메뉴 건너뛰기




Volumn 1782, Issue 7-8, 2008, Pages 482-488

Cystathionine beta synthase deficiency induces catalase-mediated hydrogen peroxide detoxification in mice liver

Author keywords

Homocysteine; NADPH oxidase; Oxidative stress; Reactive nitrogen species; Reactive oxygen species

Indexed keywords

CATALASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; HYDROGEN PEROXIDE; NITRITE; PEROXYNITRITE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; COPPER ZINC SUPEROXIDE DISMUTASE; CYSTATHIONINE BETA SYNTHASE; HEME OXYGENASE 1; PRIMER DNA; SUPEROXIDE DISMUTASE;

EID: 49649119223     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2008.05.003     Document Type: Article
Times cited : (13)

References (61)
  • 1
    • 0032771346 scopus 로고    scopus 로고
    • Homocysteine metabolism
    • Selhub J. Homocysteine metabolism. Annu. Rev. Nutr. 19 (1999) 217-246
    • (1999) Annu. Rev. Nutr. , vol.19 , pp. 217-246
    • Selhub, J.1
  • 2
    • 0026633925 scopus 로고
    • Hyperhomocyst(e)inemia as a risk factor for occlusive vascular disease
    • Kang S.S., Wong P.W., and Malinow M.R. Hyperhomocyst(e)inemia as a risk factor for occlusive vascular disease. Annu. Rev. Nutr. 12 (1992) 279-298
    • (1992) Annu. Rev. Nutr. , vol.12 , pp. 279-298
    • Kang, S.S.1    Wong, P.W.2    Malinow, M.R.3
  • 4
    • 0014545138 scopus 로고
    • Vascular pathology of homocysteinemia: implications for the pathogenesis of arteriosclerosis
    • McCully K.S. Vascular pathology of homocysteinemia: implications for the pathogenesis of arteriosclerosis. Am. J. Pathol. 56 (1969) 111-128
    • (1969) Am. J. Pathol. , vol.56 , pp. 111-128
    • McCully, K.S.1
  • 5
    • 0031718236 scopus 로고    scopus 로고
    • Mechanisms of thrombosis in hyperhomocysteinemia
    • Lentz S.R. Mechanisms of thrombosis in hyperhomocysteinemia. Curr. Opin. Hematol. 5 (1998) 343-349
    • (1998) Curr. Opin. Hematol. , vol.5 , pp. 343-349
    • Lentz, S.R.1
  • 6
    • 0032499024 scopus 로고    scopus 로고
    • Homocysteine and atherothrombosis
    • Welch G.N., and Loscalzo J. Homocysteine and atherothrombosis. N. Engl. J. Med. 338 (1998) 1042-1050
    • (1998) N. Engl. J. Med. , vol.338 , pp. 1042-1050
    • Welch, G.N.1    Loscalzo, J.2
  • 7
    • 0033533527 scopus 로고    scopus 로고
    • Homocyst(e)ine and cardiovascular disease: a critical review of the epidemiologic evidence
    • Eikelboom J.W., Lonn E., Genest Jr. J., Hankey G., and Yusuf S. Homocyst(e)ine and cardiovascular disease: a critical review of the epidemiologic evidence. Ann. Intern. Med. 131 (1999) 363-375
    • (1999) Ann. Intern. Med. , vol.131 , pp. 363-375
    • Eikelboom, J.W.1    Lonn, E.2    Genest Jr., J.3    Hankey, G.4    Yusuf, S.5
  • 9
    • 28344446460 scopus 로고    scopus 로고
    • Mechanisms of homocysteine-induced atherothrombosis
    • Lentz S.R. Mechanisms of homocysteine-induced atherothrombosis. J. Thromb. Haemost. 3 (2005) 1646-1654
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1646-1654
    • Lentz, S.R.1
  • 12
    • 0034664982 scopus 로고    scopus 로고
    • Characterization of homocysteine metabolism in the rat liver
    • Stead L.M., Brosnan M.E., and Brosnan J.T. Characterization of homocysteine metabolism in the rat liver. Biochem. J. 350 (2000) 685-692
    • (2000) Biochem. J. , vol.350 , pp. 685-692
    • Stead, L.M.1    Brosnan, M.E.2    Brosnan, J.T.3
  • 15
