메뉴 건너뛰기




Volumn 270, Issue 21, 2003, Pages 4326-4331

A selenium-containing single-chain abzyme with potent antioxidant activity

Author keywords

Antioxidant activity; Glutathione peroxidase; Mitochondria; scFv; Selenium

Indexed keywords

ABZYME 2F3; ANTIOXIDANT; ASCORBIC ACID; CYTOCHROME C OXIDASE; EBSELEN; FERROUS SULFATE; GLUTATHIONE PEROXIDASE; REACTIVE OXYGEN METABOLITE; SELENIUM DERIVATIVE; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG;

EID: 0242362598     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03825.x     Document Type: Article
Times cited : (13)

References (46)
  • 1
    • 0029439509 scopus 로고
    • Oxidative stress: The paradox of aerobic life
    • Davies, K.J. (1995) Oxidative stress: the paradox of aerobic life. Biochem. Soc. Symp. 61, 1-31.
    • (1995) Biochem. Soc. Symp. , vol.61 , pp. 1-31
    • Davies, K.J.1
  • 2
    • 0018263443 scopus 로고
    • The biology of oxygen radicals
    • Fridovich, I. (1978) The biology of oxygen radicals. Science 201, 875-880.
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 5
    • 0029151027 scopus 로고
    • Oxidative stress-induced cataract: Mechanism of action
    • Spector, A. (1995) Oxidative stress-induced cataract: mechanism of action. FASEB J. 9, 1173-1182.
    • (1995) FASEB J. , vol.9 , pp. 1173-1182
    • Spector, A.1
  • 6
    • 0028170326 scopus 로고
    • Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress
    • Michiels, C., Raes, M., Toussaaint, O. & Remacle, J. (1994) Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic. Biol. Med. 17, 235-248.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaaint, O.3    Remacle, J.4
  • 7
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobinfrom oxidase breakdown
    • Mills, G.C. (1957) Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobinfrom oxidase breakdown. J. Biol. Chem. 229, 189-195.
    • (1957) J. Biol. Chem. , vol.229 , pp. 189-195
    • Mills, G.C.1
  • 9
    • 0015880169 scopus 로고
    • Glutathione peroxidase: A selenoenzyme
    • Flohé, L., Genzler, W.A. & Schock, H.H. (1973) Glutathione peroxidase: a selenoenzyme. FEBS Lett. 32, 132-134.
    • (1973) FEBS Lett. , vol.32 , pp. 132-134
    • Flohé, L.1    Genzler, W.A.2    Schock, H.H.3
  • 10
    • 0028088668 scopus 로고
    • Purification and characterization of phospholipid hydroperoxide glutathione peroxidase from rat testis mitochondrial membranes
    • Roveri, A., Maiorino, M., Nissii, C. & Ursini, F. (1994) Purification and characterization of phospholipid hydroperoxide glutathione peroxidase from rat testis mitochondrial membranes. Biochim. Biophys. Acta 1208, 211-221.
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 211-221
    • Roveri, A.1    Maiorino, M.2    Nissii, C.3    Ursini, F.4
  • 11
    • 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. (1995) Rat phospholipid-hydroperoxide glutathione peroxidase. cDNA cloning and identification of multiple transcription and translation start sites. J. Biol. Chem. 270, 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
  • 12
    • 0025060737 scopus 로고
    • Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation. In situ reduction of phospholipid and cholesterol hydroperoxides
    • Thomas, J.P., Maiorina, M., Ursini, F. & Girotti, A.W. (1990) Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation. In situ reduction of phospholipid and cholesterol hydroperoxides. J. Biol. Chem. 265, 454-461.
    • (1990) J. Biol. Chem. , vol.265 , pp. 454-461
    • Thomas, J.P.1    Maiorina, M.2    Ursini, F.3    Girotti, A.W.4
  • 13
    • 0025024349 scopus 로고
    • A human cDNa sequence of a novel glutathione peroxidase-related protein
