메뉴 건너뛰기




Volumn 98, Issue 1, 2004, Pages 73-84

Effect of long-term se deficiency on the antioxidant capacities of rat vascular tissue

Author keywords

Antioxidant capacity; Glutathione peroxidase; Selenium; Thioredoxin reductase; Vascular tissue

Indexed keywords

ANTIOXIDANT; DRINKING WATER; GLUTATHIONE PEROXIDASE; MALONALDEHYDE; SELENIUM; SUPEROXIDE DISMUTASE; THIOREDOXIN REDUCTASE;

EID: 1942517972     PISSN: 01634984     EISSN: None     Source Type: Journal    
DOI: 10.1385/BTER:98:1:73     Document Type: Article
Times cited : (43)

References (41)
  • 1
    • 0343307138 scopus 로고    scopus 로고
    • Death by design: Programmed cell death in cardiovascular biology and disease
    • W. R. MacLellan and M. D. Schneider, Death by design: programmed cell death in cardiovascular biology and disease, Circ. Res. 81, 137-144 (1997).
    • (1997) Circ. Res. , vol.81 , pp. 137-144
    • MacLellan, W.R.1    Schneider, M.D.2
  • 2
    • 0032424180 scopus 로고    scopus 로고
    • Apoptosis of endothelial cells - Contribution to the pathophysiology of atherosclerosis
    • S. Dimmeler, C. Hermann, and A. M. Zerher, Apoptosis of endothelial cells - contribution to the pathophysiology of atherosclerosis, Eur. Cytokine Network 9, 697-698 (1998).
    • (1998) Eur. Cytokine Network , vol.9 , pp. 697-698
    • Dimmeler, S.1    Hermann, C.2    Zerher, A.M.3
  • 3
    • 0034662094 scopus 로고    scopus 로고
    • The importance of selenium to human health
    • M. P. Rayman, The importance of selenium to human health, Lancet 356, 233-241 (2000).
    • (2000) Lancet , vol.356 , pp. 233-241
    • Rayman, M.P.1
  • 5
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • L. Z. Zhong and A. Holmgren, Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations, J. Biol. Chem. 275, 18,121-18,128 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 18121-18128
    • Zhong, L.Z.1    Holmgren, A.2
  • 6
    • 0038957365 scopus 로고    scopus 로고
    • Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress
    • M. J. Prieto-Alamo, J. Jurado, G. M. Rafaela, et al., Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress, J. Biol. Chem. 275, 13,398-13,405 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 13398-13405
    • Prieto-Alamo, M.J.1    Jurado, J.2    Rafaela, G.M.3
  • 7
    • 0032944618 scopus 로고    scopus 로고
    • Effect of selenium on rat thioredoxin reductase activity
    • M. M. Berggren, J. F. Mangin, J. R. Gasdaska, et al., Effect of selenium on rat thioredoxin reductase activity, Biochem. Pharmacol. 57, 187-193 (1999).
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 187-193
    • Berggren, M.M.1    Mangin, J.F.2    Gasdaska, J.R.3
  • 8
    • 0031578221 scopus 로고    scopus 로고
    • Thioredoxin reductase activity is decreased by selenium deficiency
    • K. E. Hill, G. W. McCollum, M. E. Boeglin, et al., Thioredoxin reductase activity is decreased by selenium deficiency, Biochem. Biophys. Res. Commun. 234, 293-295 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 293-295
    • Hill, K.E.1    McCollum, G.W.2    Boeglin, M.E.3
  • 9
    • 0033911613 scopus 로고    scopus 로고
    • Selenium deficiency-induced alterations in the vascular system of the rat
    • X. H. Qu, K. X. Huang, L. Q. Deng, et al., Selenium deficiency-induced alterations in the vascular system of the rat, Biol. Trace Element Res. 75, 119-138 (2000).
    • (2000) Biol. Trace Element Res. , vol.75 , pp. 119-138
    • Qu, X.H.1    Huang, K.X.2    Deng, L.Q.3
  • 10
    • 0027409382 scopus 로고
    • Lethal damage to endothelial cells by oxidized low density lipoprotein: Role of selenoperoxidase in cytoprotection against lipid hydroperoxide- and iron-mediated reactions
    • J. P. Thomas, P. G. Geiger, and A. W. Girotti, Lethal damage to endothelial cells by oxidized low density lipoprotein: role of selenoperoxidase in cytoprotection against lipid hydroperoxide-and iron-mediated reactions, J. Lipid Res. 34, 479-190 (1993).
    • (1993) J. Lipid Res. , vol.34 , pp. 479-1190