    • 17544374598 scopus 로고    scopus 로고
    • Hyperhomocysteinemia induces hepatic cholesterol biosynthesis and lipid accumulation via activation of transcription factors
    • Woo C.W., Siow Y.L., Pierce G.N., Choy P.C., Minuk G.Y., Mymin D., and K.O. Hyperhomocysteinemia induces hepatic cholesterol biosynthesis and lipid accumulation via activation of transcription factors. Am. J. Physiol. Endocrinol. Metab. 288 (2005) E1002-E1010
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.288
    • Woo, C.W.1    Siow, Y.L.2    Pierce, G.N.3    Choy, P.C.4    Minuk, G.Y.5    Mymin, D.6    Karmin, O.7
  • 16
    • 11144230938 scopus 로고    scopus 로고
    • Abnormal lipid metabolism in cystathionine beta-synthase-deficient mice, an animal model for hyperhomocysteinemia
    • Namekata K., Enokido Y., Ishii I., Nagai Y., Harada T., and Kimura H. Abnormal lipid metabolism in cystathionine beta-synthase-deficient mice, an animal model for hyperhomocysteinemia. J. Biol. Chem. 279 (2004) 52961-52969
    • (2004) J. Biol. Chem. , vol.279 , pp. 52961-52969
    • Namekata, K.1    Enokido, Y.2    Ishii, I.3    Nagai, Y.4    Harada, T.5    Kimura, H.6
  • 17
    • 33645282568 scopus 로고    scopus 로고
    • Elevated homocysteine reduces apolipoprotein A-I expression in hyperhomocysteinemic mice and in males with coronary artery disease
    • Mikael L.G., Genest Jr. J., and Rozen R. Elevated homocysteine reduces apolipoprotein A-I expression in hyperhomocysteinemic mice and in males with coronary artery disease. Circ. Res. 98 (2006) 564-571
    • (2006) Circ. Res. , vol.98 , pp. 564-571
    • Mikael, L.G.1    Genest Jr., J.2    Rozen, R.3
  • 18
    • 33751527922 scopus 로고    scopus 로고
    • Hyperhomocysteinemia due to cystathionine beta synthase deficiency induces dysregulation of genes involved in hepatic lipid homeostasis in mice
    • Hamelet J., Demuth K., Delabar J.M., and Janel N. Hyperhomocysteinemia due to cystathionine beta synthase deficiency induces dysregulation of genes involved in hepatic lipid homeostasis in mice. J. Hepatol. 46 (2007) 151-159
    • (2007) J. Hepatol. , vol.46 , pp. 151-159
    • Hamelet, J.1    Demuth, K.2    Delabar, J.M.3    Janel, N.4
  • 19
    • 0022552919 scopus 로고
    • Endothelial cell injury due to copper-catalyzed hydrogen peroxide generation from homocysteine
    • Starkebaum G., and Harlan J.M. Endothelial cell injury due to copper-catalyzed hydrogen peroxide generation from homocysteine. J. Clin. Invest. 77 (1986) 1370-1376
    • (1986) J. Clin. Invest. , vol.77 , pp. 1370-1376
    • Starkebaum, G.1    Harlan, J.M.2
  • 20
    • 0030188563 scopus 로고    scopus 로고
    • The oxidant stress of hyperhomocyst(e)inemia
    • Loscalzo J. The oxidant stress of hyperhomocyst(e)inemia. J. Clin. Invest. 98 (1996) 5-7
    • (1996) J. Clin. Invest. , vol.98 , pp. 5-7
    • Loscalzo, J.1
  • 21
    • 0035940411 scopus 로고    scopus 로고
    • Overexpression of cellular glutathione peroxidase rescues homocyst(e)ine-induced endothelial dysfunction
    • Weiss N., Zhang Y.Y., Heydrick S., Bierl C., and Loscalzo J. Overexpression of cellular glutathione peroxidase rescues homocyst(e)ine-induced endothelial dysfunction. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 12503-12508
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12503-12508
    • Weiss, N.1    Zhang, Y.Y.2    Heydrick, S.3    Bierl, C.4    Loscalzo, J.5
  • 22
