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Volumn 42, Issue 1, 2007, Pages 118-123

Effect of mercury on selenium utilization and selenoperoxidase activity in LNCaP cells

Author keywords

Glutathione peroxidase; Mercury; Methyl Se cysteine; Selenite; Selenium; Selenocysteine; Selenomethionine

Indexed keywords

ISOENZYME; MERCURY; MERCURY CHLORIDE; METHYLSELENIUM CYSTEINE; SELENITE; SELENIUM; SELENIUM DERIVATIVE; SELENOMETHIONINE; SELENOPEROXIDASE; SELENOPROTEIN;

EID: 33751532451     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.09.026     Document Type: Article
Times cited : (15)

References (43)
  • 1
    • 0033946867 scopus 로고    scopus 로고
    • Environmental medicine, part three: long-term effects of chronic low-dose mercury exposure
    • Crinnion W.J. Environmental medicine, part three: long-term effects of chronic low-dose mercury exposure. Altern. Med. Rev. 5 (2000) 209-223
    • (2000) Altern. Med. Rev. , vol.5 , pp. 209-223
    • Crinnion, W.J.1
  • 2
    • 0024416697 scopus 로고
    • Accumulation of methylmercury and inorganic mercury in the brain
    • Friberg L., and Mottet N.K. Accumulation of methylmercury and inorganic mercury in the brain. Biol. Trace Elem. Res. 21 (1989) 201-206
    • (1989) Biol. Trace Elem. Res. , vol.21 , pp. 201-206
    • Friberg, L.1    Mottet, N.K.2
  • 3
    • 0004070809 scopus 로고
    • Biological monitoring of toxic metals
    • Clarkson T.W., Friberg L., Nordberg G.F., and Sager P.R. (Eds), Plenum, New York
    • Clarkson T.W., Hursh J.B., Sager P.R., and Syversen J.P. Biological monitoring of toxic metals. In: Clarkson T.W., Friberg L., Nordberg G.F., and Sager P.R. (Eds). Mercury (1988), Plenum, New York 199-246
    • (1988) Mercury , pp. 199-246
    • Clarkson, T.W.1    Hursh, J.B.2    Sager, P.R.3    Syversen, J.P.4
  • 4
    • 0034808580 scopus 로고    scopus 로고
    • Evaluation of methylmercury biotransformation using rat liver slices
    • Yasutake A., and Hirayama K. Evaluation of methylmercury biotransformation using rat liver slices. Arch. Toxicol. 75 (2001) 400-406
    • (2001) Arch. Toxicol. , vol.75 , pp. 400-406
    • Yasutake, A.1    Hirayama, K.2
  • 5
    • 0035830692 scopus 로고    scopus 로고
    • Mercuric chloride, but not methylmercury, inhibits glutamine synthetase activity in primary cultures of cortical astrocytes
    • Allen J.W., Mutkus L.A., and Aschner M. Mercuric chloride, but not methylmercury, inhibits glutamine synthetase activity in primary cultures of cortical astrocytes. Brain Res. 891 (2001) 148-157
    • (2001) Brain Res. , vol.891 , pp. 148-157
    • Allen, J.W.1    Mutkus, L.A.2    Aschner, M.3
  • 6
  • 7
    • 70449138981 scopus 로고
    • A physicochemical rationale for the biological activity of mercury and its compounds
    • Hughes W.L. A physicochemical rationale for the biological activity of mercury and its compounds. Ann. N. Y. Acad. Sci. 65 (1957) 454-460
    • (1957) Ann. N. Y. Acad. Sci. , vol.65 , pp. 454-460
    • Hughes, W.L.1
  • 8
    • 0000228139 scopus 로고
    • The chemistry of mercury in biological systems
    • Nrigau J.O. (Ed), Elsevier, Amsterdam
    • Carthy A.J., and Malone S.F. The chemistry of mercury in biological systems. In: Nrigau J.O. (Ed). The biochemistry of mercury in the environment (1979), Elsevier, Amsterdam 433-479
    • (1979) The biochemistry of mercury in the environment , pp. 433-479
    • Carthy, A.J.1    Malone, S.F.2
  • 9
    • 0028904550 scopus 로고
    • Methylmercury-thiol uptake into cultured brain capillary endothelial cells on amino acid system L
    • Mokrzan E.M., Kerper L.E., Ballatori N., and Clarkson T.W. Methylmercury-thiol uptake into cultured brain capillary endothelial cells on amino acid system L. J. Pharmacol. Exp. Ther. 272 (1995) 1277-1284
    • (1995) J. Pharmacol. Exp. Ther. , vol.272 , pp. 1277-1284
    • Mokrzan, E.M.1    Kerper, L.E.2    Ballatori, N.3    Clarkson, T.W.4
  • 10