    • Thomas, J.P.1    Geiger, P.G.2    Girotti, A.W.3
  • 11
    • 0031227866 scopus 로고    scopus 로고
    • Selenium and cardiovascular disease - An update
    • J. K. Huttunen, Selenium and cardiovascular disease - an update, Biomed. Environ. Stud. 10, 116-124 (1997).
    • (1997) Biomed. Environ. Stud. , vol.10 , pp. 116-124
    • Huttunen, J.K.1
  • 12
    • 0026497715 scopus 로고
    • Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells
    • M. R. Fernando, H. Nanri, S. Yoshitake, et al., Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells, Eur. J. Biochem. 209, 917-922 (1992).
    • (1992) Eur. J. Biochem. , vol.209 , pp. 917-922
    • Fernando, M.R.1    Nanri, H.2    Yoshitake, S.3
  • 13
    • 0034696832 scopus 로고    scopus 로고
    • Purification of the newly found selenium-containing proteins in the arterial wall and brain of the rat
    • X. H. Qu, K. X. Huang, Z. X. Wu, et al., Purification of the newly found selenium-containing proteins in the arterial wall and brain of the rat, Biochem. Biophys. Res. Commun. 270, 688-694 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 688-694
    • Qu, X.H.1    Huang, K.X.2    Wu, Z.X.3
  • 14
    • 0036223851 scopus 로고    scopus 로고
    • Role of selenium in cytoprotection against cholesterol oxide-induced vascular damage in rats
    • K. X. Huang, H. M. Liu, Z. X. Chen, et al., Role of selenium in cytoprotection against cholesterol oxide-induced vascular damage in rats, Atherosclerosis 162, 137-144 (2002).
    • (2002) Atherosclerosis , vol.162 , pp. 137-144
    • Huang, K.X.1    Liu, H.M.2    Chen, Z.X.3
  • 15
    • 0013866973 scopus 로고
    • Fluorometric determination of selenium in biological material with 2,3-diaminoaphthalene
    • J. H. Wathingson, Fluorometric determination of selenium in biological material with 2,3-diaminoaphthalene, Anal. Chem. 38(1), 92-96 (1966).
    • (1966) Anal. Chem. , vol.38 , Issue.1 , pp. 92-96
    • Wathingson, J.H.1
  • 16
    • 0016170551 scopus 로고
    • Effect of dietary selenium on erythrocyte and liver glutathione peroxidase in the rat
    • D. G. Hofeman, R. A. Sunde, and W. G. Hoekstra, Effect of dietary selenium on erythrocyte and liver glutathione peroxidase in the rat, J. Nutr. 104, 580-587 (1974).
    • (1974) J. Nutr. , vol.104 , pp. 580-587
    • Hofeman, D.G.1    Sunde, R.A.2    Hoekstra, W.G.3
  • 17
    • 0024402834 scopus 로고
    • An assay for superoxide dismutase activity in mammalian tissue homogenates
    • D. R. Spitz and L. W. Oberley, An assay for superoxide dismutase activity in mammalian tissue homogenates, Anal. Biochem. 179, 8-18 (1989).
    • (1989) Anal. Biochem. , vol.179 , pp. 8-18
    • Spitz, D.R.1    Oberley, L.W.2
  • 18
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • O. Hiroshi, O. Nobuko, and Y. Kunio, Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction, Anal. Biochem. 95, 351-358 (1979).
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Hiroshi, O.1    Nobuko, O.2    Kunio, Y.3
  • 19
    • 0027509770 scopus 로고
    • A novel method for measuring antioxidant capacity and its application to monitoring the antioxidant status in premature neonates
    • N. J. Miller, C. Rice-Evans, M. J. Davies, et al., A novel method for measuring antioxidant capacity and its application to monitoring the antioxidant status in premature neonates, Clin. Sci. 84, 407-412 (1993).
    • (1993) Clin. Sci. , vol.84 , pp. 407-412
    • Miller, N.J.1    Rice-Evans, C.2    Davies, M.J.3
  • 20
    • 0017653811 scopus 로고
    • Bovine thioredoxin system: Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction
    • A. Holmgren, Bovine thioredoxin system: purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction, J. Biol. Chem. 252, 4600-4606 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 4600-4606
    • Holmgren, A.1
  • 21
    • 0027186030 scopus 로고
    • Purification of human thioredoxin reductase: Properties and characterization by absorption and circular dichroism spectroscopy
