메뉴 건너뛰기




Volumn 168, Issue 1, 2003, Pages 39-48

Homocysteine strongly enhances metal-catalyzed LDL oxidation in the presence of cystine and cysteine

Author keywords

AAPH; Copper; Cysteine; Homocysteine; Iron; Low density lipoprotein; Oxidation

Indexed keywords

AZO COMPOUND; COPPER COMPLEX; CYSTEINE; CYSTINE; HISTIDINE; HOMOCYSTEINE; IRON COMPLEX; LOW DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN CHOLESTEROL; PEROXY RADICAL;

EID: 0038065631     PISSN: 00219150     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0021-9150(03)00057-1     Document Type: Article
Times cited : (41)

References (46)
  • 2
    • 0024342063 scopus 로고
    • Plasma homocysteine, a risk factor for vascular disease: Plasma levels in health, disease, and drug therapy
    • Ueland P.M., Refsum H. Plasma homocysteine, a risk factor for vascular disease: plasma levels in health, disease, and drug therapy. J. Lab. Clin. Med. 114:1989;473-501.
    • (1989) J. Lab. Clin. Med. , vol.114 , pp. 473-501
    • Ueland, P.M.1    Refsum, H.2
  • 3
    • 0029939676 scopus 로고    scopus 로고
    • Homocysteine and vascular disease
    • McCully K.S. Homocysteine and vascular disease. Nat. Med. 2:1996;386-389.
    • (1996) Nat. Med. , vol.2 , pp. 386-389
    • McCully, K.S.1
  • 4
    • 0032499024 scopus 로고    scopus 로고
    • Homocysteine and atherothrombosis
    • Welch G.N., 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
  • 6
    • 0029864947 scopus 로고    scopus 로고
    • Reduced, oxidized and protein-bound forms of homocysteine and other aminothiols in plasma comprise the redox thiol status - A possible element of the extracellular antioxidant defense system
    • Ueland P.M., Mansoor M.A., Guttormsen A.B., Muller F., Aukrust P., Refsum H., Svardal A.M. Reduced, oxidized and protein-bound forms of homocysteine and other aminothiols in plasma comprise the redox thiol status - a possible element of the extracellular antioxidant defense system. J. Nutr. 126:1996;1281s-1284s.
    • (1996) J. Nutr. , vol.126
    • Ueland, P.M.1    Mansoor, M.A.2    Guttormsen, A.B.3    Muller, F.4    Aukrust, P.5    Refsum, H.6    Svardal, A.M.7
  • 7
    • 0031748377 scopus 로고    scopus 로고
    • The redox status of aminothiols as a clue to homocysteine-induced vascular damage?
    • Koch H.G., Goebeler M., Marquardt T., Roth J., Harms E. The redox status of aminothiols as a clue to homocysteine-induced vascular damage? Eur. J. Pediatr. 157:1998;2s102-2s106.
    • (1998) Eur. J. Pediatr. , vol.157
    • Koch, H.G.1    Goebeler, M.2    Marquardt, T.3    Roth, J.4    Harms, E.5
  • 8
    • 0034023742 scopus 로고    scopus 로고
    • Homocysteine and atherothrombosis - Mechanisms for injury
    • Thambyrajah J., Townend J.N. Homocysteine and atherothrombosis - mechanisms for injury. Eur. Heart J. 21:2000;967-974.
    • (2000) Eur. Heart J. , vol.21 , pp. 967-974
    • Thambyrajah, J.1    Townend, J.N.2
  • 9
    • 0015954510 scopus 로고
    • Generation of superoxide free radical during the autoxidation of thiols
    • Misra H.P. Generation of superoxide free radical during the autoxidation of thiols. J. Biol. Chem. 249:1974;2151-2155.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2151-2155
    • Misra, H.P.1
  • 10
    • 0022749498 scopus 로고
    • Generation of hydrogen peroxide by incidental metal ion-catalyzed autooxidation of glutathione
    • Albro P.W., Corbett J.T., Schroeder J.L. Generation of hydrogen peroxide by incidental metal ion-catalyzed autooxidation of glutathione. J. Inorg. Biochem. 27:1986;191-203.