    • Akasaka, M., Mizoguchi, J. & Takahashi, K. (1990) A human cDNA sequence of a novel glutathione peroxidase-related protein. Nucleic Acids Res. 18, 4619-4621.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4619-4621
    • Akasaka, M.1    Mizoguchi, J.2    Takahashi, K.3
  • 14
    • 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. (1998) Selenium-dependent glutathione peroxidase-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine. Biochim. Biophys. Acta 1381, 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
  • 15
    • 0023186348 scopus 로고
    • Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzyme
    • Takahashi, K., Avissar, N., Whitin, J. & Cohen, H. (1987) Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme. Arch. Biochem. Biophys. 256, 677-686.
    • (1987) Arch. Biochem. Biophys. , vol.256 , pp. 677-686
    • Takahashi, K.1    Avissar, N.2    Whitin, J.3    Cohen, H.4
  • 16
    • 0027246660 scopus 로고
    • Glutathione peroxidase isolated plasma reduces phospholipid hydroperoxides
    • Yamamato, Y. & Takahashi, K. (1993) Glutathione peroxidase isolated plasma reduces phospholipid hydroperoxides. Arch. Biochem. Biophys. 305, 541-545.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 541-545
    • Yamamato, Y.1    Takahashi, K.2
  • 17
    • 14444271790 scopus 로고    scopus 로고
    • Mice with a homozygous null mutation for the most abundant glutathione peroxidase, GPX1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide
    • De Haan, J., Bladier, C., Griffiths, P., Kelner, M., O'Shea, R.P., Cheung, N.S., Bronson, R.T., Silvestro, M.J., Wild, S., Zheng, S.S., Beart, P.M., Herzog, P.J. & Kola, I. (1998) Mice with a homozygous null mutation for the most abundant glutathione peroxidase, GPX1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide. J. Biol. Chem. 273, 22528-22536.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22528-22536
    • De Haan, J.1    Bladier, C.2    Griffiths, P.3    Kelner, M.4    O'Shea, R.P.5    Cheung, N.S.6    Bronson, R.T.7    Silvestro, M.J.8    Wild, S.9    Zheng, S.S.10    Beart, P.M.11    Herzog, P.J.12    Kola, I.13
  • 18
    • 0035819585 scopus 로고    scopus 로고
    • Glutathione peroxidase-like antioxidant activity of diaryl diselenides: A mechanistic study
    • Mugesh, G., Panda, A., Singh, H.B., Punekar, N.S. & Butcher, R.J. (2001) Glutathione peroxidase-like antioxidant activity of diaryl diselenides: a mechanistic study. J. Am. Chem. Soc. 123, 839-850.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 839-850
    • Mugesh, G.1    Panda, A.2    Singh, H.B.3    Punekar, N.S.4    Butcher, R.J.5
  • 19
    • 0035312554 scopus 로고    scopus 로고
    • Structure-activity correlation between natural glutathione peroxidase (GPx) and mimics: A biomimetic concept for the design and synthesis of more efficient GPx mimics
    • Mugesh, G. & du Mont, W.W. (2001) Structure-activity correlation between natural glutathione peroxidase (GPx) and mimics: a biomimetic concept for the design and synthesis of more efficient GPx mimics. Chemistry 7, 1365-1370.
    • (2001) Chemistry , vol.7 , pp. 1365-1370
    • Mugesh, G.1    Du Mont, W.W.2
  • 20
    • 0035385139 scopus 로고    scopus 로고
    • Chemistry of biologically important synthetic organoselenium compounds
    • Mugesh, G., du Mont, W.W. & Sies, H. (2001) Chemistry of biologically important synthetic organoselenium compounds. Chem. Rev. 101, 2125-2179.
    • (2001) Chem. Rev. , vol.101 , pp. 2125-2179
    • Mugesh, G.1    Du Mont, W.W.2    Sies, H.3
  • 21
    • 0027533505 scopus 로고
    • Ebselen, a selenoorganic compound as glutathione peroxidase mimic
    • Sies, H. (1993) Ebselen, a selenoorganic compound as glutathione peroxidase mimic. Free Radic. Biol. Med. 14, 313-323.
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 313-323
