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Volumn 48, Issue 7, 2010, Pages 1973-1979

Protective effect of lipoic acid against methotrexate-induced oxidative stress in liver mitochondria

Author keywords

Lipid peroxidation; Lipoic acid; Methotrexate; Mitochondria; Oxidative stress

Indexed keywords

CARBONYL DERIVATIVE; FREE RADICAL; GLUTATHIONE; METHOTREXATE; MITOCHONDRIAL PROTEIN; SUPEROXIDE; THIOCTIC ACID; THIOL;

EID: 77953544509     PISSN: 02786915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fct.2010.04.047     Document Type: Article
Times cited : (93)

References (52)
  • 1
    • 70350126423 scopus 로고    scopus 로고
    • Modulatory role of lipoic acid on lipopolysaccharide-induced oxidative stress in adult rat Sertoli cells in vitro
    • Aly H.A., Lightfoot D.A., El-Shemy H.A. Modulatory role of lipoic acid on lipopolysaccharide-induced oxidative stress in adult rat Sertoli cells in vitro. Chem. Biol. Interact. 2009, 182:112-118.
    • (2009) Chem. Biol. Interact. , vol.182 , pp. 112-118
    • Aly, H.A.1    Lightfoot, D.A.2    El-Shemy, H.A.3
  • 4
    • 70449431360 scopus 로고    scopus 로고
    • Antioxidant effects of natural bioactive compounds
    • Balsano C., Alisi A. Antioxidant effects of natural bioactive compounds. Curr. Pharm. Des. 2009, 15:3063-3073.
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 3063-3073
    • Balsano, C.1    Alisi, A.2
  • 5
    • 0030768236 scopus 로고    scopus 로고
    • The pharmacology of the antioxidant lipoic acid
    • Biewenga G.P., Haenen G.R., Bast A. The pharmacology of the antioxidant lipoic acid. Gen. Pharmacol. 1997, 29:315-331.
    • (1997) Gen. Pharmacol. , vol.29 , pp. 315-331
    • Biewenga, G.P.1    Haenen, G.R.2    Bast, A.3
  • 6
    • 31044455445 scopus 로고    scopus 로고
    • Redox modifications of protein-thiols: emerging roles in cell signaling
    • Biswas S., Chida A.S., Rahman I. Redox modifications of protein-thiols: emerging roles in cell signaling. Biochem. Pharmacol. 2006, 71:551-564.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 551-564
    • Biswas, S.1    Chida, A.S.2    Rahman, I.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive MTXhod for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive MTXhod for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0017872475 scopus 로고
    • Microsomal lipid peroxidation
    • Buege J.A., Aust S.D. Microsomal lipid peroxidation. Methods Enzymol. 1978, 52:302-310.
    • (1978) Methods Enzymol. , vol.52 , pp. 302-310
    • Buege, J.A.1    Aust, S.D.2
  • 10
    • 0030714553 scopus 로고    scopus 로고
    • Effect of methotrexate (MTX) on NAD(P)+ dehydrogenases of HeLa cells: malic enzyme, 2-oxoglutarate and isocitrate dehydrogenases
    • Caetano N.N., Campello A.P., Carnieri E.G., Kluppel M.L., Oliveira M.B. Effect of methotrexate (MTX) on NAD(P)+ dehydrogenases of HeLa cells: malic enzyme, 2-oxoglutarate and isocitrate dehydrogenases. Cell Biochem. Funct. 1997, 15:259-264.
    • (1997) Cell Biochem. Funct. , vol.15 , pp. 259-264
    • Caetano, N.N.1    Campello, A.P.2    Carnieri, E.G.3    Kluppel, M.L.4    Oliveira, M.B.5
  • 12
    • 33746876627 scopus 로고    scopus 로고
    • N-acetylcysteine ameliorates methotrexate-induced oxidative liver damage in rats
    • Cetinkaya A., Bulbuloglu E., Kurutas E.B., Kantarceken B. N-acetylcysteine ameliorates methotrexate-induced oxidative liver damage in rats. Med. Sci. Monit. 2006, 12:274-278.
    • (2006) Med. Sci. Monit. , vol.12 , pp. 274-278
    • Cetinkaya, A.1    Bulbuloglu, E.2    Kurutas, E.B.3    Kantarceken, B.4
  • 13
    • 0030817853 scopus 로고    scopus 로고
