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Volumn 29, Issue 2, 2009, Pages 114-122

Vitamin C attenuates hypochlorite-mediated loss of paraoxonase-1 activity from human plasma

Author keywords

Antioxidants; Ascorbic acid; Cardiovascular diseases; Human; Hypochlorous acid; Lipoproteins, HDL; Paraoxonase

Indexed keywords

ARYLDIALKYLPHOSPHATASE 1; ARYLESTERASE; ASCORBIC ACID; GLUCONOLACTONASE; HIGH DENSITY LIPOPROTEIN; HYPOCHLORITE; LOW DENSITY LIPOPROTEIN; LYSINE; PHOSPHOTRIESTERASE; TOSYLCHLORAMIDE SODIUM;

EID: 61749084202     PISSN: 02715317     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nutres.2009.01.003     Document Type: Article
Times cited : (17)

References (59)
  • 1
    • 0037180771 scopus 로고    scopus 로고
    • Inflammation in atherosclerosis
    • Libby P. Inflammation in atherosclerosis. Nature 420 (2002) 868-874
    • (2002) Nature , vol.420 , pp. 868-874
    • Libby, P.1
  • 2
    • 0033973485 scopus 로고    scopus 로고
    • High density lipoprotein oxidation: in vitro susceptibility and potential in vivo consequences
    • Francis G.A. High density lipoprotein oxidation: in vitro susceptibility and potential in vivo consequences. Biochim Biophys Acta 1483 (2000) 217-235
    • (2000) Biochim Biophys Acta , vol.1483 , pp. 217-235
    • Francis, G.A.1
  • 3
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: friend and foe
    • Klebanoff S.J. Myeloperoxidase: friend and foe. J Leukoc Biol 77 (2005) 598-625
    • (2005) J Leukoc Biol , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 4
    • 4344577056 scopus 로고    scopus 로고
    • Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease
    • Zheng L., Nukuna B., Brennan M.L., Sun M., Goormastic M., Settle M., et al. Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease. J Clin Invest 114 (2004) 529-541
    • (2004) J Clin Invest , vol.114 , pp. 529-541
    • Zheng, L.1    Nukuna, B.2    Brennan, M.L.3    Sun, M.4    Goormastic, M.5    Settle, M.6
  • 5
    • 1542288310 scopus 로고    scopus 로고
    • High-density lipoprotein cholesterol and coronary heart disease
    • Young C.E., Karas R.H., and Kuvin J.T. High-density lipoprotein cholesterol and coronary heart disease. Cardiol Rev 12 (2004) 107-119
    • (2004) Cardiol Rev , vol.12 , pp. 107-119
    • Young, C.E.1    Karas, R.H.2    Kuvin, J.T.3
  • 7
    • 17644367506 scopus 로고    scopus 로고
    • Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase
    • Khersonsky O., and Tawfik D.S. Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 44 (2005) 6371-6382
    • (2005) Biochemistry , vol.44 , pp. 6371-6382
    • Khersonsky, O.1    Tawfik, D.S.2
  • 8
    • 33646202459 scopus 로고    scopus 로고
    • The catalytic histidine dyad of HDL-associated serum paraoxonase 1 (PON1) is essential for PON1-mediated inhibition of LDL oxidation and stimulation of macrophage cholesterol efflux
    • Rosenblat M., Gaidukov L., Khersonsky O., Vaya J., Oren R., Tawfik D.S., et al. The catalytic histidine dyad of HDL-associated serum paraoxonase 1 (PON1) is essential for PON1-mediated inhibition of LDL oxidation and stimulation of macrophage cholesterol efflux. J Biol Chem 281 (2006) 7657-7665
    • (2006) J Biol Chem , vol.281 , pp. 7657-7665
    • Rosenblat, M.1    Gaidukov, L.2    Khersonsky, O.3    Vaya, J.4    Oren, R.5    Tawfik, D.S.6
