메뉴 건너뛰기




Volumn 9, Issue 7, 1998, Pages 370-379

Free radical-mediated lipid peroxidation induced by T-2 toxin in yeast (Kluyveromyces marxianus)

Author keywords

Electron paramagnetic resonance; Lipid peroxidation; Malondialdehyde; Mycotoxins; T 2 toxin; Yeast

Indexed keywords

ALPHA TOCOPHEROL; ANTIOXIDANT; HYDROXYL RADICAL; MALONALDEHYDE; MYCOTOXIN; T 2 TOXIN;

EID: 0032125125     PISSN: 09552863     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-2863(98)00031-X     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 0025369970 scopus 로고
    • The measurement and mechanism of lipid peroxidation in biological systems
    • Gutteridge J.M.C., Halliwell B. The measurement and mechanism of lipid peroxidation in biological systems. Trends Biochem. Sci. 15:1990;129-135.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 129-135
    • Gutteridge, J.M.C.1    Halliwell, B.2
  • 2
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay J.A., Linn S. DNA damage and oxygen radical toxicity. Science. 240:1988;1302-1309.
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 3
    • 0025301715 scopus 로고
    • Covalent modification reactions are marking steps in protein turnover
    • Stadtman E.R. Covalent modification reactions are marking steps in protein turnover. Biochemistry. 29:1990;6323-6331.
    • (1990) Biochemistry , vol.29 , pp. 6323-6331
    • Stadtman, E.R.1
  • 4
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman E.R. Protein oxidation and aging. Science. 257:1992;1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 5
    • 0025289049 scopus 로고
    • Free radicals, antioxidant enzymes, and carcinogenesis
    • Sun Y. Free radicals, antioxidant enzymes, and carcinogenesis. Free Rad. Biol. Med. 8:1990;583-599.
    • (1990) Free Rad. Biol. Med. , vol.8 , pp. 583-599
    • Sun, Y.1
  • 8
    • 0025165364 scopus 로고
    • NADPH-cytochrome-P-450 reductase promoted hydroxyl radical production by the iron (III)-ochratoxin A complex
    • Hasinoff B.B., Rahimtula A.D., Omar R.F. NADPH-cytochrome-P-450 reductase promoted hydroxyl radical production by the iron (III)-ochratoxin A complex. Biochim. Biophys. Acta. 1032:1990;78-81.
    • (1990) Biochim. Biophys. Acta , vol.1032 , pp. 78-81
    • Hasinoff, B.B.1    Rahimtula, A.D.2    Omar, R.F.3
  • 10
    • 0026215727 scopus 로고
    • Role of cytochrome P-450 in ochratoxin A-stimulated lipid peroxidation
    • Omar R.F., Rahimtula A.D., Bartsch H. Role of cytochrome P-450 in ochratoxin A-stimulated lipid peroxidation. J. Biochem. Toxicol. 6:1991;203-209.
    • (1991) J. Biochem. Toxicol. , vol.6 , pp. 203-209
    • Omar, R.F.1    Rahimtula, A.D.2    Bartsch, H.3
  • 11
    • 0028276212 scopus 로고
    • Structure-activity studies in E. coli strains on ochratoxin A (OTA) and its analogues implicate a genotoxic free radical and a cytotoxic thiol derivative as reactive metabolites
    • Malaveille C., Brun G., Bartsch H. Structure-activity studies in E. coli strains on ochratoxin A (OTA) and its analogues implicate a genotoxic free radical and a cytotoxic thiol derivative as reactive metabolites. Mut. Res. 307:1994;141-147.
    • (1994) Mut. Res. , vol.307 , pp. 141-147
    • Malaveille, C.1    Brun, G.2    Bartsch, H.3
  • 12
    • 0028065122 scopus 로고
    • Modulation of ochratoxin-produced genotoxicity in mice by vitamin C
    • Bose S., Sinha S.P. Modulation of ochratoxin-produced genotoxicity in mice by vitamin C. Food Chem. Toxicol. 32:1994;533-537.
    • (1994) Food Chem. Toxicol. , vol.32 , pp. 533-537
    • Bose, S.1    Sinha, S.P.2
  • 14
    • 0029959825 scopus 로고    scopus 로고
