메뉴 건너뛰기




Volumn 23, Issue 3, 1997, Pages 373-384

Sensitivity of protein sulfhydryl repair enzymes to oxidative stress

Author keywords

Glutathione; Oxidative stress; Reactive oxygen species (ROS); Thiol; Thioltransferase (glutaredoxin); Thioredoxin

Indexed keywords

DITHIOL DERIVATIVE; FERROUS ION; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); REACTIVE OXYGEN METABOLITE; SCAVENGER; THIOL DERIVATIVE; THIOREDOXIN; THIOREDOXIN REDUCTASE; TRANSFERASE;

EID: 0030992028     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(97)00009-9     Document Type: Article
Times cited : (83)

References (61)
  • 1
    • 0025317268 scopus 로고
    • Glutathione: Toxicological implications
    • Reed D. J. Glutathione: Toxicological implications. Annu. Rev. Pharmacol. Toxicol. 30:1990;603-631.
    • (1990) Annu. Rev. Pharmacol. Toxicol. , vol.30 , pp. 603-631
    • Reed, D.J.1
  • 2
    • 0026560043 scopus 로고
    • Thiol depletion induces lethal cell injury in cultured cardiomyocytes
    • Dhanbhoora C. M., Babson J. R. Thiol depletion induces lethal cell injury in cultured cardiomyocytes. Arch. Biochem. Biophys. 293:1992;130-139.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 130-139
    • Dhanbhoora, C.M.1    Babson, J.R.2
  • 3
    • 0028031742 scopus 로고
    • Oxidative stress modifies the activity of cardiac sarcolemmal phospholipase C
    • Meij J. T., Suzuki S., Panagia V., Dhalla N. S. Oxidative stress modifies the activity of cardiac sarcolemmal phospholipase C. Biochim. Biophys. Acta. 1199:1994;6-12.
    • (1994) Biochim. Biophys. Acta. , vol.1199 , pp. 6-12
    • Meij, J.T.1    Suzuki, S.2    Panagia, V.3    Dhalla, N.S.4
  • 4
    • 0023867498 scopus 로고
    • S-thiolation of creatine kinase and glycogen phosphorylase b initiated by partially reduced oxygen species
    • Park E. M., Thomas J. A. S-thiolation of creatine kinase and glycogen phosphorylase b initiated by partially reduced oxygen species. Biochim. Biophys. Acta. 964:1988;151-160.
    • (1988) Biochim. Biophys. Acta. , vol.964 , pp. 151-160
    • Park, E.M.1    Thomas, J.A.2
  • 5
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • Stadtman E. R. Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences. Free Radic. Biol. Med. 9:1990;315-325.
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 6
    • 0345036072 scopus 로고
    • DNA damage related to increased hydrogen peroxide generation by hypolipemic drug-induced liver peroxisomes
    • Fahl W. E., Lalwani N. D., Watanabe T., Goel S. K., Reddy J. K. DNA damage related to increased hydrogen peroxide generation by hypolipemic drug-induced liver peroxisomes. Proc. Natl. Acad. Sci. USA. 81:1984;7827-7830.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7827-7830
    • Fahl, W.E.1    Lalwani, N.D.2    Watanabe, T.3    Goel, S.K.4    Reddy, J.K.5
  • 7
    • 0025878908 scopus 로고
    • Masssive conversion of guanosine to 8-hydroxyguanosine in mouse liver mitochondrial DNA by administration of azidothymidine
    • Hayakawa M., Ogawa T., Sugiyama S., Tanaka M., Ozawa T. Masssive conversion of guanosine to 8-hydroxyguanosine in mouse liver mitochondrial DNA by administration of azidothymidine. Biochem. Biophys. Res. Comm. 176:1991;87-93.
    • (1991) Biochem. Biophys. Res. Comm. , vol.176 , pp. 87-93
    • Hayakawa, M.1    Ogawa, T.2    Sugiyama, S.3    Tanaka, M.4    Ozawa, T.5
  • 8
    • 0021343227 scopus 로고
    • Canine myocardial reperfusion injury. Its reduction by the combined administration of superoxide dismutase and catalase
    • Jolly S. R., Kane W. J., Bailie M. B., Abrams G. D., Lucchesi B. R. Canine myocardial reperfusion injury. Its reduction by the combined administration of superoxide dismutase and catalase. Circ. Res. 54:1984;277-285.