  • 9
    • 21244491480 scopus 로고    scopus 로고
    • Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
    • Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., and La Du B.N. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J Lipid Res 46 (2005) 1239-1247
    • (2005) J Lipid Res , vol.46 , pp. 1239-1247
    • Draganov, D.I.1    Teiber, J.F.2    Speelman, A.3    Osawa, Y.4    Sunahara, R.5    La Du, B.N.6
  • 11
    • 0001218860 scopus 로고
    • Ascorbate is an outstanding antioxidant in human blood plasma
    • Frei B., England L., and Ames B.N. Ascorbate is an outstanding antioxidant in human blood plasma. Proc Natl Acad Sci USA 86 (1989) 6377-6381
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6377-6381
    • Frei, B.1    England, L.2    Ames, B.N.3
  • 12
    • 0141864320 scopus 로고    scopus 로고
    • Vitamin C inhibits lipid oxidation in human HDL
    • Hillstrom R.J., Yacapin-Ammons A.K., and Lynch S.M. Vitamin C inhibits lipid oxidation in human HDL. J Nutr 133 (2003) 3047-3051
    • (2003) J Nutr , vol.133 , pp. 3047-3051
    • Hillstrom, R.J.1    Yacapin-Ammons, A.K.2    Lynch, S.M.3
  • 13
    • 33746832487 scopus 로고    scopus 로고
    • Vitamin C preserves the cardio-protective paraoxonase activity of high-density lipoprotein during oxidant stress
    • Calla M.S., and Lynch S.M. Vitamin C preserves the cardio-protective paraoxonase activity of high-density lipoprotein during oxidant stress. Arch Biochem Biophys 452 (2006) 129-137
    • (2006) Arch Biochem Biophys , vol.452 , pp. 129-137
    • Calla, M.S.1    Lynch, S.M.2
  • 14
    • 30544444120 scopus 로고    scopus 로고
    • Myeloperoxidase-mediated oxidation of high-density lipoproteins: fingerprints of newly recognized potential proatherogenic lipoproteins
    • Malle E., Marsche G., Panzenboeck U., and Sattler W. Myeloperoxidase-mediated oxidation of high-density lipoproteins: fingerprints of newly recognized potential proatherogenic lipoproteins. Arch Biochem Biophys 445 (2006) 245-255
    • (2006) Arch Biochem Biophys , vol.445 , pp. 245-255
    • Malle, E.1    Marsche, G.2    Panzenboeck, U.3    Sattler, W.4
  • 15
    • 0242320353 scopus 로고    scopus 로고
    • Oxidative stress does not modulate metabolic rate or skeletal muscle sympathetic activity with primary aging in adult humans
    • Bell C., Jones P.P., and Seals D.R. Oxidative stress does not modulate metabolic rate or skeletal muscle sympathetic activity with primary aging in adult humans. J Clin Endocrinol Metab 88 (2003) 4950-4954
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 4950-4954
    • Bell, C.1    Jones, P.P.2    Seals, D.R.3
  • 16
    • 21444439731 scopus 로고    scopus 로고
    • Vitamin C: from popular food supplement to specific drug
    • Goldenberg H. Vitamin C: from popular food supplement to specific drug. Forum Nutr 56 (2003) 42-45
    • (2003) Forum Nutr , vol.56 , pp. 42-45
    • Goldenberg, H.1
  • 17
  • 19
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83 (1977) 346-356
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 20
    • 71849104860 scopus 로고
    • Protein estimation with the Folin phenol reagent
    • Lowry O., Rosebrough N., Farr A., and Randall R. Protein estimation with the Folin phenol reagent. J Biol Chem 193 (1951) 265-275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.1    Rosebrough, N.2    Farr, A.3    Randall, R.4