    • Free radical generation as induced by ochratoxin A and its analogs in bacteria (Bacillus brevis)
    • Hoehler D., Marquardt R.R., McIntosh A.R., Xiao H. Free radical generation as induced by ochratoxin A and its analogs in bacteria (Bacillus brevis). J. Biol. Chem. 271:1996;27388-27394.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27388-27394
    • Hoehler, D.1    Marquardt, R.R.2    McIntosh, A.R.3    Xiao, H.4
  • 15
    • 0030926268 scopus 로고    scopus 로고
    • Induction of free radicals in hepatocytes, mitochondria and microsomes of rats by ochratoxin A and its analogs
    • Hoehler D., Marquardt R.R., McIntosh A.R., Hatch G.M. Induction of free radicals in hepatocytes, mitochondria and microsomes of rats by ochratoxin A and its analogs. Biochim. Biophys. Acta. 1357:1997;225-233.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 225-233
    • Hoehler, D.1    Marquardt, R.R.2    McIntosh, A.R.3    Hatch, G.M.4
  • 16
    • 84994997942 scopus 로고    scopus 로고
    • Protective effect of antioxidants against free radical-mediated lipid peroxidation induced by DON or T-2 toxin
    • Rizzo, A.F., Atroshi, F., Ahotupa, M., Sankari, S., and Elovaara, E. Protective effect of antioxidants against free radical-mediated lipid peroxidation induced by DON or T-2 toxin. J. Vet. Med. 41, 81-90.
    • J. Vet. Med. , vol.41 , pp. 81-90
    • Rizzo, A.F.1    Atroshi, F.2    Ahotupa, M.3    Sankari, S.4    Elovaara, E.5
  • 17
    • 0028048598 scopus 로고
    • Structure-activity relationships and interactions among trichothecene mycotoxins as assessed by yeast bioassay
    • Madhyastha M.S., Marquardt R.R., Abramson D. Structure-activity relationships and interactions among trichothecene mycotoxins as assessed by yeast bioassay. Toxicon. 32:1994;1147-1152.
    • (1994) Toxicon , vol.32 , pp. 1147-1152
    • Madhyastha, M.S.1    Marquardt, R.R.2    Abramson, D.3
  • 19
    • 0000475970 scopus 로고
    • Effects of different cereal and oilseed substrates on the growth and production of toxins by Aspergillus alutaceus and Penicillium verrucosum
    • Madhyastha M.S., Marquardt R.R., Frohlich A.A., Platford G., Abramson D. Effects of different cereal and oilseed substrates on the growth and production of toxins by Aspergillus alutaceus and Penicillium verrucosum. J. Agric. Food Chem. 38:1990;1506-1510.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1506-1510
    • Madhyastha, M.S.1    Marquardt, R.R.2    Frohlich, A.A.3    Platford, G.4    Abramson, D.5
  • 21
    • 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. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0025472731 scopus 로고
    • High performance liquid chromatographic analysis of the malondialdehyde content of chicken liver
    • Squires E.J. High performance liquid chromatographic analysis of the malondialdehyde content of chicken liver. Poultry Sci. 69:1990;1371-1376.
    • (1990) Poultry Sci. , vol.69 , pp. 1371-1376
    • Squires, E.J.1
  • 23
    • 0019587427 scopus 로고
    • Determination of TBA number by high performance liquid chromatography
    • Kakuda Y., Stanley D.W., van de Voort F.R. Determination of TBA number by high performance liquid chromatography. J. Am. Oil Chem. Soc. 58:1981;773-775.
    • (1981) J. Am. Oil Chem. Soc. , vol.58 , pp. 773-775
    • Kakuda, Y.1    Stanley, D.W.2    Van De Voort, F.R.3
  • 25
    • 0020048321 scopus 로고
    • Production of hydroxyl radical by decomposition of superoxide spin trapped adducts
    • Finkelstein E., Rosen G.M., Rauckman E.J. Production of hydroxyl radical by decomposition of superoxide spin trapped adducts. Mol. Pharmacol. 21:1982;262-265.