    • (1986) J. Inorg. Biochem. , vol.27 , pp. 191-203
    • Albro, P.W.1    Corbett, J.T.2    Schroeder, J.L.3
  • 11
    • 0025989783 scopus 로고
    • Human arterial endothelial cell detachment in vitro: Its promotion by homocysteine and cysteine
    • Dudman N.P., Hicks C., Wang J., Wilcken D.E. Human arterial endothelial cell detachment in vitro: its promotion by homocysteine and cysteine. Atherosclerosis. 91:1991;77-83.
    • (1991) Atherosclerosis , vol.91 , pp. 77-83
    • Dudman, N.P.1    Hicks, C.2    Wang, J.3    Wilcken, D.E.4
  • 13
    • 0034659148 scopus 로고    scopus 로고
    • The oxidative modification hypothesis of atherogenesis: An overview
    • Chisolm G.M., Steinberg D. The oxidative modification hypothesis of atherogenesis: an overview. Free Radic. Biol. Med. 28:2000;1815-1826.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1815-1826
    • Chisolm, G.M.1    Steinberg, D.2
  • 14
    • 15844407675 scopus 로고    scopus 로고
    • Ceruloplasmin enhances smooth muscle cell- and endothelial cell-mediated low density lipoprotein oxidation by a superoxide-dependent mechanism
    • Mukhopadhyay C.K., Ehrenwald E., Fox P.L. Ceruloplasmin enhances smooth muscle cell- and endothelial cell-mediated low density lipoprotein oxidation by a superoxide-dependent mechanism. J. Biol. Chem. 271:1996;14773-14778.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14773-14778
    • Mukhopadhyay, C.K.1    Ehrenwald, E.2    Fox, P.L.3
  • 15
    • 0021270874 scopus 로고
    • Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases. Role of endogenous ceruloplasmin in low density lipoprotein oxidation by human U937 monocytic cells
    • Biemond P., van Eijk H.G., Swaak A.J., Koster J.F., Ehrenwald E., Fox P.L. Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases. Role of endogenous ceruloplasmin in low density lipoprotein oxidation by human U937 monocytic cells. J. Clin. Invest. 73:1984;1576-1579.
    • (1984) J. Clin. Invest. , vol.73 , pp. 1576-1579
    • Biemond, P.1    Van Eijk, H.G.2    Swaak, A.J.3    Koster, J.F.4    Ehrenwald, E.5    Fox, P.L.6
  • 16
    • 0026474266 scopus 로고
    • Low density lipoprotein oxidation by stimulated neutrophils and ferritin
    • Abdalla D.S., Campa A., Monteiro H.P. Low density lipoprotein oxidation by stimulated neutrophils and ferritin. Atherosclerosis. 97:1992;149-159.
    • (1992) Atherosclerosis , vol.97 , pp. 149-159
    • Abdalla, D.S.1    Campa, A.2    Monteiro, H.P.3
  • 17
    • 0026526023 scopus 로고
    • Ferritin as a source of iron for oxidative damage
    • Reif D.W. Ferritin as a source of iron for oxidative damage. Free Radic. Biol. Med. 12:1992;417-427.
    • (1992) Free Radic. Biol. Med. , vol.12 , pp. 417-427
    • Reif, D.W.1
  • 18
    • 0034667888 scopus 로고    scopus 로고
    • Effect of a prolonged superoxide flux on transferrin and ferritin
    • Paul T. Effect of a prolonged superoxide flux on transferrin and ferritin. Arch. Biochem. Biophys. 382:2000;253-261.