  • 21
    • 0030669763 scopus 로고    scopus 로고
    • Effects of reagent and enzymatically generated hypochlorite on physicochemical and metabolic properties of high density lipoproteins
    • Panzenboeck U., Raitmayer S., Reicher H., Lindner H., Glatter O., Malle E., et al. Effects of reagent and enzymatically generated hypochlorite on physicochemical and metabolic properties of high density lipoproteins. J Biol Chem 272 (1997) 29711-29720
    • (1997) J Biol Chem , vol.272 , pp. 29711-29720
    • Panzenboeck, U.1    Raitmayer, S.2    Reicher, H.3    Lindner, H.4    Glatter, O.5    Malle, E.6
  • 22
    • 0032966768 scopus 로고    scopus 로고
    • Hypochlorite modification of high density lipoprotein: effects on cholesterol efflux from J774 macrophages
    • Bergt C., Reicher H., Malle E., and Sattler W. Hypochlorite modification of high density lipoprotein: effects on cholesterol efflux from J774 macrophages. FEBS Lett 452 (1999) 295-300
    • (1999) FEBS Lett , vol.452 , pp. 295-300
    • Bergt, C.1    Reicher, H.2    Malle, E.3    Sattler, W.4
  • 23
    • 0034162772 scopus 로고    scopus 로고
    • Vitamin C protects against and reverses specific hypochlorous acid- and chloramine-dependent modifications of low-density lipoprotein
    • Carr A.C., Tijerina T., and Frei B. Vitamin C protects against and reverses specific hypochlorous acid- and chloramine-dependent modifications of low-density lipoprotein. Biochem J 346 (2000) 491-499
    • (2000) Biochem J , vol.346 , pp. 491-499
    • Carr, A.C.1    Tijerina, T.2    Frei, B.3
  • 24
    • 45849125708 scopus 로고    scopus 로고
    • Hypochlorite-modified high-density lipoprotein acts as a sink for myeloperoxidase in vitro
    • Marsche G., Furtmuller P.G., Obinger C., Sattler W., and Malle E. Hypochlorite-modified high-density lipoprotein acts as a sink for myeloperoxidase in vitro. Cardiovasc Res 79 (2008) 187-194
    • (2008) Cardiovasc Res , vol.79 , pp. 187-194
    • Marsche, G.1    Furtmuller, P.G.2    Obinger, C.3    Sattler, W.4    Malle, E.5
  • 26
    • 0028233559 scopus 로고
    • Assays for the chlorination activity of myeloperoxidase
    • Kettle A.J., and Winterbourn C.C. Assays for the chlorination activity of myeloperoxidase. Methods Enzymol 233 (1994) 502-512
    • (1994) Methods Enzymol , vol.233 , pp. 502-512
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 27
  • 28
    • 0030827926 scopus 로고    scopus 로고
    • Effect of the molecular polymorphisms of human paraoxonase (PON1) on the rate of hydrolysis of paraoxon
    • Mackness B., Mackness M.I., Arrol S., Turkie W., and Durrington P.N. Effect of the molecular polymorphisms of human paraoxonase (PON1) on the rate of hydrolysis of paraoxon. Br J Pharmacol 122 (1997) 265-268
    • (1997) Br J Pharmacol , vol.122 , pp. 265-268
    • Mackness, B.1    Mackness, M.I.2    Arrol, S.3    Turkie, W.4    Durrington, P.N.5
  • 29
    • 17344369784 scopus 로고    scopus 로고
    • Paraoxonase active site required for protection against LDL oxidation involves its free sulfhydryl group and is different from that required for its arylesterase/paraoxonase activities: selective action of human paraoxonase allozymes Q and R