    • 0024810730 scopus 로고
    • Toxicity of thiols and disulphides: involvement of free-radical species
    • Munday R. Toxicity of thiols and disulphides: involvement of free-radical species. Free Radic. Biol. Med. 7 (1989) 659-673
    • (1989) Free Radic. Biol. Med. , vol.7 , pp. 659-673
    • Munday, R.1
  • 26
    • 33746854283 scopus 로고    scopus 로고
    • Hyperhomocysteinemia induces liver injury in rat: protective effect of folic acid supplementation
    • Woo C.W., Prathapasinghe G.A., Siow Y.L., and K.O. Hyperhomocysteinemia induces liver injury in rat: protective effect of folic acid supplementation. Biochim. Biophys. Acta 1762 (2006) 656-665
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 656-665
    • Woo, C.W.1    Prathapasinghe, G.A.2    Siow, Y.L.3    K.O4
  • 27
    • 1242328722 scopus 로고    scopus 로고
    • Opposite effect of methionine-supplemented diet, a model of hyperhomocysteinemia, on plasma and liver antioxidant status in normotensive and spontaneously hypertensive rats
    • Robin S., Courderot-Masuyer C., Nicod L., Jacqueson A., Richert L., and Berthelot A. Opposite effect of methionine-supplemented diet, a model of hyperhomocysteinemia, on plasma and liver antioxidant status in normotensive and spontaneously hypertensive rats. J. Nutr. Biochem. 15 (2004) 80-89
    • (2004) J. Nutr. Biochem. , vol.15 , pp. 80-89
    • Robin, S.1    Courderot-Masuyer, C.2    Nicod, L.3    Jacqueson, A.4    Richert, L.5    Berthelot, A.6
  • 29
    • 0035182406 scopus 로고    scopus 로고
    • Folate depletion and elevated plasma homocysteine promote oxidative stress in rat livers
    • Huang R.F., Hsu Y.C., Lin H.L., and Yang F.L. Folate depletion and elevated plasma homocysteine promote oxidative stress in rat livers. J. Nutr. 131 (2001) 33-38
    • (2001) J. Nutr. , vol.131 , pp. 33-38
    • Huang, R.F.1    Hsu, Y.C.2    Lin, H.L.3    Yang, F.L.4
  • 30
    • 31544434851 scopus 로고    scopus 로고
    • Proteomic analysis reveals changes in the liver protein pattern of rats exposed to dietary folate deficiency
    • Chanson A., Sayd T., Rock E., Chambon C., Santé-Lhoutellier V., Potier de Courcy G., and Brachet P. Proteomic analysis reveals changes in the liver protein pattern of rats exposed to dietary folate deficiency. J. Nutr. 135 (2005) 2524-2529
    • (2005) J. Nutr. , vol.135 , pp. 2524-2529
    • Chanson, A.1    Sayd, T.2    Rock, E.3    Chambon, C.4    Santé-Lhoutellier, V.5    Potier de Courcy, G.6    Brachet, P.7
  • 31
    • 0036144873 scopus 로고    scopus 로고
    • Cellular redox state and endothelial dysfunction in mildly hyperhomocysteinemic cystathionine beta-synthase-deficient mice
    • Weiss N., Heydrick S., Zhang Y.Y., Bierl C., Cap A., and Loscalzo J. Cellular redox state and endothelial dysfunction in mildly hyperhomocysteinemic cystathionine beta-synthase-deficient mice. Arterioscler. Thromb. Vasc. Biol. 22 (2002) 34-41
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 34-41
    • Weiss, N.1    Heydrick, S.2    Zhang, Y.Y.3    Bierl, C.4    Cap, A.5    Loscalzo, J.6
  • 33
    • 0028926633 scopus 로고
    • Measurement of homocyst(e)ine in the prediction of atherosclerosis
    • Fortin L.J., and Genest Jr. J. Measurement of homocyst(e)ine in the prediction of atherosclerosis. Clin. Biochem. 28 (1995) 155-162
    • (1995) Clin. Biochem. , vol.28 , pp. 155-162
    • Fortin, L.J.1    Genest Jr., J.2