    • (2000) Arch. Biochem. Biophys. , vol.382 , pp. 253-261
    • Paul, T.1
  • 19
    • 0031965781 scopus 로고    scopus 로고
    • Hemin binding and oxidation of lipoproteins in serum: Mechanisms and effect on the interaction of LDL with human macrophages
    • Camejo G., Halberg C., Manschik Lundin A., et al. Hemin binding and oxidation of lipoproteins in serum: mechanisms and effect on the interaction of LDL with human macrophages. J. Lipid Res. 39:1998;755-766.
    • (1998) J. Lipid Res. , vol.39 , pp. 755-766
    • Camejo, G.1    Halberg, C.2    Manschik Lundin, A.3
  • 20
    • 0023882543 scopus 로고
    • Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts
    • Silver I.A., Murrills R.J., Etherington D.J. Microelectrode studies on the acid microenvironment beneath adherent macrophages and osteoclasts. Exp. Cell Res. 175:1988;266-276.
    • (1988) Exp. Cell Res. , vol.175 , pp. 266-276
    • Silver, I.A.1    Murrills, R.J.2    Etherington, D.J.3
  • 21
    • 0030956262 scopus 로고    scopus 로고
    • Does an acidic pH explain why low density lipoprotein is oxidised in atherosclerotic lesions?
    • Leake D.S. Does an acidic pH explain why low density lipoprotein is oxidised in atherosclerotic lesions? Atherosclerosis. 129:1997;149-157.
    • (1997) Atherosclerosis , vol.129 , pp. 149-157
    • Leake, D.S.1
  • 22
    • 0025203833 scopus 로고
    • A comparison of the structure and properties of serum transferrin from 17 animal species
    • Welch S. A comparison of the structure and properties of serum transferrin from 17 animal species. Comp. Biochem. Physiol. B. 97:1990;417-427.
    • (1990) Comp. Biochem. Physiol. B. , vol.97 , pp. 417-427
    • Welch, S.1
  • 23
    • 0025744263 scopus 로고
    • Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH
    • Sipe D.M., Murphy R.F. Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH. J. Biol. Chem. 266:1991;8002-8007.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8002-8007
    • Sipe, D.M.1    Murphy, R.F.2
  • 24
    • 0028141498 scopus 로고
    • Iron released from transferrin at acidic pH can catalyse the oxidation of low density lipoprotein
    • Lamb D.J., Leake D.S. Iron released from transferrin at acidic pH can catalyse the oxidation of low density lipoprotein. FEBS Lett. 352:1994;15-18.
    • (1994) FEBS Lett. , vol.352 , pp. 15-18
    • Lamb, D.J.1    Leake, D.S.2
  • 26
    • 0028092229 scopus 로고
    • Homocysteine induces iron-catalyzed lipid peroxidation of low-density lipoprotein that is prevented by alpha-tocopherol
    • Hirano K., Ogihara T., Miki M., Yasuda H., Tamai H., Kawamura N., Mino M. Homocysteine induces iron-catalyzed lipid peroxidation of low-density lipoprotein that is prevented by alpha-tocopherol. Free Radic. Res. 21:1994;267-276.
    • (1994) Free Radic. Res. , vol.21 , pp. 267-276
    • Hirano, K.1    Ogihara, T.2    Miki, M.3    Yasuda, H.4    Tamai, H.5    Kawamura, N.6    Mino, M.7
  • 27
    • 0029005904 scopus 로고
    • Structural requirements for oxidation of low-density lipoprotein by thiols
    • Wood J.L., Graham A. Structural requirements for oxidation of low-density lipoprotein by thiols. FEBS Lett. 366:1995;75-80.
    • (1995) FEBS Lett. , vol.366 , pp. 75-80
    • Wood, J.L.1    Graham, A.2
  • 28
    • 0031127537 scopus 로고    scopus 로고
    • Physiological thiol compounds exert pro- and anti-oxidant effects, respectively, on iron- and copper-dependent oxidation of human low-density lipoprotein
    • Lynch S.M., Frei B. Physiological thiol compounds exert pro- and anti-oxidant effects, respectively, on iron- and copper-dependent oxidation of human low-density lipoprotein. Biochim. Biophys. Acta. 1345:1997;215-221.