    • Aviram M., Billecke S., Sorenson R., Bisgaier C., Newton R., Rosenblat M., et al. Paraoxonase active site required for protection against LDL oxidation involves its free sulfhydryl group and is different from that required for its arylesterase/paraoxonase activities: selective action of human paraoxonase allozymes Q and R. Arterioscler Thromb Vasc Biol 18 (1998) 1617-1624
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 1617-1624
    • Aviram, M.1    Billecke, S.2    Sorenson, R.3    Bisgaier, C.4    Newton, R.5    Rosenblat, M.6
  • 30
    • 30444432098 scopus 로고    scopus 로고
    • Chromogenic and fluorogenic assays for the lactonase activity of serum paraoxonases
    • Khersonsky O., and Tawfik D.S. Chromogenic and fluorogenic assays for the lactonase activity of serum paraoxonases. Chembiochem 7 (2006) 49-53
    • (2006) Chembiochem , vol.7 , pp. 49-53
    • Khersonsky, O.1    Tawfik, D.S.2
  • 31
    • 33748546980 scopus 로고    scopus 로고
    • A long and winding road: defining the biological role and clinical importance of paraoxonases
    • James R.W. A long and winding road: defining the biological role and clinical importance of paraoxonases. Clin Chem Lab Med 44 (2006) 1052-1059
    • (2006) Clin Chem Lab Med , vol.44 , pp. 1052-1059
    • James, R.W.1
  • 32
    • 0343475105 scopus 로고    scopus 로고
    • Kinetics of tryptophan oxidation in plasma lipoproteins by myeloperoxidase-generated HOCl
    • Jerlich A., Hammel M., Nigon F., Chapman M.J., and Schaur R.J. Kinetics of tryptophan oxidation in plasma lipoproteins by myeloperoxidase-generated HOCl. Eur J Biochem 267 (2000) 4137-4143
    • (2000) Eur J Biochem , vol.267 , pp. 4137-4143
    • Jerlich, A.1    Hammel, M.2    Nigon, F.3    Chapman, M.J.4    Schaur, R.J.5
  • 33
    • 0344875683 scopus 로고    scopus 로고
    • Oxidative inactivation of paraoxonase 1, an antioxidant protein, and its effect on antioxidant action
    • Nguyen S.D., and Sok D.E. Oxidative inactivation of paraoxonase 1, an antioxidant protein, and its effect on antioxidant action. Free Radic Res 37 (2003) 1319-1330
    • (2003) Free Radic Res , vol.37 , pp. 1319-1330
    • Nguyen, S.D.1    Sok, D.E.2
  • 34
    • 0347917079 scopus 로고    scopus 로고
    • Hypochlorous acid and low serum paraoxonase activity in haemodialysis patients: an in vitro study
    • Sutherland W.H., de Jong S.A., and Walker R.J. Hypochlorous acid and low serum paraoxonase activity in haemodialysis patients: an in vitro study. Nephrol Dial Transplant 19 (2004) 75-82
    • (2004) Nephrol Dial Transplant , vol.19 , pp. 75-82
    • Sutherland, W.H.1    de Jong, S.A.2    Walker, R.J.3
  • 35
    • 34247363573 scopus 로고    scopus 로고
    • HDL oxidation compromises its influence on paraoxonase-1 secretion and its capacity to modulate enzyme activity
    • Deakin S., Moren X., and James R.W. HDL oxidation compromises its influence on paraoxonase-1 secretion and its capacity to modulate enzyme activity. Arterioscler Thromb Vasc Biol 27 (2007) 1146-1152
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 1146-1152
    • Deakin, S.1    Moren, X.2    James, R.W.3
  • 36
    • 53849141485 scopus 로고    scopus 로고
    • Hypochlorous acid is a potent inactivator of human plasminogen at concentrations secreted by activated granulocytes