    • (1984) Circ. Res. , vol.54 , pp. 277-285
    • Jolly, S.R.1    Kane, W.J.2    Bailie, M.B.3    Abrams, G.D.4    Lucchesi, B.R.5
  • 9
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B., Gutteridge J. M. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219:1984;1-14.
    • (1984) Biochem. J. , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 10
    • 0025973603 scopus 로고
    • Myocardial sulfhydryl pool alterations occur during reperfusion after brief and prolonged myocardial ischemia in vivo
    • Lesnefsky E. J., Dauber I. M., Horwitz L. D. Myocardial sulfhydryl pool alterations occur during reperfusion after brief and prolonged myocardial ischemia in vivo. Circ. Res. 68:1991;605-613.
    • (1991) Circ. Res. , vol.68 , pp. 605-613
    • Lesnefsky, E.J.1    Dauber, I.M.2    Horwitz, L.D.3
  • 11
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler D. M. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu. Rev. Biochem. 54:1985;305-329.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 305-329
    • Ziegler, D.M.1
  • 12
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert H. F. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas. Mol. Biol. 63:1990;69-172.
    • (1990) Adv. Enzymol. Relat. Areas. Mol. Biol. , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 13
    • 0023874677 scopus 로고
    • Mechanisms of oxidant-mediated cell injury: The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide
    • Hyslop P. A., Hinshaw D. B., Halsey W. A., Schraufstatter I. U., Sauerheber R. D., Spragg R. G., Jackson J. H., Cochrane C. G. Mechanisms of oxidant-mediated cell injury: The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide. J. Biol. Chem. 263:1988;1665-1675.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1665-1675
    • Hyslop, P.A.1    Hinshaw, D.B.2    Halsey, W.A.3    Schraufstatter, I.U.4    Sauerheber, R.D.5    Spragg, R.G.6    Jackson, J.H.7    Cochrane, C.G.8
  • 14
    • 0025096654 scopus 로고
    • Cellular recovery of glyceraldehyde-3-phosphate dehydrogenase activity and thiol status after exposure to hydroperoxides
    • Brodie A. E., Reed D. J. Cellular recovery of glyceraldehyde-3-phosphate dehydrogenase activity and thiol status after exposure to hydroperoxides. Arch. Biochem. Biophys. 276:1990;212-218.
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 212-218
    • Brodie, A.E.1    Reed, D.J.2
  • 15
    • 0025124881 scopus 로고
    • Oxidative stress alters specific membrane currents in isolated cardiac myocytes
    • Bhatnagar A., Srivastava S. K., Szabo G. Oxidative stress alters specific membrane currents in isolated cardiac myocytes. Circ. Res. 67:1990;535-549.
    • (1990) Circ. Res. , vol.67 , pp. 535-549
    • Bhatnagar, A.1    Srivastava, S.K.2    Szabo, G.3
  • 16
    • 0023655531 scopus 로고
    • Protein damage and protein degradation by oxygen radicals: Modification of secondary and tertiary structure
    • Davies K. J. A., Delsignore M. E. Protein damage and protein degradation by oxygen radicals: Modification of secondary and tertiary structure. J. Biol. Chem. 262:1987;9908-9913.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9908-9913
    • Davies, K.J.A.1    Delsignore, M.E.2
  • 17
    • 0000696097 scopus 로고
    • Glutathione: General review of mechanism of action
    • D. Dolphin, R. Paulson, & O. Amramovic. New York: John Wiley & Sons
    • Mannervik B., Carlberg L., Larson K. Glutathione: General review of mechanism of action. Dolphin D., Paulson R., Amramovic O. Coenzymes and cofactors. Part A. III:1989;475-516 John Wiley & Sons, New York.
    • (1989) Coenzymes and cofactors , vol.3 , Issue.PART A , pp. 475-516
    • Mannervik, B.1    Carlberg, L.2    Larson, K.3
  • 18
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264:1989;13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 20
    • 0000326249 scopus 로고
    • Glutathionyl specificity of thioltransferases: Mechanistic and physiological implications
    • L. Packer, & E. Cadenas. New York: Marcel Dekker, Inc
    • Mieyal J. J., Gravina S. A., Mieyal P. A., Srinivasan U., Starke D. W. Glutathionyl specificity of thioltransferases: Mechanistic and physiological implications. Packer L., Cadenas E. Biothiols in health and disease. 1995;305-372 Marcel Dekker, Inc, New York.