    • J. E. Oblong, P. Y. Gasdaska, K. Sherrill, et al., Purification of human thioredoxin reductase: properties and characterization by absorption and circular dichroism spectroscopy, Biochemistry 32, 7271-7277 (1993).
    • (1993) Biochemistry , vol.32 , pp. 7271-7277
    • Oblong, J.E.1    Gasdaska, P.Y.2    Sherrill, K.3
  • 22
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • O. H. Lowery, N. J. Roscbrough, A. L. Farr, et al., Protein measurement with the folin phenol reagent, J. Biol. Chem. 193, 265-275 (1951).
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowery, O.H.1    Roscbrough, N.J.2    Farr, A.L.3
  • 23
    • 0020581052 scopus 로고
    • Selenium concentration and glutathione peroxidase activity in normal and neoplastic development of the mouse mammary gland
    • H. W. Lane and D. Medina, Selenium concentration and glutathione peroxidase activity in normal and neoplastic development of the mouse mammary gland, Cancer Res. 43, 1558-1561 (1983).
    • (1983) Cancer Res. , vol.43 , pp. 1558-1561
    • Lane, H.W.1    Medina, D.2
  • 24
    • 0027213554 scopus 로고
    • Regulation of selenoproteins
    • R. F. Burk and K. E. Hill, Regulation of selenoproteins, Annu. Rev. Nutr. 13, 65-81 (1993).
    • (1993) Annu. Rev. Nutr. , vol.13 , pp. 65-81
    • Burk, R.F.1    Hill, K.E.2
  • 25
    • 0029076826 scopus 로고
    • Glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase are differentially regulated in rats by dietary selenium
    • X. G. Lei, J. K. Evenson, K. M. Thompson, et al., Glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase are differentially regulated in rats by dietary selenium, J. Nutr. 125, 1438-1446 (1995).
    • (1995) J. Nutr. , vol.125 , pp. 1438-1446
    • Lei, X.G.1    Evenson, J.K.2    Thompson, K.M.3
  • 26
    • 0023892793 scopus 로고
    • Effect of selenium status on mRNA levels for glutathione peroxidase in rat liver
    • M. S. Saedi, C. G. Smith, J. Frampton, et al., Effect of selenium status on mRNA levels for glutathione peroxidase in rat liver, Biochem. Biophys. Res. Commun. 153, 855-861 (1988).
    • (1988) Biochem. Biophys. Res. Commun. , vol.153 , pp. 855-861
    • Saedi, M.S.1    Smith, C.G.2    Frampton, J.3
  • 27
    • 0028820877 scopus 로고
    • Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats
    • G. Bermano, F. Nicol, J. A. Dyer, et al., Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats, Biochem. J. 311, 425-430 (1995).
    • (1995) Biochem. J. , vol.311 , pp. 425-430
    • Bermano, G.1    Nicol, F.2    Dyer, J.A.3
  • 28
    • 0028859763 scopus 로고
    • Tissue specificity of selenoprotein gene expression in rats
    • M. J. Christensen, P. M. Cammack, and C. D. Wray, Tissue specificity of selenoprotein gene expression in rats, J. Nutr. Biochem. 6, 367-372 (1995).
    • (1995) J. Nutr. Biochem. , vol.6 , pp. 367-372
    • Christensen, M.J.1    Cammack, P.M.2    Wray, C.D.3
  • 29
    • 0028943790 scopus 로고
    • Systemic nature of endothelial dysfunction in atherosclerosis
    • J. J. Anderson, M. D. Gerhard, I. T. Meredith, et al., Systemic nature of endothelial dysfunction in atherosclerosis, Am. J. Cardiol. 75, 71B-74B (1995).
    • (1995) Am. J. Cardiol. , vol.75
    • Anderson, J.J.1    Gerhard, M.D.2    Meredith, I.T.3
  • 30
    • 0029682733 scopus 로고    scopus 로고
    • Selenium, glutathione peroxidase, peroxides and platelet functions
    • D. Vitoux, P. Chappuis, J. Arnaud, et al., Selenium, glutathione peroxidase, peroxides and platelet functions, Ann. Biol. Clin. 54, 181-187 (1996).
    • (1996) Ann. Biol. Clin. , vol.54 , pp. 181-187
    • Vitoux, D.1    Chappuis, P.2    Arnaud, J.3
  • 31
    • 0033975784 scopus 로고    scopus 로고
    • Altered eicosanoid biosynthesis in selenium-deficient endothelial cells
    • Y. Z. Cao, C. C. Reddy, and L. M. Sordillo, Altered eicosanoid biosynthesis in selenium-deficient endothelial cells, Free Radical Biol. Med. 28, 381-389 (2000).
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 381-389
    • Cao, Y.Z.1    Reddy, C.C.2    Sordillo, L.M.3