    • Gugliucci A. Hypochlorous acid is a potent inactivator of human plasminogen at concentrations secreted by activated granulocytes. Clin Chem Lab Med 46 (2008) 1403-1409
    • (2008) Clin Chem Lab Med , vol.46 , pp. 1403-1409
    • Gugliucci, A.1
  • 37
    • 0028885708 scopus 로고
    • Human suction blister interstitial fluid prevents metal ion-dependent oxidation of low density lipoprotein by macrophages and in cell-free systems
    • Dabbagh A.J., and Frei B. Human suction blister interstitial fluid prevents metal ion-dependent oxidation of low density lipoprotein by macrophages and in cell-free systems. J Clin Invest 96 (1995) 1958-1966
    • (1995) J Clin Invest , vol.96 , pp. 1958-1966
    • Dabbagh, A.J.1    Frei, B.2
  • 39
    • 0027416685 scopus 로고
    • Antioxidant protection against hypochlorous acid in human plasma
    • Hu M.L., Louie S., Cross C.E., Motchnik P., and Halliwell B. Antioxidant protection against hypochlorous acid in human plasma. J Lab Clin Med 121 (1993) 257-262
    • (1993) J Lab Clin Med , vol.121 , pp. 257-262
    • Hu, M.L.1    Louie, S.2    Cross, C.E.3    Motchnik, P.4    Halliwell, B.5
  • 40
    • 0035282618 scopus 로고    scopus 로고
    • Relative reactivities of N-chloramines and hypochlorous acid with human plasma constituents
    • Carr A.C., Hawkins C.L., Thomas S.R., Stocker R., and Frei B. Relative reactivities of N-chloramines and hypochlorous acid with human plasma constituents. Free Radic Biol Med 30 (2001) 526-536
    • (2001) Free Radic Biol Med , vol.30 , pp. 526-536
    • Carr, A.C.1    Hawkins, C.L.2    Thomas, S.R.3    Stocker, R.4    Frei, B.5
  • 41
    • 0018566269 scopus 로고
    • The determination of lipids and proteins in suction blister fluid
    • Vermeer B.J., Reman F.C., and van Gent C.M. The determination of lipids and proteins in suction blister fluid. J Invest Dermatol 73 (1979) 303-305
    • (1979) J Invest Dermatol , vol.73 , pp. 303-305
    • Vermeer, B.J.1    Reman, F.C.2    van Gent, C.M.3
  • 42
  • 44
    • 33644909215 scopus 로고    scopus 로고
    • Lipoprotein profiles in plasma and interstitial fluid analyzed with an automated gel-filtration system
    • Parini P., Johansson L., Broijersen A., Angelin B., and Rudling M. Lipoprotein profiles in plasma and interstitial fluid analyzed with an automated gel-filtration system. Eur J Clin Invest 36 (2006) 98-104
    • (2006) Eur J Clin Invest , vol.36 , pp. 98-104
    • Parini, P.1    Johansson, L.2    Broijersen, A.3    Angelin, B.4    Rudling, M.5
  • 45
    • 0020702109 scopus 로고
    • Assessment of chlorination by human neutrophils
    • Foote C.S., Goyne T.E., and Lehrer R.I. Assessment of chlorination by human neutrophils. Nature 301 (1983) 715-716
    • (1983) Nature , vol.301 , pp. 715-716
    • Foote, C.S.1    Goyne, T.E.2    Lehrer, R.I.3
  • 46
    • 0019988650 scopus 로고
    • Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation
    • Weiss S.J., Klein R., Slivka A., and Wei M. Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J Clin Invest 70 (1982) 598-607
    • (1982) J Clin Invest , vol.70 , pp. 598-607
    • Weiss, S.J.1    Klein, R.2    Slivka, A.3    Wei, M.4
  • 47
    • 16244419437 scopus 로고    scopus 로고
    • Leukocytosis and ischemic vascular disease morbidity and mortality: is it time to intervene?