    • (1995) Biothiols in health and disease , pp. 305-372
    • Mieyal, J.J.1    Gravina, S.A.2    Mieyal, P.A.3    Srinivasan, U.4    Starke, D.W.5
  • 21
    • 0026497715 scopus 로고
    • Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells
    • Fernando M. R., Nanri H., Yoshitake S., Nagata-Kuno K., Minakami S. Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells. Eur. J. Biochem. 209:1992;917-922.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 917-922
    • Fernando, M.R.1    Nanri, H.2    Yoshitake, S.3    Nagata-Kuno, K.4    Minakami, S.5
  • 22
    • 0025895933 scopus 로고
    • Thioltransferase in human red blood cells: Purification and properties
    • Mieyal J. J., Starke D. W., Gravina S. A., Dothey C., Chung J. S. Thioltransferase in human red blood cells: purification and properties. Biochemistry. 30:1991;6088-6097.
    • (1991) Biochemistry , vol.30 , pp. 6088-6097
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Dothey, C.4    Chung, J.S.5
  • 23
    • 0021096562 scopus 로고
    • An essential role of cytosolic thioltransferase in protection of pyruvate kinase from rabbit liver against oxidative inactivation
    • Axelsson K., Mannervik B. An essential role of cytosolic thioltransferase in protection of pyruvate kinase from rabbit liver against oxidative inactivation. FEBS Lett. 152:1983;114-118.
    • (1983) FEBS Lett. , vol.152 , pp. 114-118
    • Axelsson, K.1    Mannervik, B.2
  • 24
    • 0024517167 scopus 로고
    • Involvement of thioltransferase- and thioredoxin-dependent systems in the protection of "essential" thiol groups of ornithine decarboxylase
    • Flamigni F., Marmiroli S., Marcello C. M., Guarnier I. C. Involvement of thioltransferase- and thioredoxin-dependent systems in the protection of "essential" thiol groups of ornithine decarboxylase. Biochem. J. 259:1989;111-115.
    • (1989) Biochem. J. , vol.259 , pp. 111-115
    • Flamigni, F.1    Marmiroli, S.2    Marcello, C.M.3    Guarnier, I.C.4
  • 25
    • 0021284165 scopus 로고
    • Redox control of enzyme activities by thiol/disulfide exchange
    • Gilbert H. F. Redox control of enzyme activities by thiol/disulfide exchange. Meth. Enzymol. 107:1984;330-351.
    • (1984) Meth. Enzymol. , vol.107 , pp. 330-351
    • Gilbert, H.F.1
  • 26
    • 0024743065 scopus 로고
    • The mechanisms of reduction of protein mixed disulfides (dethiolation) in cardiac tissue
    • Park E., Thomas J. A. The mechanisms of reduction of protein mixed disulfides (dethiolation) in cardiac tissue. Arch. Biochem. Biophys. 274:1989;47-54.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 47-54
    • Park, E.1    Thomas, J.A.2
  • 27
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina S. A., Mieyal J. J. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry. 32:1993;3368-3376.
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 28
    • 0028037601 scopus 로고
    • Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins
    • Yoshitake S., Nanri H., Fernando M. R., Minikami S. Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J. Biochem. 116:1994;42-46.
    • (1994) J. Biochem. , vol.116 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minikami, S.4
  • 30
    • 0026600817 scopus 로고
    • Reduction of infarct size by cell-permeable oxygen metabolite scavengers
    • Lesnefsky E. J. Reduction of infarct size by cell-permeable oxygen metabolite scavengers. Free Radic. Biol. Med. 12:1992;429-446.
    • (1992) Free Radic. Biol. Med. , vol.12 , pp. 429-446
    • Lesnefsky, E.J.1
  • 31
    • 0028207246 scopus 로고
    • Exogenous intracellular, but not extracellular, iron augments myocardial oxidative injury during ischemia and reperfusion
    • Lesnefsky E. J., Ye J. Exogenous intracellular, but not extracellular, iron augments myocardial oxidative injury during ischemia and reperfusion. Am. J. Physiol. 266:1994;H384-H392.
