • Increase oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice
    • Williams M.D., VanRemmen H., Conrad C.C., Huang T.T., Epstein C.J., Richardson A. Increase oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice. J. Biol. Chem. 273:1998;28510-28515.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28510-28515
    • Williams, M.D.1    Vanremmen, H.2    Conrad, C.C.3    Huang, T.T.4    Epstein, C.J.5    Richardson, A.6
  • 8
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • (review)
    • Zoratti M., Szabo I. The mitochondrial permeability transition. Biochim. Biophys. Acta. 1241:1995;139-176. (review).
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 10
    • 0030971057 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
    • Ho Y.S., Magnenat J.L., Bronson R.T., Cao J., Gargano M., Sugawara M., Funk C.D. Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J. Biol. Chem. 272:1997;16644-16651.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16644-16651
    • Ho, Y.S.1    Magnenat, J.L.2    Bronson, R.T.3    Cao, J.4    Gargano, M.5    Sugawara, M.6    Funk, C.D.7
  • 12
    • 0033582533 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells
    • Arai M., Imai H., Koumura T., Yoshida M., Emoto K., Umeda M., Chiba N., Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells. J. Biol. Chem. 274:1999;4924-4933.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4924-4933
    • Arai, M.1    Imai, H.2    Koumura, T.3    Yoshida, M.4    Emoto, K.5    Umeda, M.6    Chiba, N.7    Nakagawa, Y.8
  • 13
    • 0028825467 scopus 로고
    • Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites
    • Pushpa-Rekha T.R., Burdsall A.L., Oleksa L.M., Chisolm G.M., Driscoll D.M. Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites. J. Biol. Chem. 270:1995;26993-26999.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26993-26999
    • Pushpa-Rekha, T.R.1    Burdsall, A.L.2    Oleksa, L.M.3    Chisolm, G.M.4    Driscoll, D.M.5
  • 14
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione peroxidase gene: The selenocysteine in the active site is encoded by the 'termination' codon, TGA
    • Chambers I., Frampton J., Goldfarb P., Affara N., McBain W., Harrison P.R. The structure of the mouse glutathione peroxidase gene the selenocysteine in the active site is encoded by the 'termination' codon, TGA. Embo. J. 5:1986;1221-1227.
    • (1986) Embo. J. , vol.5 , pp. 1221-1227
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    McBain, W.5    Harrison, P.R.6
  • 15
    • 0029007151 scopus 로고
    • Tissue non-specific alkaline phosphatase is expressed in both embryonic and extraembryonic lineages during mouse embryogenesis but is not required for migration of primordial germ cells
    • MacGregor, G. R.; Zambrowicz, B. P.; Soriano, P. Tissue non-specific alkaline phosphatase is expressed in both embryonic and extraembryonic lineages during mouse embryogenesis but is not required for migration of primordial germ cells. Development 121:1487-86; 1995.
    • (1995) Development , vol.121 , pp. 1487-1486
    • MacGregor, G.R.1    Zambrowicz, B.P.2    Soriano, P.3
  • 16
    • 0026023289 scopus 로고
    • Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice
    • Soriano P., Montgomery C., Geske R., Bradley A. Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell. 64:1991;693-702.
    • (1991) Cell , vol.64 , pp. 693-702
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4
  • 18
    • 0003396697 scopus 로고
    • P.M. Wassarman, & M.L. DePamphilis. San Diego: Academic Press
    • Stewart C.L. Wassarman P.M., DePamphilis M.L. Guide to techniques in mouse development. 1993;823-855 Academic Press, San Diego.
    • (1993) Guide to Techniques in Mouse Development , pp. 823-855
    • Stewart, C.L.1
  • 19
    • 0029964226 scopus 로고    scopus 로고
    • Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines
    • Trounce I.A., Kim Y.L., Jun A.S., Wallace D.C. Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines. Meth. Enzymol. 264:1996;484-509.
    • (1996) Meth. Enzymol. , vol.264 , pp. 484-509
    • Trounce, I.A.1    Kim, Y.L.2    Jun, A.S.3    Wallace, D.C.4
  • 21
    • 0021160336 scopus 로고
    • A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes: Its use in the simultaneous fluorimetric assay of cellular activation processes
    • Hyslop P.A., Sklar L.A. A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes its use in the simultaneous fluorimetric assay of cellular activation processes. Analytical Biochem. 141:1984;280-286.
    • (1984) Analytical Biochem. , vol.141 , pp. 280-286
    • Hyslop, P.A.1    Sklar, L.A.2
  • 22
    • 0031853099 scopus 로고    scopus 로고
    • Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria
    • Kwong L.K., Sohal R.S. Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria. Arch. Biochem. Biophys. 350:1998;118-126.