  • 34
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Krawetz S., and Misener S. (Eds), Humana Press, Totowa
    • Rozen S., and Skaletsky H.J. Primer3 on the WWW for general users and for biologist programmers. In: Krawetz S., and Misener S. (Eds). Bioinformatics Methods and Protocols: Methods in Molecular Biology (2000), Humana Press, Totowa 365-386
    • (2000) Bioinformatics Methods and Protocols: Methods in Molecular Biology , pp. 365-386
    • Rozen, S.1    Skaletsky, H.J.2
  • 35
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29 (2001) e45
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 39
    • 34248232009 scopus 로고    scopus 로고
    • Comparison of nitrite/nitrate concentration in human plasma and serum samples measured by the enzymatic batch Griess assay, ion-pairing HPLC and ion-trap GC-MS: the importance of a correct removal of proteins in the Griess assay
    • Romitelli F., Santini S.A., Chierici E., Pitocco D., Tavazzi B., Amorini A.M., Lazzarino G., and Di Stasio E. Comparison of nitrite/nitrate concentration in human plasma and serum samples measured by the enzymatic batch Griess assay, ion-pairing HPLC and ion-trap GC-MS: the importance of a correct removal of proteins in the Griess assay. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 851 (2007) 257-267
    • (2007) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.851 , pp. 257-267
    • Romitelli, F.1    Santini, S.A.2    Chierici, E.3    Pitocco, D.4    Tavazzi, B.5    Amorini, A.M.6    Lazzarino, G.7    Di Stasio, E.8
  • 40
    • 0032031626 scopus 로고    scopus 로고
    • Intracellular but not extracellular conversion of nitroxyl anion into nitric oxide leads to stimulation of human neutrophil migration
    • Vanuffelen B.E., Van Der Zee J., De Koster B.M., Vansteveninck J., and Elferink J.G. Intracellular but not extracellular conversion of nitroxyl anion into nitric oxide leads to stimulation of human neutrophil migration. Biochem. J. 330 (1998) 719-722
    • (1998) Biochem. J. , vol.330 , pp. 719-722
    • Vanuffelen, B.E.1    Van Der Zee, J.2    De Koster, B.M.3    Vansteveninck, J.4    Elferink, J.G.5
  • 41
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • Paglia D.E., and Valentine W.N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med. 70 (1967) 158-169
    • (1967) J. Lab. Clin. Med. , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 42
    • 0020966833 scopus 로고
    • Selenium-dependent and non-selenium-dependent glutathione peroxidases in human tissue extracts
    • Carmagnol F., Sinet P.M., and Jerome H. Selenium-dependent and non-selenium-dependent glutathione peroxidases in human tissue extracts. Biochim. Biophys. Acta 759 (1983) 49-57
    • (1983) Biochim. Biophys. Acta , vol.759 , pp. 49-57
    • Carmagnol, F.1    Sinet, P.M.2    Jerome, H.3
  • 44
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 45
    • 0036775158 scopus 로고    scopus 로고
    • Heme oxygenase-1: redox regulation and role in the hepatic response to oxidative stress
    • Bauer M., and Bauer I. Heme oxygenase-1: redox regulation and role in the hepatic response to oxidative stress. Antioxid. Redox. Signal. 4 (2002) 749-758
    • (2002) Antioxid. Redox. Signal. , vol.4 , pp. 749-758
    • Bauer, M.1    Bauer, I.2
  • 46
    • 0036268227 scopus 로고    scopus 로고
    • Nitric oxide in liver diseases: friend, foe, or just passerby?