    • (1994) Am. J. Physiol. , vol.266
    • Lesnefsky, E.J.1    Ye, J.2
  • 32
    • 0028006152 scopus 로고
    • Hydrogen peroxide cytotoxicity in cultured cardiac myocytes is iron dependent
    • Byler R. M., Sherman N. A., Wallner J. S., Horwitz L. D. Hydrogen peroxide cytotoxicity in cultured cardiac myocytes is iron dependent. Am. J. Physiol. 266:1994;H121-H127.
    • (1994) Am. J. Physiol. , vol.266
    • Byler, R.M.1    Sherman, N.A.2    Wallner, J.S.3    Horwitz, L.D.4
  • 33
    • 0027441943 scopus 로고
    • Iron and coronary heart disease. Iron makes myocardium vulnerable to ischemia [letter]
    • Sullivan J. L. Iron and coronary heart disease. Iron makes myocardium vulnerable to ischemia [letter]. Br. Med. J. 307:1993;1066-1067.
    • (1993) Br. Med. J. , vol.307 , pp. 1066-1067
    • Sullivan, J.L.1
  • 34
    • 0021111024 scopus 로고
    • Hydroxyl free radical formation from hydrogen peroxide by ferrous iron-nucleotide complexes
    • Floyd R. A., Lewis C. A. Hydroxyl free radical formation from hydrogen peroxide by ferrous iron-nucleotide complexes. Biochemistry. 22:1983;2645-2649.
    • (1983) Biochemistry. , vol.22 , pp. 2645-2649
    • Floyd, R.A.1    Lewis, C.A.2
  • 35
    • 0020808417 scopus 로고
    • Direct demonstration that ferrous ion complexes of di- and triphosphate nucleotides catalyze hydroxyl free radical formation from hydrogen peroxide
    • Floyd R. A. Direct demonstration that ferrous ion complexes of di- and triphosphate nucleotides catalyze hydroxyl free radical formation from hydrogen peroxide. Arch. Biochem. Biophys. 225:1983;263-270.
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 263-270
    • Floyd, R.A.1
  • 36
    • 0000098037 scopus 로고
    • Direct measurement of free radical generation following reperfusion of ischemic myocardium
    • Zweier J. L., Flaherty J. T., Weisfeldt M. L. Direct measurement of free radical generation following reperfusion of ischemic myocardium. Proc. Natl. Acad. Sci. USA. 84:1987;1404-1407.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1404-1407
    • Zweier, J.L.1    Flaherty, J.T.2    Weisfeldt, M.L.3
  • 37
    • 0020488534 scopus 로고
    • Rat liver thioredoxin and thioredoxin reductase: Purification and characterization
    • Luthman M., Holmgren A. Rat liver thioredoxin and thioredoxin reductase: Purification and characterization. Biochemistry. 21:1982;6628-6633.
    • (1982) Biochemistry , vol.21 , pp. 6628-6633
    • Luthman, M.1    Holmgren, A.2
  • 39
    • 0000024076 scopus 로고
    • Catalase
    • H.U. Bergmeyer. Deerfield, FL: Weinheim
    • Aebi H. E. Catalase. Bergmeyer H. U. Methods of enzymatic analysis. 1983;273-286 Weinheim, Deerfield, FL.
    • (1983) Methods of enzymatic analysis , pp. 273-286
    • Aebi, H.E.1
  • 40
    • 0022272480 scopus 로고
    • Glutathione reductase
    • A. Meister. Orlando, FL: Academic Press
    • Carlberg I., Mannervik B. Glutathione reductase. Meister A. Methods in Enzymology. 1985;485-486 Academic Press, Orlando, FL.
    • (1985) Methods in Enzymology , pp. 485-486
    • Carlberg, I.1    Mannervik, B.2
  • 41
    • 0021440787 scopus 로고
    • Purification and some properties of bovine liver cytosol thioltransferase
    • Hatakeyama M., Tanimoto Y., Mizoguchi T. Purification and some properties of bovine liver cytosol thioltransferase. J. Biochem. 95:1984;1811-1818.
    • (1984) J. Biochem. , vol.95 , pp. 1811-1818
    • Hatakeyama, M.1    Tanimoto, Y.2    Mizoguchi, T.3
  • 42
    • 0018196480 scopus 로고
    • Tissue distrubution and subcellular localization of bovine thioredoxin determined by radioimmunoassay
    • Holmgren A., Luthman M. Tissue distrubution and subcellular localization of bovine thioredoxin determined by radioimmunoassay. Biochemistry. 17:1978;4071-4077.