    • (1997) Biochim. Biophys. Acta , vol.1345 , pp. 215-221
    • Lynch, S.M.1    Frei, B.2
  • 29
    • 0027142389 scopus 로고
    • Oxidation of low density lipoprotein by thiols: Superoxide-dependent and -independent mechanisms
    • Heinecke J.W., Kawamura M., Suzuki L., Chait A. Oxidation of low density lipoprotein by thiols: superoxide-dependent and -independent mechanisms. J. Lipid Res. 34:1993;2051-2061.
    • (1993) J. Lipid Res. , vol.34 , pp. 2051-2061
    • Heinecke, J.W.1    Kawamura, M.2    Suzuki, L.3    Chait, A.4
  • 30
    • 0031686455 scopus 로고    scopus 로고
    • Cellular thiol production and oxidation of low-density lipoprotein
    • Graham A. Cellular thiol production and oxidation of low-density lipoprotein. Free Radic. Res. 28:1998;611-621.
    • (1998) Free Radic. Res. , vol.28 , pp. 611-621
    • Graham, A.1
  • 31
    • 0035477031 scopus 로고    scopus 로고
    • A critical overview of the chemistry of copper-dependent low density lipoprotein oxidation: Roles of lipid hydroperoxides, alpha-tocopherol, thiols, and ceruloplasmin
    • Burkitt M.J. A critical overview of the chemistry of copper-dependent low density lipoprotein oxidation: roles of lipid hydroperoxides, alpha-tocopherol, thiols, and ceruloplasmin. Arch. Biochem. Biophys. 394:2001;117-135.
    • (2001) Arch. Biochem. Biophys. , vol.394 , pp. 117-135
    • Burkitt, M.J.1
  • 32
    • 0032797368 scopus 로고    scopus 로고
    • The effect of cyst(e)ine on the auto-oxidation of homocysteine
    • Hogg N. The effect of cyst(e)ine on the auto-oxidation of homocysteine. Free Radic. Biol. Med. 27:1999;28-33.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 28-33
    • Hogg, N.1
  • 33
    • 33745026603 scopus 로고
    • The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum
    • Havel R.J., Eder H.A.B.J.H. The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum. J. Clin. Invest. 34:1955;1345-1353.
    • (1955) J. Clin. Invest. , vol.34 , pp. 1345-1353
    • Havel, R.J.1    Eder, H.A.B.J.H.2
  • 34
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 7:1976;72248-72254.
    • (1976) Anal. Biochem. , vol.7 , pp. 72248-72254
    • Bradford, M.M.1
  • 35
    • 0028945240 scopus 로고
    • A quantitative test for copper using bicinchoninic acid
    • Brenner A.J., Harris E.D. A quantitative test for copper using bicinchoninic acid. Anal. Biochem. 226:1995;80-84.
    • (1995) Anal. Biochem. , vol.226 , pp. 80-84
    • Brenner, A.J.1    Harris, E.D.2
  • 36
    • 0018069570 scopus 로고
    • Determination of malonaldehyde precursor in tissues by thiobarbituric acid test
    • Mihara M., Uchiyama M. Determination of malonaldehyde precursor in tissues by thiobarbituric acid test. Anal. Biochem. 86:1978;271-278.
    • (1978) Anal. Biochem. , vol.86 , pp. 271-278
    • Mihara, M.1    Uchiyama, M.2
  • 37
    • 0014358088 scopus 로고
    • Electrophoretic separation of plasma lipoproteins in agarose gels
    • Noble R.P. Electrophoretic separation of plasma lipoproteins in agarose gels. J. Lipid Res. 9:1968;693-700.