    • (1982) Mol. Pharmacol. , vol.21 , pp. 262-265
    • Finkelstein, E.1    Rosen, G.M.2    Rauckman, E.J.3
  • 26
    • 0022571141 scopus 로고
    • Hydroxyl radical formation as a result of the interaction between primaquine and reduced pyridine nucleotides
    • Augusto O., Weingrill C.L.V., Schreier S., Amemiya H. Hydroxyl radical formation as a result of the interaction between primaquine and reduced pyridine nucleotides. Arch. Biochem. Biophys. 244:1986;147-155.
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 147-155
    • Augusto, O.1    Weingrill, C.L.V.2    Schreier, S.3    Amemiya, H.4
  • 27
    • 0027957717 scopus 로고
    • A kinetic approach to the selection of a sensitive spin trapping system for the detection of hydroxyl radical
    • Pou S., Ramos C.L., Gladwell T., Renks E., Centra M., Young D., Cohen M.S., Rosen G.M. A kinetic approach to the selection of a sensitive spin trapping system for the detection of hydroxyl radical. Anal. Biochem. 217:1994;76-83.
    • (1994) Anal. Biochem. , vol.217 , pp. 76-83
    • Pou, S.1    Ramos, C.L.2    Gladwell, T.3    Renks, E.4    Centra, M.5    Young, D.6    Cohen, M.S.7    Rosen, G.M.8
  • 29
    • 0027010643 scopus 로고
    • Trichothecene synergism, additivity, and antagonism: The significance of the maximally quiescent ratio
    • Koshinsky H.A., Khachatourians G.G. Trichothecene synergism, additivity, and antagonism The significance of the maximally quiescent ratio . Natural Toxins. 1:1992;38-47.
    • (1992) Natural Toxins , vol.1 , pp. 38-47
    • Koshinsky, H.A.1    Khachatourians, G.G.2
  • 30
    • 0023618253 scopus 로고
    • Role of lipid peroxidation in toxicity of T-2 toxin
    • Schuster A., Hunder G., Fichtl B., Forth W. Role of lipid peroxidation in toxicity of T-2 toxin. Toxicon. 25:1987;1321-1328.
    • (1987) Toxicon , vol.25 , pp. 1321-1328
    • Schuster, A.1    Hunder, G.2    Fichtl, B.3    Forth, W.4
  • 32
    • 0027366166 scopus 로고
    • A comparative evaluation of thiobarbituric acid methods for the determination of malondialdehyde in biological materials
    • Draper H.H., Squires E.J., Mahmoodi H., Wu J., Agarwal S., Hadley M. A comparative evaluation of thiobarbituric acid methods for the determination of malondialdehyde in biological materials. Free Radic. Biol. Med. 15:1993;353-363.
    • (1993) Free Radic. Biol. Med. , vol.15 , pp. 353-363
    • Draper, H.H.1    Squires, E.J.2    Mahmoodi, H.3    Wu, J.4    Agarwal, S.5    Hadley, M.6
  • 33
    • 0020684032 scopus 로고
    • Determination of malonaldehyde in biological materials by high-pressure liquid chromatography
    • Bird R.P., Hung S.O., Hadley M., Draper H.H. Determination of malonaldehyde in biological materials by high-pressure liquid chromatography. Anal. Biochem. 128:1983;240-244.
    • (1983) Anal. Biochem. , vol.128 , pp. 240-244
    • Bird, R.P.1    Hung, S.O.2    Hadley, M.3    Draper, H.H.4
  • 34
    • 0000096190 scopus 로고
    • The thiobarbituric acid reaction and the autooxidation of polyunsaturated fatty acids methylesters
    • Dahle L.K., Hil L.G., Holman R.I. The thiobarbituric acid reaction and the autooxidation of polyunsaturated fatty acids methylesters. Arch. Biochem. Biophys. 98:1962;253-261.
    • (1962) Arch. Biochem. Biophys. , vol.98 , pp. 253-261
    • Dahle, L.K.1    Hil, L.G.2    Holman, R.I.3
  • 35
    • 0024378751 scopus 로고
    • Nutritional regulation of yeast Δ-9 fatty acid desaturase activity
    • Bossi M.A., Martin C.E. Nutritional regulation of yeast Δ-9 fatty acid desaturase activity. J. Bacteriol. 171:1989;6409-6413.
    • (1989) J. Bacteriol. , vol.171 , pp. 6409-6413