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 118-126
    • Kwong, L.K.1    Sohal, R.S.2
  • 23
    • 0023658649 scopus 로고
    • Mitochondrial membrane potential estimated with the correction of probe binding
    • Demura M., Kamo N., Kobatake Y. Mitochondrial membrane potential estimated with the correction of probe binding. Biochim. Biophys. Acta. 894:1987;355-364.
    • (1987) Biochim. Biophys. Acta , vol.894 , pp. 355-364
    • Demura, M.1    Kamo, N.2    Kobatake, Y.3
  • 24
    • 0018665167 scopus 로고
    • Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state
    • Kamo N., Muratsugu M., Hongoh R., Kobatake Y. Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state. J. Membr. Biol. 49:1979;105-121.
    • (1979) J. Membr. Biol. , vol.49 , pp. 105-121
    • Kamo, N.1    Muratsugu, M.2    Hongoh, R.3    Kobatake, Y.4
  • 25
    • 0021207554 scopus 로고
    • Membrane potential and surface potential in mitochondria: Uptake and binding of lipophilic cations
    • Rottenberg H. Membrane potential and surface potential in mitochondria Uptake and binding of lipophilic cations. J. Membr. Biol. 81:1984;127-138.
    • (1984) J. Membr. Biol. , vol.81 , pp. 127-138
    • Rottenberg, H.1
  • 26
    • 0022829380 scopus 로고
    • Kinetic control of mitochondrial ATP synthesis
    • LaNoue K.F., Jeffries F.M., Radda G.K. Kinetic control of mitochondrial ATP synthesis. Biochemistry. 25:1986;7667-7675.
    • (1986) Biochemistry , vol.25 , pp. 7667-7675
    • Lanoue, K.F.1    Jeffries, F.M.2    Radda, G.K.3
  • 27
    • 0025992469 scopus 로고
    • Promoter traps in embryonic stem cells: A genetic screen to identify and mutate developmental genes in mice
    • Friedrich G., Soriano P. Promoter traps in embryonic stem cells a genetic screen to identify and mutate developmental genes in mice. Genes Dev. 5:1991;1513-1523.
    • (1991) Genes Dev. , vol.5 , pp. 1513-1523
    • Friedrich, G.1    Soriano, P.2
  • 28
    • 0028205403 scopus 로고
    • Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria
    • Godeas C., Sandri G., Panfili E. Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria. Biochim. Biophys. Acta. 1191:1994;147-150.
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 147-150
    • Godeas, C.1    Sandri, G.2    Panfili, E.3
  • 29
  • 30
    • 0031879339 scopus 로고    scopus 로고
    • Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine
    • Esworthy R.S., Swiderek K.M., Ho Y.S., Chu F.F. Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine. Biochim. Biophys. Acta. 1381:1998;213-226.
    • (1998) Biochim. Biophys. Acta , vol.1381 , pp. 213-226
    • Esworthy, R.S.1    Swiderek, K.M.2    Ho, Y.S.3    Chu, F.F.4
  • 31
    • 0031029962 scopus 로고    scopus 로고
    • In vivo control of respiration by cytochrome c oxidase in wild-type and mitochondrial DNA mutation-carrying human cells
    • Villani G., Attardi G. In vivo control of respiration by cytochrome c oxidase in wild-type and mitochondrial DNA mutation-carrying human cells. Proc. Natl. Acad. Sci. USA. 94:1997;1166-1171.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1166-1171
    • Villani, G.1    Attardi, G.2
  • 32
    • 0028874588 scopus 로고
    • Functional analysis of subunits III and IV of Bacillus subtilis aa3-600 quinol oxidase by in vitro mutagenesis and gene replacement
    • Villani G., Tattoli M., Capitanio N., Glaser P., Papa S., Danchin A. Functional analysis of subunits III and IV of Bacillus subtilis aa3-600 quinol oxidase by in vitro mutagenesis and gene replacement. Biochim. Biophys. Acta. 1232:1995;67-74.
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 67-74
    • Villani, G.1    Tattoli, M.2    Capitanio, N.3    Glaser, P.4    Papa, S.5    Danchin, A.6
  • 33
    • 0030038762 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore is modulated by oxidative agents through both pyridine nucleotides and glutathione at two separate sites
    • Chernyak B.V., Bernardi P. The mitochondrial permeability transition pore is modulated by oxidative agents through both pyridine nucleotides and glutathione at two separate sites. Eur. J. Biochem. 238:1996;623-630.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 623-630
    • Chernyak, B.V.1    Bernardi, P.2
  • 34
    • 0028075423 scopus 로고
    • Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel
    • Connern C.P., Halestrap A.P. Recruitment of mitochondrial cyclophilin to the mitochondrial inner membrane under conditions of oxidative stress that enhance the opening of a calcium-sensitive non-specific channel. Biochem. J. 302:1994;321-324.