    • (1978) Biochemistry , vol.17 , pp. 4071-4077
    • Holmgren, A.1    Luthman, M.2
  • 43
    • 0027186030 scopus 로고
    • Purification of human thioredoxin reductase: Properties and characterization by absorption and circular dichroism spectroscopy
    • Oblong J. E., Gasdaska P. Y., Sherrill K., Powis G. Purification of human thioredoxin reductase: Properties and characterization by absorption and circular dichroism spectroscopy. Biochemistry. 32:1993;7271-7277.
    • (1993) Biochemistry , vol.32 , pp. 7271-7277
    • Oblong, J.E.1    Gasdaska, P.Y.2    Sherrill, K.3    Powis, G.4
  • 44
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin: Exceptional reactivity of insulin and suggested fuctions of thioredoxin in mechanism of hormone action
    • Holmgren A. Reduction of disulfides by thioredoxin: Exceptional reactivity of insulin and suggested fuctions of thioredoxin in mechanism of hormone action. J. Biol. Chem. 254:1979;9113-9119.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 45
    • 0021339281 scopus 로고
    • Role of cardiac glutathione transferase and of the glutathione S-conjugate export system in biotransformation of 4-hydroxynonenal in the heart
    • Ishikawa T., Sies H. Role of cardiac glutathione transferase and of the glutathione S-conjugate export system in biotransformation of 4-hydroxynonenal in the heart. J. Biol. Chem. 259:1984;3838-3843.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3838-3843
    • Ishikawa, T.1    Sies, H.2
  • 46
    • 0023694445 scopus 로고
    • Evidence for a role of iron-catalyzed oxidants in functional and metabolic stunning in the canine heart
    • Farber N. E., Vercellotti G. M., Jacob H. S., Pieper G. M., Gross G. J. Evidence for a role of iron-catalyzed oxidants in functional and metabolic stunning in the canine heart. Circ. Res. 63:1988;351-360.
    • (1988) Circ. Res. , vol.63 , pp. 351-360
    • Farber, N.E.1    Vercellotti, G.M.2    Jacob, H.S.3    Pieper, G.M.4    Gross, G.J.5
  • 47
    • 0023870433 scopus 로고
    • Evidence for direct toxic effects of free radicals on the myocardium
    • Burton K. P. Evidence for direct toxic effects of free radicals on the myocardium. Free Radic. Biol. Med. 4:1988;15-24.
    • (1988) Free Radic. Biol. Med. , vol.4 , pp. 15-24
    • Burton, K.P.1
  • 49
    • 0025274652 scopus 로고
    • Intracellular iron redistribution: An important determinant of reperfusion damage to rabbit kidneys
    • Healing G., Gower J., Fuller B., Green C. Intracellular iron redistribution: An important determinant of reperfusion damage to rabbit kidneys. Biochem. Pharm. 39:1990;1239-1245.
    • (1990) Biochem. Pharm. , vol.39 , pp. 1239-1245
    • Healing, G.1    Gower, J.2    Fuller, B.3    Green, C.4
  • 51
    • 0017700831 scopus 로고
    • Low molecular weight intracellular iron transport compounds
    • Jacobs A. Low molecular weight intracellular iron transport compounds. Blood. 50:1977;433-439.
    • (1977) Blood , vol.50 , pp. 433-439
    • Jacobs, A.1
  • 52
    • 0027291233 scopus 로고
    • Effect of pyruvate on rat heart thiol status during ischemia and hypoxia followed by reperfusion
    • Rigobello M. P., Bindoli A. Effect of pyruvate on rat heart thiol status during ischemia and hypoxia followed by reperfusion. Mol. Cell. Biochem. 122:1993;93-100.
    • (1993) Mol. Cell. Biochem. , vol.122 , pp. 93-100
    • Rigobello, M.P.1    Bindoli, A.2
  • 53
    • 0020632088 scopus 로고
    • Evidence for suitability of glutathione peroxidase as a protective enzyme: Studies of oxidative damage, renaturation, and proteolysis
    • Condell R. A., Tappel A. L. Evidence for suitability of glutathione peroxidase as a protective enzyme: Studies of oxidative damage, renaturation, and proteolysis. Arch. Biochem. Biophys. 223:1983;407-416.