  • 32
    • 0032848137 scopus 로고    scopus 로고
    • Selenium metabolism, selenoproteins and mechanisms of cancer prevention: Complexities with thioredoxin reductase
    • H. E. Ganther, Selenium metabolism, selenoproteins and mechanisms of cancer prevention: complexities with thioredoxin reductase, Carcinogenesis 20, 1657-1666 (1999).
    • (1999) Carcinogenesis , vol.20 , pp. 1657-1666
    • Ganther, H.E.1
  • 33
    • 0037150999 scopus 로고    scopus 로고
    • Mutational analysis of human thioredoxin reductase 1
    • X. R. Ma, J. B. Hu, D. J. Lindner, et al., Mutational analysis of human thioredoxin reductase 1, J. Biol. Chem. 277, 22,460-22,468 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 22460-22468
    • Ma, X.R.1    Hu, J.B.2    Lindner, D.J.3
  • 34
    • 0032502720 scopus 로고    scopus 로고
    • Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue
    • L. Zhong, E. S. J. Arner, J. Ljung, et al., Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue, J. Biol. Chem. 273, 8581-8591 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8581-8591
    • Zhong, L.1    Arner, E.S.J.2    Ljung, J.3
  • 35
    • 0032555276 scopus 로고    scopus 로고
    • Human thioredoxin reductase from HeLa cells: Selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin
    • S. N. Gorlatov and T. C. Stadtman, Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin, Proc. Natl. Acad. Sci. USA 95, 8520-8525 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8520-8525
    • Gorlatov, S.N.1    Stadtman, T.C.2
  • 36
    • 0033609827 scopus 로고    scopus 로고
    • Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductase
    • Q. A. Sun, Y. Wu, F. Zappacosta, et al., Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductase, J. Biol. Chem. 274, 24,522-24,530 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 24522-24530
    • Sun, Q.A.1    Wu, Y.2    Zappacosta, F.3
  • 37
    • 0033775650 scopus 로고    scopus 로고
    • Thioredoxin reductase as a pathophysiological factor and drug target
    • K. Becker, S. Gromer, R. H. Schirmer, et al., Thioredoxin reductase as a pathophysiological factor and drug target, Eur. J. Biochem. 267, 6118-6125 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6118-6125
    • Becker, K.1    Gromer, S.2    Schirmer, R.H.3
  • 38
    • 0035138443 scopus 로고    scopus 로고
    • Role of thioredoxin reductase in the Yaplp-dependent response to oxidative stress in Sacharomyces cerevisiae
    • O. C. Harel, R. Stearman, A. P. Gasch, et al., Role of thioredoxin reductase in the Yaplp-dependent response to oxidative stress in Sacharomyces cerevisiae, Mol. Microbiol. 39, 595-605 (2001).
    • (2001) Mol. Microbiol. , vol.39 , pp. 595-605
    • Harel, O.C.1    Stearman, R.2    Gasch, A.P.3
  • 39
    • 0026497715 scopus 로고
    • Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells
    • M. R. Fernando, H. Nanri, S. Yoshitake, et al., Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells, Eur. J. Biochem. 209, 917-922 (1992).
    • (1992) Eur. J. Biochem. , vol.209 , pp. 917-922
    • Fernando, M.R.1    Nanri, H.2    Yoshitake, S.3
  • 40
    • 0034852588 scopus 로고    scopus 로고
    • The biochemistry of selenium and the glutathione system
    • G. E. Arteel and H. Sies, The biochemistry of selenium and the glutathione system, Environ. Toxicol. Pharmacol. 10, 153-158 (2001).
    • (2001) Environ. Toxicol. Pharmacol. , vol.10 , pp. 153-158
    • Arteel, G.E.1    Sies, H.2
  • 41
    • 0033152682 scopus 로고    scopus 로고
    • Functional expression of rat thioredoxin reductase: Selenocysteine insertion sequence element is essential for the active enzyme
    • W. Fujiwara, T. Fujii, J. Fujii, et al., Functional expression of rat thioredoxin reductase: selenocysteine insertion sequence element is essential for the active enzyme, Biochem. J. 340, 439-444 (1999).
    • (1999) Biochem. J. , vol.340 , pp. 439-444
    • Fujiwara, W.1    Fujii, T.2    Fujii, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.