    • Coller B.S. Leukocytosis and ischemic vascular disease morbidity and mortality: is it time to intervene?. Arterioscler Thromb Vasc Biol 25 (2005) 658-670
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 658-670
    • Coller, B.S.1
  • 48
    • 40949127806 scopus 로고    scopus 로고
    • Relationship of paraoxonase 1 (PON1) gene polymorphisms and functional activity with systemic oxidative stress and cardiovascular risk
    • Bhattacharyya T., Nicholls S.J., Topol E.J., Zhang R., Yang X., Schmitt D., et al. Relationship of paraoxonase 1 (PON1) gene polymorphisms and functional activity with systemic oxidative stress and cardiovascular risk. JAMA 299 (2008) 1265-1276
    • (2008) JAMA , vol.299 , pp. 1265-1276
    • Bhattacharyya, T.1    Nicholls, S.J.2    Topol, E.J.3    Zhang, R.4    Yang, X.5    Schmitt, D.6
  • 49
    • 46549085029 scopus 로고    scopus 로고
    • Paraoxonase and arylesterase activities in untreated dipper and non-dipper hypertensive patients
    • Yildiz A., Gur M., Demirbag R., Yilmaz R., Akyol S., Aslan M., et al. Paraoxonase and arylesterase activities in untreated dipper and non-dipper hypertensive patients. Clin Biochem 41 (2008) 779-784
    • (2008) Clin Biochem , vol.41 , pp. 779-784
    • Yildiz, A.1    Gur, M.2    Demirbag, R.3    Yilmaz, R.4    Akyol, S.5    Aslan, M.6
  • 51
    • 55549124890 scopus 로고    scopus 로고
    • Assessment of paraoxonase activities in patients with knee osteoarthritis
    • Soran N., Altindag O., Cakir H., Celik H., Demirkol A., and Aksoy N. Assessment of paraoxonase activities in patients with knee osteoarthritis. Redox Rep 13 (2008) 194-198
    • (2008) Redox Rep , vol.13 , pp. 194-198
    • Soran, N.1    Altindag, O.2    Cakir, H.3    Celik, H.4    Demirkol, A.5    Aksoy, N.6
  • 52
    • 40849114570 scopus 로고    scopus 로고
    • Lipid peroxidation in hemodialysis patients: effect of vitamin C supplementation
    • Ferretti G., Bacchetti T., Masciangelo S., and Pallotta G. Lipid peroxidation in hemodialysis patients: effect of vitamin C supplementation. Clin Biochem 41 (2008) 381-386
    • (2008) Clin Biochem , vol.41 , pp. 381-386
    • Ferretti, G.1    Bacchetti, T.2    Masciangelo, S.3    Pallotta, G.4
  • 54
    • 0028843708 scopus 로고
    • Kinetics and mechanisms of hypochlorous acid reactions
    • Folkes L.K., Candeias L.P., and Wardman P. Kinetics and mechanisms of hypochlorous acid reactions. Arch Biochem Biophys 323 (1995) 120-126
    • (1995) Arch Biochem Biophys , vol.323 , pp. 120-126
    • Folkes, L.K.1    Candeias, L.P.2    Wardman, P.3
  • 55
    • 0036253437 scopus 로고    scopus 로고
    • Human neutrophils oxidize low-density lipoprotein by a hypochlorous acid-dependent mechanism: the role of vitamin C
    • Carr A.C., and Frei B. Human neutrophils oxidize low-density lipoprotein by a hypochlorous acid-dependent mechanism: the role of vitamin C. Biol Chem 383 (2002) 627-636
    • (2002) Biol Chem , vol.383 , pp. 627-636
    • Carr, A.C.1    Frei, B.2
  • 56
    • 0032525801 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation
    • Hawkins C.L., and Davies M.J. Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochem J 332 (1998) 617-625
    • (1998) Biochem J , vol.332 , pp. 617-625
    • Hawkins, C.L.1    Davies, M.J.2
  • 57
    • 0033151902 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation
    • Hawkins C.L., and Davies M.J. Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation. Biochem J 340 (1999) 539-548
    • (1999) Biochem J , vol.340 , pp. 539-548
    • Hawkins, C.L.1    Davies, M.J.2
  • 58
    • 0033927959 scopus 로고    scopus 로고
    • Oxidation of LDL by myeloperoxidase and reactive nitrogen species: reaction pathways and antioxidant protection
    • Carr A.C., McCall M.R., and Frei B. Oxidation of LDL by myeloperoxidase and reactive nitrogen species: reaction pathways and antioxidant protection. Arterioscler Thromb Vasc Biol 20 (2000) 1716-1723
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 1716-1723
    • Carr, A.C.1    McCall, M.R.2    Frei, B.3
  • 59
    • 0035710891 scopus 로고    scopus 로고
    • Hypochlorous acid-modified low-density lipoprotein inactivates the lysosomal protease cathepsin B: protection by ascorbic and lipoic acids
    • Carr A.C. Hypochlorous acid-modified low-density lipoprotein inactivates the lysosomal protease cathepsin B: protection by ascorbic and lipoic acids. Redox Rep 6 (2001) 343-349
    • (2001) Redox Rep , vol.6 , pp. 343-349
    • Carr, A.C.1


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