    • Sies, H.1
  • 22
    • 0028130551 scopus 로고
    • Ebselen: A glutathione peroxidase mimic
    • Sies, H. (1994) Ebselen: a glutathione peroxidase mimic. Methods Enzymol. 234, 476-482.
    • (1994) Methods Enzymol. , vol.234 , pp. 476-482
    • Sies, H.1
  • 23
    • 0011869643 scopus 로고    scopus 로고
    • Ebselen as a glutathione peroxidase mimic and as a scavenger of peroxynitrite
    • Sies, H. (1997) Ebselen as a glutathione peroxidase mimic and as a scavenger of peroxynitrite. Adv. Pharmacol. 38, 229-246.
    • (1997) Adv. Pharmacol. , vol.38 , pp. 229-246
    • Sies, H.1
  • 24
    • 0034656845 scopus 로고    scopus 로고
    • Interaction of peroxynitrite with selenoproteins and glutathione peroxidase mimics
    • Sies, H. & Arteel, G.E. (2000) Interaction of peroxynitrite with selenoproteins and glutathione peroxidase mimics. Free Radic. Biol. Med. 28, 1451-1455.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1451-1455
    • Sies, H.1    Arteel, G.E.2
  • 26
    • 0032524263 scopus 로고    scopus 로고
    • Biochemical characterization of selenium-containing catalytic antibody as a cytosolic glutathione peroxidase mimic
    • Ding, L., Liu, Z., Zhu, Z.Q., Luo, G.M., Zhao, D.Q. & Ni, J.Z. (1998) Biochemical characterization of selenium-containing catalytic antibody as a cytosolic glutathione peroxidase mimic. Biochem. J. 332, 251-255.
    • (1998) Biochem. J. , vol.332 , pp. 251-255
    • Ding, L.1    Liu, Z.2    Zhu, Z.Q.3    Luo, G.M.4    Zhao, D.Q.5    Ni, J.Z.6
  • 28
    • 0035886938 scopus 로고    scopus 로고
    • Cloning and expressing of a single-chain catalytic antibody that acts as a glutathione peroxidase mimic with high catalytic efficiency
    • Ren, X.J., Gao, S.J., You, D.L., Huang, H.L., Liu, Z., Mu, Y., Liu, J.Q., Zhang, Y., Yang, G.L., Lou, G.M., Yang, T.S. & Shen, J.C. (2001) Cloning and expressing of a single-chain catalytic antibody that acts as a glutathione peroxidase mimic with high catalytic efficiency. Biochem. J. 359, 369-374.
    • (2001) Biochem. J. , vol.359 , pp. 369-374
    • Ren, X.J.1    Gao, S.J.2    You, D.L.3    Huang, H.L.4    Liu, Z.5    Mu, Y.6    Liu, J.Q.7    Zhang, Y.8    Yang, G.L.9    Lou, G.M.10    Yang, T.S.11    Shen, J.C.12
  • 29
    • 0034816070 scopus 로고    scopus 로고
    • Kinetics study of a selenium containing scFv catalytic antibody that mimics glutathione peroxidase
    • Su, D., You, D.L., Ren, X.J., Luo, G.M., Mu, Y., Yan, G.L., Xue, Y. & Shen, J.C. (2001) Kinetics study of a selenium containing scFv catalytic antibody that mimics glutathione peroxidase. Biochem. Biophys. Res. Commun. 285, 702-707.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 702-707
    • Su, D.1    You, D.L.2    Ren, X.J.3    Luo, G.M.4    Mu, Y.5    Yan, G.L.6    Xue, Y.7    Shen, J.C.8
  • 30
    • 0019373459 scopus 로고
    • The use of restriction endonucleases to measure mitochondrial DNA sequence relatedness in natural populations. III. Techniques and potential applications
    • Lansman, R.A., Shade, R.O., Shapiro, J.F. & Avise, J.C. (1981) The use of restriction endonucleases to measure mitochondrial DNA sequence relatedness in natural populations. III. Techniques and potential applications. J. Mol. Evol. 17, 214-226.
    • (1981) J. Mol. Evol. , vol.17 , pp. 214-226
    • Lansman, R.A.1    Shade, R.O.2    Shapiro, J.F.3    Avise, J.C.4
  • 31
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0017070586 scopus 로고
    • Autoxidation of polyunsaturated fatty acids. II. A suggested mechanism for the formation of TBA-reactive materials from prostaglandin-like endoperoxides
    • Pryor, W.A., Stanley, J.P. & Blair, E. (1976) Autoxidation of polyunsaturated fatty acids. II. A suggested mechanism for the formation of TBA-reactive materials from prostaglandin-like endoperoxides. Lipids 11, 370-379.