    • Bossi, M.A.1    Martin, C.E.2
  • 36
    • 0025885256 scopus 로고
    • Incorporation of unsaturated fatty acids by Saccharomyces cerevisiae: Conservation of fatty-acyl saturation in phosphatidylinositol
    • Pilkington B.J., Rose A.H. Incorporation of unsaturated fatty acids by Saccharomyces cerevisiae Conservation of fatty-acyl saturation in phosphatidylinositol . Yeast. 7:1991;489-494.
    • (1991) Yeast , vol.7 , pp. 489-494
    • Pilkington, B.J.1    Rose, A.H.2
  • 37
    • 0021246303 scopus 로고
    • Spin-trapping of free radicals formed during in vitro and in vivo metabolism of 3-methylindole
    • Kubow S., Janzen E.G., Bray T.M. Spin-trapping of free radicals formed during in vitro and in vivo metabolism of 3-methylindole. J. Biol. Chem. 259:1984;4447-4451.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4447-4451
    • Kubow, S.1    Janzen, E.G.2    Bray, T.M.3
  • 38
    • 0014340106 scopus 로고
    • Will antioxidant nutrients slow aging processes?
    • Tappel A.L. Will antioxidant nutrients slow aging processes? Geriatrics. 23:1968;97-105.
    • (1968) Geriatrics , vol.23 , pp. 97-105
    • Tappel, A.L.1
  • 39
    • 0019464939 scopus 로고
    • Vitamin C and iron
    • Nienhuis A.W. Vitamin C and iron. New Engl. J. Med. 304:1981;170-171.
    • (1981) New Engl. J. Med. , vol.304 , pp. 170-171
    • Nienhuis, A.W.1
  • 40
    • 0023144940 scopus 로고
    • Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactoferrin and transferrin promoters of hydroxyl radical generation?
    • Aruoma O.I., Halliwell B. Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactoferrin and transferrin promoters of hydroxyl radical generation? Biochem. J. 241:1987;273-278.
    • (1987) Biochem. J. , vol.241 , pp. 273-278
    • Aruoma, O.I.1    Halliwell, B.2
  • 41
    • 0020636216 scopus 로고
    • Superoxide-dependent and ascorbate dependent formation of hydroxyl radicals in the presence of copper salts: A physiologically significant reaction?
    • Rowley D.A., Halliwell B. Superoxide-dependent and ascorbate dependent formation of hydroxyl radicals in the presence of copper salts A physiologically significant reaction? Arch. Biochem. Biophys. 225:1983;279-284.
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 279-284
    • Rowley, D.A.1    Halliwell, B.2
  • 42
    • 0028595950 scopus 로고
    • Prooxidant and antioxidant effects of trolox on ferric ion-induced oxidation of erythrocyte membrane lipids
    • Ko K.M., Yick P.K., Poon M.K.T., Ip S.P. Prooxidant and antioxidant effects of trolox on ferric ion-induced oxidation of erythrocyte membrane lipids. Mol. Cell. Biochem. 141:1994;65-70.
    • (1994) Mol. Cell. Biochem. , vol.141 , pp. 65-70
    • Ko, K.M.1    Yick, P.K.2    Poon, M.K.T.3    Ip, S.P.4
  • 43
    • 0028911877 scopus 로고
    • Hydroxylation of deoxyguanosine in DNA by copper and thiols
    • Spear N., Aust S.D. Hydroxylation of deoxyguanosine in DNA by copper and thiols. Arch. Biochem. Biophys. 317:1995;142-148.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 142-148
    • Spear, N.1    Aust, S.D.2
  • 44
    • 0024552294 scopus 로고
    • Superoxide dismutase deficiency and the toxicity of the products of autooxidation of polyunsaturated fatty acids in yeast
    • Bilinski T., Litwinska J., Blaszczynski M., Bajus A. Superoxide dismutase deficiency and the toxicity of the products of autooxidation of polyunsaturated fatty acids in yeast. Biochim. Biophys. Acta. 1001:1989;102-106.
    • (1989) Biochim. Biophys. Acta , vol.1001 , pp. 102-106
    • Bilinski, T.1    Litwinska, J.2    Blaszczynski, M.3    Bajus, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.