    • (1968) J. Lipid Res. , vol.9 , pp. 693-700
    • Noble, R.P.1
  • 38
    • 0024584235 scopus 로고
    • A spectrophotometric assay for lipid peroxides in serum lipoproteins using a commercially available reagent
    • el Saadani M., Esterbauer H., el Sayed M., Goher M., Nassar A.Y., Jurgens G. A spectrophotometric assay for lipid peroxides in serum lipoproteins using a commercially available reagent. J. Lipid Res. 30:1989;627-630.
    • (1989) J. Lipid Res. , vol.30 , pp. 627-630
    • El Saadani, M.1    Esterbauer, H.2    El Sayed, M.3    Goher, M.4    Nassar, A.Y.5    Jurgens, G.6
  • 39
    • 0018344688 scopus 로고
    • A precise method for the determination of whole blood and plasma sulfhydryl groups
    • Ellman G., Lysko H. A precise method for the determination of whole blood and plasma sulfhydryl groups. Anal. Biochem. 93:1979;98-102.
    • (1979) Anal. Biochem. , vol.93 , pp. 98-102
    • Ellman, G.1    Lysko, H.2
  • 41
  • 42
    • 0028950523 scopus 로고
    • Reactions of copper(II)-oligopeptide complexes with hydrogen peroxide: Effects of biological reductants
    • Ueda J., Shimazu Y., Ozawa T. Reactions of copper(II)-oligopeptide complexes with hydrogen peroxide: effects of biological reductants. Free Radic. Biol. Med. 18:1995;929-933.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 929-933
    • Ueda, J.1    Shimazu, Y.2    Ozawa, T.3
  • 43
    • 0024358960 scopus 로고
    • The action of defined oxygen-centred free radicals on human low-density lipoprotein
    • Bedwell S., Dean R.T., Jessup W. The action of defined oxygen-centred free radicals on human low-density lipoprotein. Biochem. J. 262:1989;707-712.
    • (1989) Biochem. J. , vol.262 , pp. 707-712
    • Bedwell, S.1    Dean, R.T.2    Jessup, W.3
  • 44
    • 0021734783 scopus 로고
    • Selective promotion of ferrous ion-dependent lipid peroxidation in Ehrlich ascites tumor cells by histidine as compared with other amino acids
    • Winkler P., Schaur R.J., Schauenstein E. Selective promotion of ferrous ion-dependent lipid peroxidation in Ehrlich ascites tumor cells by histidine as compared with other amino acids. Biochim. Biophys. Acta. 796:1984;226-231.
    • (1984) Biochim. Biophys. Acta , vol.796 , pp. 226-231
    • Winkler, P.1    Schaur, R.J.2    Schauenstein, E.3
  • 45
    • 0032407583 scopus 로고    scopus 로고
    • Human serum, cysteine and histidine inhibit the oxidation of low density lipoprotein less at acidic pH
    • Patterson R.A., Leake D.S. Human serum, cysteine and histidine inhibit the oxidation of low density lipoprotein less at acidic pH. FEBS Lett. 434:1998;317-321.
    • (1998) FEBS Lett. , vol.434 , pp. 317-321
    • Patterson, R.A.1    Leake, D.S.2
  • 46
    • 0029891753 scopus 로고    scopus 로고
    • Effect of homocysteine on copper ion-catalyzed, azo compound-initiated, and mononuclear cell-mediated oxidative modification of low density lipoprotein
    • Halvorsen B., Brude I., Drevon C.A., Nysom J., Ose L., Christiansen E.N., Nenseter M.S. Effect of homocysteine on copper ion-catalyzed, azo compound-initiated, and mononuclear cell-mediated oxidative modification of low density lipoprotein. J. Lipid Res. 37:1996;1591-1600.
    • (1996) J. Lipid Res. , vol.37 , pp. 1591-1600
    • Halvorsen, B.1    Brude, I.2    Drevon, C.A.3    Nysom, J.4    Ose, L.5    Christiansen, E.N.6    Nenseter, M.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.