    • An in vitro study on methotrexate hydroxylation in rat and human liver
    • Chládek J., Martínková J., Sispera L. An in vitro study on methotrexate hydroxylation in rat and human liver. Physiol. Res. 1997, 46:371-379.
    • (1997) Physiol. Res. , vol.46 , pp. 371-379
    • Chládek, J.1    Martínková, J.2    Sispera, L.3
  • 14
    • 0025191284 scopus 로고
    • Respiratory activity of isolated rat liver mitochondria following in vitro exposure to oxygen species: a threshold study
    • Corbisier P., Raes M., Michiels C., Pigeolet E., Houbion A., Delaive E., Remacle J. Respiratory activity of isolated rat liver mitochondria following in vitro exposure to oxygen species: a threshold study. Mech. Ageing Dev. 1990, 51:249-263.
    • (1990) Mech. Ageing Dev. , vol.51 , pp. 249-263
    • Corbisier, P.1    Raes, M.2    Michiels, C.3    Pigeolet, E.4    Houbion, A.5    Delaive, E.6    Remacle, J.7
  • 15
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • Flohé L., Gunzler W.A. Assays of glutathione peroxidase. Methods Enzymol. 1984, 105:114-121.
    • (1984) Methods Enzymol. , vol.105 , pp. 114-121
    • Flohé, L.1    Gunzler, W.A.2
  • 16
    • 0021288878 scopus 로고
    • Superoxide dismutase assays
    • Flohé L., Otting F. Superoxide dismutase assays. Methods Enzymol. 1984, 105:93-104.
    • (1984) Methods Enzymol. , vol.105 , pp. 93-104
    • Flohé, L.1    Otting, F.2
  • 17
    • 0020683340 scopus 로고
    • Studies of formation and efflux of methotrexate polyglutamates with cultured hepatic cells
    • Galivan J., Balinska M. Studies of formation and efflux of methotrexate polyglutamates with cultured hepatic cells. Adv. Exp. Med. Biol. 1983, 163:235-246.
    • (1983) Adv. Exp. Med. Biol. , vol.163 , pp. 235-246
    • Galivan, J.1    Balinska, M.2
  • 18
    • 27944504099 scopus 로고    scopus 로고
    • Oxidoreduction of protein thiols in redox regulation
    • Ghezzi P. Oxidoreduction of protein thiols in redox regulation. Biochem. Soc. Trans. 2005, 33:1378-1381.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1378-1381
    • Ghezzi, P.1
  • 21
    • 0017064979 scopus 로고
    • Fluorometric method for determination of oxidized and reduced glutathione in tissues
    • Hissin P.J., Hilf R.A. Fluorometric method for determination of oxidized and reduced glutathione in tissues. Anal. Biochem. 1976, 74:214-226.
    • (1976) Anal. Biochem. , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.A.2
  • 22
    • 0032489654 scopus 로고    scopus 로고
    • Docosahexaenoic acid exhibits a potent protection of small intestine from methotrexate-induced damage in mice
    • Horie T., Nakamaru M., Masubuchi Y. Docosahexaenoic acid exhibits a potent protection of small intestine from methotrexate-induced damage in mice. Life Sci. 1998, 62:1333-1338.
    • (1998) Life Sci. , vol.62 , pp. 1333-1338
    • Horie, T.1    Nakamaru, M.2    Masubuchi, Y.3
  • 25
    • 0035207169 scopus 로고    scopus 로고
    • Folinic acid protects against suppression of growth by methotrexate in mice
    • Iqbal M.P., Sultana F., Mehboobali N., Pervez S. Folinic acid protects against suppression of growth by methotrexate in mice. Biopharm. Drug Dispos. 2001, 22:169-178.
    • (2001) Biopharm. Drug Dispos. , vol.22 , pp. 169-178
    • Iqbal, M.P.1    Sultana, F.2    Mehboobali, N.3    Pervez, S.4
  • 26
    • 0037404909 scopus 로고    scopus 로고
    • Melatonin prevents methotrexate-induced hepatorenal oxidative injury in rats
    • Jahovic N., Cevik H., Sehirli A.O., Yeĝen B.C., Sener G. Melatonin prevents methotrexate-induced hepatorenal oxidative injury in rats. J. Pineal Res. 2003, 34:282-287.