    • 0036690307 scopus 로고    scopus 로고
    • Antioxidant potential and gap junction-mediated intercellular communication as early biological markers of mercuric chloride toxicity in the MDCK cell line
    • Aleo M.F., Morandini F., Bettoni F., Tanganelli S., Vezzola A., Giuliani R., Steimberg N., Apostoli P., and Mazzoleni G. Antioxidant potential and gap junction-mediated intercellular communication as early biological markers of mercuric chloride toxicity in the MDCK cell line. Toxicol. In Vitro 16 (2002) 457-465
    • (2002) Toxicol. In Vitro , vol.16 , pp. 457-465
    • Aleo, M.F.1    Morandini, F.2    Bettoni, F.3    Tanganelli, S.4    Vezzola, A.5    Giuliani, R.6    Steimberg, N.7    Apostoli, P.8    Mazzoleni, G.9
  • 11
    • 1842867270 scopus 로고    scopus 로고
    • Modification of mercury toxicity by selenium: practical importance?
    • Watanabe C. Modification of mercury toxicity by selenium: practical importance?. Tohoku J. Exp. Med. 196 (2002) 71-77
    • (2002) Tohoku J. Exp. Med. , vol.196 , pp. 71-77
    • Watanabe, C.1
  • 12
    • 0014203551 scopus 로고
    • The protective effect of small amounts of selenite in sublimate intoxication
    • Parizek J., and Ostadalova I. The protective effect of small amounts of selenite in sublimate intoxication. Experientia 23 (1967) 142-143
    • (1967) Experientia , vol.23 , pp. 142-143
    • Parizek, J.1    Ostadalova, I.2
  • 13
    • 0015500586 scopus 로고
    • Selenium: relation to decreased toxicity of methylmercury added to diets containing tuna
    • Ganther H.E., Goudie C., Sunde M.L., Kopecky M.J., Wagner P., OH S.W., and Hoekstra W.G. Selenium: relation to decreased toxicity of methylmercury added to diets containing tuna. Science 175 (1972) 1122-1124
    • (1972) Science , vol.175 , pp. 1122-1124
    • Ganther, H.E.1    Goudie, C.2    Sunde, M.L.3    Kopecky, M.J.4    Wagner, P.5    OH, S.W.6    Hoekstra, W.G.7
  • 14
    • 0016651634 scopus 로고
    • Correlation between selenium and mercury in man following exposure to inorganic mercury
    • Kosta L., Byrne A.R., and Zelenko V. Correlation between selenium and mercury in man following exposure to inorganic mercury. Nature 254 (1975) 238-239
    • (1975) Nature , vol.254 , pp. 238-239
    • Kosta, L.1    Byrne, A.R.2    Zelenko, V.3
  • 15
    • 0028938588 scopus 로고
    • Selenium concentrations in brain after exposure to methylmercury: relations between the inorganic mercury fraction and selenium
    • Bjorkman L., Mottet K., Nylander M., Vahter M., Lind B., and Friberg L. Selenium concentrations in brain after exposure to methylmercury: relations between the inorganic mercury fraction and selenium. Arch. Toxicol. 69 (1995) 228-234
    • (1995) Arch. Toxicol. , vol.69 , pp. 228-234
    • Bjorkman, L.1    Mottet, K.2    Nylander, M.3    Vahter, M.4    Lind, B.5    Friberg, L.6
  • 16
    • 0016919405 scopus 로고
    • Metabolic aspects of selenium action and toxicity
    • Diplock A.T. Metabolic aspects of selenium action and toxicity. CRC Crit. Rev. Toxicol. 4 (1976) 271-329
    • (1976) CRC Crit. Rev. Toxicol. , vol.4 , pp. 271-329
    • Diplock, A.T.1
  • 19
    • 0345310068 scopus 로고    scopus 로고
    • Chemopreventive agents: selenium
    • Combs Jr. G.F., and Gray W.P. Chemopreventive agents: selenium. Pharmacol. Ther. 79 (1998) 179-192
    • (1998) Pharmacol. Ther. , vol.79 , pp. 179-192
    • Combs Jr., G.F.1    Gray, W.P.2
  • 20
    • 14044262903 scopus 로고    scopus 로고
    • Selective rescue of selenoprotein expression in mice lacking a highly specialized methyl group in selenocysteine tRNA
    • Carlson B.A., Xu X.M., Gladyshev V.N., and Hatfield D.L. Selective rescue of selenoprotein expression in mice lacking a highly specialized methyl group in selenocysteine tRNA. J. Biol. Chem. 280 (2005) 5542-5548
    • (2005) J. Biol. Chem. , vol.280 , pp. 5542-5548
    • Carlson, B.A.1    Xu, X.M.2    Gladyshev, V.N.3    Hatfield, D.L.4