    • (1994) Biochem. J. , vol.302 , pp. 321-324
    • Connern, C.P.1    Halestrap, A.P.2
  • 35
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • Halestrap A.P., Woodfield K.Y., Connern C.P. Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. J. Biol. Chem. 272:1997;3346-3354.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 38
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial disease in mouse and man
    • Wallace D.C. Mitochondrial disease in mouse and man. Science. 283:1999;1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 39
    • 0025769968 scopus 로고
    • Immunohistochemical localization of glutathione-S-transferase and glutathione peroxidase in adult Syrian hamster tissues and during kidney development
    • Oberley T.D., Oberley L.W., Slattery A.F., Elwell J.H. Immunohistochemical localization of glutathione-S-transferase and glutathione peroxidase in adult Syrian hamster tissues and during kidney development. Am. J. Pathol. 139:1991;355-369.
    • (1991) Am. J. Pathol. , vol.139 , pp. 355-369
    • Oberley, T.D.1    Oberley, L.W.2    Slattery, A.F.3    Elwell, J.H.4
  • 40
    • 0030572752 scopus 로고    scopus 로고
    • Immunocytochemical localization of seleno-glutathione peroxidase in the adult mouse brain
    • Trepanier G., Furling D., Puymirat J., Mirault M.E. Immunocytochemical localization of seleno-glutathione peroxidase in the adult mouse brain. Neuroscience. 75:1996;231-243.
    • (1996) Neuroscience , vol.75 , pp. 231-243
    • Trepanier, G.1    Furling, D.2    Puymirat, J.3    Mirault, M.E.4
  • 41
    • 0031879339 scopus 로고    scopus 로고
    • Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine
    • Esworthy R.S., Swiderek K.M., Ho Y.S., Chu F.F. Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine. Biochim. Biophys. Acta. 1381:1998;213-226.
    • (1998) Biochim. Biophys. Acta , vol.1381 , pp. 213-226
    • Esworthy, R.S.1    Swiderek, K.M.2    Ho, Y.S.3    Chu, F.F.4
  • 42
    • 0027993038 scopus 로고
    • Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion
    • Maser R.L., Magenheimer B.S., Calvet J.P. Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion. J. Biol. Chem. 269:1994;27066-27073.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27066-27073
    • Maser, R.L.1    Magenheimer, B.S.2    Calvet, J.P.3
  • 44
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha
    • Kang S.W., Chae H.Z., Seo M.S., Kim K., Baines I.C., Rhee S.G. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J. Biol. Chem. 273:1998;6297-6302.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6297-6302
    • Kang, S.W.1    Chae, H.Z.2    Seo, M.S.3    Kim, K.4    Baines, I.C.5    Rhee, S.G.6
  • 45
    • 0029863399 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites
    • Costantini P., Chernyak B.V., Petronilli V., Bernardi P. Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J. Biol. Chem. 271:1996;6746-6751.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6746-6751
    • Costantini, P.1    Chernyak, B.V.2    Petronilli, V.3    Bernardi, P.4
  • 46
    • 0028342438 scopus 로고
    • Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse
    • Sohal R.S., Ku H.-H., Agarwal S., Forster M.J., Lal H. Oxidative damage, mitochondrial oxidant generation and antioxidant defenses during aging and in response to food restriction in the mouse. Mech. Aging Dev. 74:1994;21-133.
    • (1994) Mech. Aging Dev. , vol.74 , pp. 21-133
    • Sohal, R.S.1    Ku, H.-H.2    Agarwal, S.3    Forster, M.J.4    Lal, H.5
  • 47
    • 0345596416 scopus 로고    scopus 로고
    • Alterations of antioxidant enzymes and oxidative damage to macromolecules in different organs of rats during aging
    • Tian L., Cai Q., Wei H. Alterations of antioxidant enzymes and oxidative damage to macromolecules in different organs of rats during aging. Free Radic. Biol. Med. 24:1998;1477-1484.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 1477-1484
    • Tian, L.1    Cai, Q.2    Wei, H.3
  • 48
    • 0029076728 scopus 로고
    • Changes in the levels of enzymes which modulate the antioxidant balance occur during aging and correlate with cellular damage
    • Cristiano F., de Haan J.B., Ianello R.C., Kola I. Changes in the levels of enzymes which modulate the antioxidant balance occur during aging and correlate with cellular damage. Mech. Aging Dev. 80:1995;93-105.
    • (1995) Mech. Aging Dev. , vol.80 , pp. 93-105
    • Cristiano, F.1    De Haan, J.B.2    Ianello, R.C.3    Kola, I.4
  • 49
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • (review)
    • Beckman K.B., Ames B.N. The free radical theory of aging matures. Physiol. Rev. 78:1998;547-581. (review).
    • (1998) Physiol. Rev. , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.