    • (1976) Lipids , vol.11 , pp. 370-379
    • Pryor, W.A.1    Stanley, J.P.2    Blair, E.3
  • 35
    • 0013816680 scopus 로고
    • Studies on cytochrome c peroxidase. I. Purification and some properties
    • Yonetani, T. & Ray, G.S. (1965) Studies on cytochrome c peroxidase. I. Purification and some properties. J. Biol. Chem. 240, 4503-4508.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4503-4508
    • Yonetani, T.1    Ray, G.S.2
  • 37
    • 0032704101 scopus 로고    scopus 로고
    • Antioxidants, oxidative stress, and degenerative neurological disorders
    • Floyed, R.A. (1999) Antioxidants, oxidative stress, and degenerative neurological disorders. Proc. Soc. Exp. Biol. 222, 236-245.
    • (1999) Proc. Soc. Exp. Biol. , vol.222 , pp. 236-245
    • Floyed, R.A.1
  • 38
    • 0032504657 scopus 로고    scopus 로고
    • Role of mitochondria in oxidative stress and ageing
    • Lenaz, G. (1998) Role of mitochondria in oxidative stress and ageing. Biochim. Biophys. Acta 1366, 53-67.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 53-67
    • Lenaz, G.1
  • 39
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov, S.S., Skulachev, V.P. & Starkov, A.A. (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416, 15-18.
    • (1997) FEBS Lett. , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 40
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: Channels, exchangers, and permeability transition
    • Bernardi, P. (1999) Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 79, 1127-1155.
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 41
    • 0024503507 scopus 로고
    • tert-Butyl-hydroperoxide kills cultured hepatocytes by peroxidizing membranes lipids
    • Masaki, N., Kyle, M.E. & Farber, J.L. (1989) tert-Butyl- hydroperoxide kills cultured hepatocytes by peroxidizing membranes lipids. Arch. Biochem. Biophys. 269, 390-399.
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 390-399
    • Masaki, N.1    Kyle, M.E.2    Farber, J.L.3
  • 42
    • 0022381068 scopus 로고
    • Ferric iron and superoxide ions are requried for the killing of cultured hepatocytes by hydrogen peroxide
    • Starke, P.E. & Farber, J.L. (1985) Ferric iron and superoxide ions are requried for the killing of cultured hepatocytes by hydrogen peroxide. J. Biol. Chem. 260, 10099-10104.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10099-10104
    • Starke, P.E.1    Farber, J.L.2
  • 44
    • 0032403050 scopus 로고    scopus 로고
    • Reactive oxygen species activate focal adhesion kinase, paxillin and p130cas tyrosine phosphorylation in endothelial cells
    • Gozin, A., Franzini, E., Andrieu, V., Da Costa, L., Rollet-Labelle, E. & Pasquier, C. (1998) Reactive oxygen species activate focal adhesion kinase, paxillin and p130cas tyrosine phosphorylation in endothelial cells. Free Radic. Biol. Med. 25, 1021-1032.
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 1021-1032
    • Gozin, A.1    Franzini, E.2    Andrieu, V.3    Da Costa, L.4    Rollet-Labelle, E.5    Pasquier, C.6
  • 45
    • 0022336547 scopus 로고
    • Mechanism of lipid peroxidation
    • Girotti, A.W. (1985) Mechanism of lipid peroxidation. Free Radic. Biol. Med. 1, 87-95.
    • (1985) Free Radic. Biol. Med. , vol.1 , pp. 87-95
    • Girotti, A.W.1
  • 46
    • 0031128356 scopus 로고    scopus 로고
    • The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver
    • Esworthy, R.S., Ho, Y.S. & Chu, F.F. (1997) The Gpx1 gene encodes mitochondrial glutathione peroxidase in the mouse liver. Arch. Biochem. Biophys. 340, 59-63.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 59-63
    • Esworthy, R.S.1    Ho, Y.S.2    Chu, F.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.