  • 21
    • 0036016079 scopus 로고    scopus 로고
    • Selenocompounds in plants and animals and their biological significance
    • Whanger P.D. Selenocompounds in plants and animals and their biological significance. J. Am. Coll. Nutr. 21 (2002) 223-232
    • (2002) J. Am. Coll. Nutr. , vol.21 , pp. 223-232
    • Whanger, P.D.1
  • 22
    • 12844265308 scopus 로고    scopus 로고
    • Characterization of potential selenium-binding proteins in the selenophosphate synthetase system
    • Ogasawara Y., Lacourciere G.M., Ishii K., and Stadtman T.C. Characterization of potential selenium-binding proteins in the selenophosphate synthetase system. Proc. Natl. Acad. Sci. USA 102 (2005) 1012-1016
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1012-1016
    • Ogasawara, Y.1    Lacourciere, G.M.2    Ishii, K.3    Stadtman, T.C.4
  • 23
    • 0035499470 scopus 로고    scopus 로고
    • Impairment of spermatogenesis in rats by methylmercury: involvement of stage- and cell- specific germ cell apoptosis
    • Homma-Takeda S., Kugenuma Y., Iwamuro T., Kumagai Y., and Shimojo N. Impairment of spermatogenesis in rats by methylmercury: involvement of stage- and cell- specific germ cell apoptosis. Toxicology 169 (2001) 25-35
    • (2001) Toxicology , vol.169 , pp. 25-35
    • Homma-Takeda, S.1    Kugenuma, Y.2    Iwamuro, T.3    Kumagai, Y.4    Shimojo, N.5
  • 28
    • 0025142673 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase
    • Maiorino M., Gregolin C., and Ursini F. Phospholipid hydroperoxide glutathione peroxidase. Methods Enzymol. 186 (1990) 448-457
    • (1990) Methods Enzymol. , vol.186 , pp. 448-457
    • Maiorino, M.1    Gregolin, C.2    Ursini, F.3
  • 29
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun A., and Weinstein D. Assay of proteins in the presence of interfering materials. Anal. Biochem. 70 (1976) 241-250
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 30
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini F., Maiorino M., and Gregolin C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta 839 (1985) 62-70
    • (1985) Biochim. Biophys. Acta , vol.839 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 31
    • 0036128974 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin reductase and thiol status
    • Bindoli A., and Rigobello M.P. Mitochondrial thioredoxin reductase and thiol status. Methods Enzymol. 347 (2002) 307-316
    • (2002) Methods Enzymol. , vol.347 , pp. 307-316
    • Bindoli, A.1    Rigobello, M.P.2
  • 32
    • 0020575805 scopus 로고
    • Purification and characterization of selenium-glutathione peroxidase from hamster liver
    • Chaudiere J., and Tappel A.L. Purification and characterization of selenium-glutathione peroxidase from hamster liver. Arch. Biochem. Biophys. 226 (1983) 448-457
    • (1983) Arch. Biochem. Biophys. , vol.226 , pp. 448-457
    • Chaudiere, J.1    Tappel, A.L.2
  • 33
    • 0006386227 scopus 로고
    • Phospholipid hydroperoxide Glutathione peroxidase is the major selenoperoxidase in nuclei and mitochondria of rat testis
    • Poli G., Albano E., and MU D. (Eds), Birkhäuser Verlag, Basel
    • Maiorino M., Roveri A., and Ursini F. Phospholipid hydroperoxide Glutathione peroxidase is the major selenoperoxidase in nuclei and mitochondria of rat testis. In: Poli G., Albano E., and MU D. (Eds). Free radicals from Basic Science to Medicine (1993), Birkhäuser Verlag, Basel 412-418
    • (1993) Free radicals from Basic Science to Medicine , pp. 412-418
    • Maiorino, M.1    Roveri, A.2    Ursini, F.3
  • 34
    • 0028291969 scopus 로고
    • Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase
    • Roveri A., Maiorino M., and Ursini F. Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase. Methods Enzymol. 233 (1994) 202-212
    • (1994) Methods Enzymol. , vol.233 , pp. 202-212
    • Roveri, A.1    Maiorino, M.2    Ursini, F.3
  • 35