    • (1983) Arch. Biochem. Biophys. , vol.223 , pp. 407-416
    • Condell, R.A.1    Tappel, A.L.2
  • 54
    • 0025096654 scopus 로고
    • Cellular recovery of glyceraldehyde-3-phosphate dehydrogenase activity and thiol status after exposure to hydroperoxides
    • Brodie A. E., Reed D. J. Cellular recovery of glyceraldehyde-3-phosphate dehydrogenase activity and thiol status after exposure to hydroperoxides. Arch. Biochem. Biophys. 276:1990;212-218.
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 212-218
    • Brodie, A.E.1    Reed, D.J.2
  • 55
    • 0026563230 scopus 로고
    • Study on human erythrocyte thioltransferase: Comparative characterization with bovine enzyme and its physiological role under oxidative stress
    • Terada T., Oshida T., Nishimura M., Maeda H., Hara T., Hosomi S., Mizoguchi T., Nishihara T. Study on human erythrocyte thioltransferase: Comparative characterization with bovine enzyme and its physiological role under oxidative stress. J. Biochem. 111:1992;688-692.
    • (1992) J. Biochem. , vol.111 , pp. 688-692
    • Terada, T.1    Oshida, T.2    Nishimura, M.3    Maeda, H.4    Hara, T.5    Hosomi, S.6    Mizoguchi, T.7    Nishihara, T.8
  • 56
    • 0021337104 scopus 로고
    • Iron-catalyzed hydroxyl radical formation: Stringent requirement for free iron coordination site
    • Graf E., Mahoney J. R., Bryant R. G., Eaton J. W. Iron-catalyzed hydroxyl radical formation: Stringent requirement for free iron coordination site. J. Biol. Chem. 259:1984;3620-3624.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3620-3624
    • Graf, E.1    Mahoney, J.R.2    Bryant, R.G.3    Eaton, J.W.4
  • 57
    • 0026086809 scopus 로고
    • Treatment with deferoxamine during ischemia improves functional and metabolic recovery and reduces reperfusion-induced oxygen radical generation in rabbit hearts
    • Williams R. E., Zweier J. L., Flaherty J. T. Treatment with deferoxamine during ischemia improves functional and metabolic recovery and reduces reperfusion-induced oxygen radical generation in rabbit hearts. Circulation. 83:1991;1006-1014.
    • (1991) Circulation , vol.83 , pp. 1006-1014
    • Williams, R.E.1    Zweier, J.L.2    Flaherty, J.T.3
  • 58
    • 0025375241 scopus 로고
    • Deferoxamine pretreatment reduces canine infarct size and oxidative injury
    • Lesnefsky E. J., Repine J. E., Horwitz L. D. Deferoxamine pretreatment reduces canine infarct size and oxidative injury. J. Pharmacol. Exper. Therap. 253:1990;1103-1109.
    • (1990) J. Pharmacol. Exper. Therap. , vol.253 , pp. 1103-1109
    • Lesnefsky, E.J.1    Repine, J.E.2    Horwitz, L.D.3
  • 59
    • 0023626933 scopus 로고
    • Improvement of post ischemic myocardial function and metabolism induced by administration of deferoxamine at the time of reflow: The role of iron in the pathogenesis of reperfusion injury
    • Ambrosio G., Zweier J. L., Jacobs W. E., Weisfeldt M. L., Flaherty J. T. Improvement of post ischemic myocardial function and metabolism induced by administration of deferoxamine at the time of reflow: the role of iron in the pathogenesis of reperfusion injury. Circulation. 76:1987;906-915.
    • (1987) Circulation , vol.76 , pp. 906-915
    • Ambrosio, G.1    Zweier, J.L.2    Jacobs, W.E.3    Weisfeldt, M.L.4    Flaherty, J.T.5
  • 61
    • 0028319278 scopus 로고
    • Responses of glutathione-related enzymes in isolated rat small intestine to Fe(2+)-EDTA-mediated oxidative stress
    • Mizoguchi T., Morita Y., Nanjo H., Terada T., Nishihara T. Responses of glutathione-related enzymes in isolated rat small intestine to Fe(2+)-EDTA-mediated oxidative stress. Biol. Pharm. Bull. 17:1994;607-611.
    • (1994) Biol. Pharm. Bull. , vol.17 , pp. 607-611
    • Mizoguchi, T.1    Morita, Y.2    Nanjo, H.3    Terada, T.4    Nishihara, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.