    • Hon W.M., Lee K.H., and Khoo H.E. Nitric oxide in liver diseases: friend, foe, or just passerby?. Ann. N. Y. Acad. Sci. 962 (2002) 275-295
    • (2002) Ann. N. Y. Acad. Sci. , vol.962 , pp. 275-295
    • Hon, W.M.1    Lee, K.H.2    Khoo, H.E.3
  • 47
    • 0030783147 scopus 로고    scopus 로고
    • Homocysteine as a modulator of platelet-derived growth factor action in vascular smooth muscle cells: a possible role for hydrogen peroxide
    • Nishio E., and Watanabe Y. Homocysteine as a modulator of platelet-derived growth factor action in vascular smooth muscle cells: a possible role for hydrogen peroxide. Br. J. Pharmacol. 122 (1997) 269-274
    • (1997) Br. J. Pharmacol. , vol.122 , pp. 269-274
    • Nishio, E.1    Watanabe, Y.2
  • 51
    • 33749329880 scopus 로고    scopus 로고
    • Enhanced susceptibility to arterial thrombosis in a murine model of hyperhomocysteinemia
    • Dayal S., Wilson K.M., Leo L., Arning E., Bottiglieri T., and Lentz S.R. Enhanced susceptibility to arterial thrombosis in a murine model of hyperhomocysteinemia. Blood 108 (2006) 2237-2243
    • (2006) Blood , vol.108 , pp. 2237-2243
    • Dayal, S.1    Wilson, K.M.2    Leo, L.3    Arning, E.4    Bottiglieri, T.5    Lentz, S.R.6
  • 52
    • 34548855958 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 in vivo suppresses NADPH oxidase-derived oxidative stress
    • Datla S.R., Dusting G.J., Mori T.A., Taylor C.J., Croft K.D., and Jiang F. Induction of heme oxygenase-1 in vivo suppresses NADPH oxidase-derived oxidative stress. Hypertension 50 (2007) 636-642
    • (2007) Hypertension , vol.50 , pp. 636-642
    • Datla, S.R.1    Dusting, G.J.2    Mori, T.A.3    Taylor, C.J.4    Croft, K.D.5    Jiang, F.6
  • 54
    • 33747839808 scopus 로고    scopus 로고
    • Thiol compounds metabolism in mice, rats and humans: comparative study and potential explanation of rodents protection against vascular diseases
    • Likogianni V., Janel N., Ledru A., Beaune P., Paul J.L., and Demuth K. Thiol compounds metabolism in mice, rats and humans: comparative study and potential explanation of rodents protection against vascular diseases. Clin. Chim. Acta 372 (2006) 140-146
    • (2006) Clin. Chim. Acta , vol.372 , pp. 140-146
    • Likogianni, V.1    Janel, N.2    Ledru, A.3    Beaune, P.4    Paul, J.L.5    Demuth, K.6
  • 55
    • 0030022388 scopus 로고    scopus 로고
    • Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes
    • Gaetani G.F., Ferraris A.M., Rolfo M., Mangerini R., Arena S., and Kirkman H.N. Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood 87 (1996) 1595-1599
    • (1996) Blood , vol.87 , pp. 1595-1599
    • Gaetani, G.F.1    Ferraris, A.M.2    Rolfo, M.3    Mangerini, R.4    Arena, S.5    Kirkman, H.N.6
  • 56
    • 0036855560 scopus 로고    scopus 로고
    • Regulation of catalase enzyme activity by cell signaling molecules
    • Yano S., and Yano N. Regulation of catalase enzyme activity by cell signaling molecules. Mol. Cell. Biochem. 240 (2002) 119-130
    • (2002) Mol. Cell. Biochem. , vol.240 , pp. 119-130
    • Yano, S.1    Yano, N.2
  • 57
    • 20444487720 scopus 로고    scopus 로고
    • Regulation of extracellular signal-regulated kinase by homocysteine in hippocampus
    • Robert K., Pagès C., Ledru A., Delabar J., Caboche J., and Janel N. Regulation of extracellular signal-regulated kinase by homocysteine in hippocampus. Neuroscience 133 (2005) 925-935
    • (2005) Neuroscience , vol.133 , pp. 925-935
    • Robert, K.1    Pagès, C.2    Ledru, A.3    Delabar, J.4    Caboche, J.5    Janel, N.6
  • 58
    • 33646677716 scopus 로고    scopus 로고
    • Homocysteine activates cAMP-response element binding protein in HepG2 through cAMP/PKA signaling pathway
    • Woo C.W., Siow Y.L., and K.O. Homocysteine activates cAMP-response element binding protein in HepG2 through cAMP/PKA signaling pathway. Arterioscler. Thromb. Vasc. Biol. 26 (2006) 1043-1050
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 1043-1050
    • Woo, C.W.1    Siow, Y.L.2    Karmin, O.3
  • 60
    • 31644451096 scopus 로고    scopus 로고
    • Metallothionein induction in the liver, kidney, heart and aorta of cadmium and isoproterenol treated rats
    • BobillierChaumont S., Maupoil V., and Berthelot A. Metallothionein induction in the liver, kidney, heart and aorta of cadmium and isoproterenol treated rats. J. Appl. Toxicol. 26 (2006) 47-55
    • (2006) J. Appl. Toxicol. , vol.26 , pp. 47-55
    • BobillierChaumont, S.1    Maupoil, V.2    Berthelot, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.