    • 0024350070 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase: specific activity in tissues of rats of different age and comparison with other glutathione peroxidases
    • Zhang L.P., Maiorino M., Roveri A., and Ursini F. Phospholipid hydroperoxide glutathione peroxidase: specific activity in tissues of rats of different age and comparison with other glutathione peroxidases. Biochim. Biophys. Acta 1006 (1989) 140-143
    • (1989) Biochim. Biophys. Acta , vol.1006 , pp. 140-143
    • Zhang, L.P.1    Maiorino, M.2    Roveri, A.3    Ursini, F.4
  • 36
    • 0025787017 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase is the 18-kDa selenoprotein expressed in human tumor cell lines
    • Maiorino M., Chu F.F., Ursini F., Davies K.J., Doroshow J.H., and Esworthy R.S. Phospholipid hydroperoxide glutathione peroxidase is the 18-kDa selenoprotein expressed in human tumor cell lines. J. Biol. Chem. 266 (1991) 7728-7732
    • (1991) J. Biol. Chem. , vol.266 , pp. 7728-7732
    • Maiorino, M.1    Chu, F.F.2    Ursini, F.3    Davies, K.J.4    Doroshow, J.H.5    Esworthy, R.S.6
  • 37
    • 0029741901 scopus 로고    scopus 로고
    • Conventional cell culture media do not adequately supply cells with antioxidants and thus facilitate peroxide-induced genotoxicity
    • Leist M., Raab B., Maurer S., Rosick U., and Brigelius-Flohé R. Conventional cell culture media do not adequately supply cells with antioxidants and thus facilitate peroxide-induced genotoxicity. Free Radic. Biol. Med. 21 (1996) 297-306
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 297-306
    • Leist, M.1    Raab, B.2    Maurer, S.3    Rosick, U.4    Brigelius-Flohé, R.5
  • 38
    • 9644269183 scopus 로고    scopus 로고
    • Does mercury promote lipid peroxidation? An in vitro study concerning mercury, copper, and iron in peroxidation of low-density lipoprotein
    • Seppanen K., Soininen P., Salonen J.T., Lotjonen S., and Laatikainen R. Does mercury promote lipid peroxidation? An in vitro study concerning mercury, copper, and iron in peroxidation of low-density lipoprotein. Biol. Trace Elem. Res. 101 (2004) 117-132
    • (2004) Biol. Trace Elem. Res. , vol.101 , pp. 117-132
    • Seppanen, K.1    Soininen, P.2    Salonen, J.T.3    Lotjonen, S.4    Laatikainen, R.5
  • 39
    • 0016252726 scopus 로고
    • Effect of mercury on erythrocyte glutathione reductase activity. In vivo and in vitro studies
    • Mykkanen H.M., and Ganther H.E. Effect of mercury on erythrocyte glutathione reductase activity. In vivo and in vitro studies. Bull. Environ. Contam. Toxicol. 12 (1974) 10-16
    • (1974) Bull. Environ. Contam. Toxicol. , vol.12 , pp. 10-16
    • Mykkanen, H.M.1    Ganther, H.E.2
  • 40
    • 6444226218 scopus 로고    scopus 로고
    • The use of high-selenium yeast to raise selenium status: how does it measure up?
    • Rayman M.P. The use of high-selenium yeast to raise selenium status: how does it measure up?. Br. J. Nutr. 92 (2004) 557-573
    • (2004) Br. J. Nutr. , vol.92 , pp. 557-573
    • Rayman, M.P.1
  • 42
    • 4444238218 scopus 로고    scopus 로고
    • Distribution of selenium-containing proteins in human serum
    • Gao Y., Liu Y., Deng G., and Wang Z. Distribution of selenium-containing proteins in human serum. Biol. Trace Elem. Res. 100 (2004) 105-115
    • (2004) Biol. Trace Elem. Res. , vol.100 , pp. 105-115
    • Gao, Y.1    Liu, Y.2    Deng, G.3    Wang, Z.4
  • 43
    • 0037337666 scopus 로고    scopus 로고
    • Gene disruption discloses role of selenoprotein P in selenium delivery to target tissues
    • Schomburg L., Schweizer U., Holtmann B., Flohé L., Sendtner M., and Kohrle J. Gene disruption discloses role of selenoprotein P in selenium delivery to target tissues. Biochem. J. 370 (2003) 397-402
    • (2003) Biochem. J. , vol.370 , pp. 397-402
    • Schomburg, L.1    Schweizer, U.2    Holtmann, B.3    Flohé, L.4    Sendtner, M.5    Kohrle, J.6


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