    • (2003) J. Pineal Res. , vol.34 , pp. 282-287
    • Jahovic, N.1    Cevik, H.2    Sehirli, A.O.3    Yeĝen, B.C.4    Sener, G.5
  • 27
    • 0028951190 scopus 로고
    • Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
    • Johnston J.A., Johnson E.S., Waller P.R., Varshavsky A. Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway. J. Biol. Chem. 1995, 270:8172-8178.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8172-8178
    • Johnston, J.A.1    Johnson, E.S.2    Waller, P.R.3    Varshavsky, A.4
  • 28
    • 0019486066 scopus 로고
    • Methotrexate accumulation and folate depletion in cells as a possible mechanism of chronic toxicity to the drug
    • Kamen B.A., Nylen P.A., Camitta B.M., Bertino J.R. Methotrexate accumulation and folate depletion in cells as a possible mechanism of chronic toxicity to the drug. Br. J. Haematol. 1981, 49:355-360.
    • (1981) Br. J. Haematol. , vol.49 , pp. 355-360
    • Kamen, B.A.1    Nylen, P.A.2    Camitta, B.M.3    Bertino, J.R.4
  • 29
    • 0034114574 scopus 로고    scopus 로고
    • Chemically induced dimerization of dihydrofolate reductase by a homobifunctional dimer of methotrexate
    • Kopytek S.J., Standaert R.F., Dyer J.C., Hu J.C. Chemically induced dimerization of dihydrofolate reductase by a homobifunctional dimer of methotrexate. Chem. Biol. 2000, 7:313-321.
    • (2000) Chem. Biol. , vol.7 , pp. 313-321
    • Kopytek, S.J.1    Standaert, R.F.2    Dyer, J.C.3    Hu, J.C.4
  • 31
    • 0035110952 scopus 로고    scopus 로고
    • Mitochondria: important target for drug toxicity?
    • Krähenbühl S. Mitochondria: important target for drug toxicity?. J. Hepatol. 2001, 34:334-336.
    • (2001) J. Hepatol. , vol.34 , pp. 334-336
    • Krähenbühl, S.1
  • 33
    • 0036403283 scopus 로고    scopus 로고
    • Interactions of lipoic acid radical cations with vitamins C and E analogue and hydroxycinnamic acid derivatives
    • Lu C., Liu Y. Interactions of lipoic acid radical cations with vitamins C and E analogue and hydroxycinnamic acid derivatives. Arch Biochem. Biophys. 2002, 406:78-84.
    • (2002) Arch Biochem. Biophys. , vol.406 , pp. 78-84
    • Lu, C.1    Liu, Y.2
  • 34
    • 0031305344 scopus 로고    scopus 로고
    • A microtiter plate assay for superoxide using MTT reduction method
    • Madesh M., Balasubramanian K.A. A microtiter plate assay for superoxide using MTT reduction method. Indian J. Biochem. Biophys. 1997, 34:535-539.
    • (1997) Indian J. Biochem. Biophys. , vol.34 , pp. 535-539
    • Madesh, M.1    Balasubramanian, K.A.2
  • 35
    • 0036098767 scopus 로고    scopus 로고
    • Antioxidant superoxide dismutase - a review: its function, regulation in the testis, and role in male fertility
    • Mruk D.D., Silvestrini B., Mo M.Y., Cheng C.Y. Antioxidant superoxide dismutase - a review: its function, regulation in the testis, and role in male fertility. Contraception 2002, 65:305-311.
    • (2002) Contraception , vol.65 , pp. 305-311
    • Mruk, D.D.1    Silvestrini, B.2    Mo, M.Y.3    Cheng, C.Y.4
  • 37
    • 0024595903 scopus 로고
    • Methotrexate: studies on cellular metabolism. III. - Effect on the transplasma-membrane redox activity and on ferricyanide-induced proton extrusion by HeLa cells
    • Oliveira M.B., Campello A.P., Klüppel W.L. Methotrexate: studies on cellular metabolism. III. - Effect on the transplasma-membrane redox activity and on ferricyanide-induced proton extrusion by HeLa cells. Cell Biochem. Funct. 1989, 7:135-137.
    • (1989) Cell Biochem. Funct. , vol.7 , pp. 135-137
    • Oliveira, M.B.1    Campello, A.P.2    Klüppel, W.L.3
  • 39
    • 0029909010 scopus 로고    scopus 로고
    • Neuroprotection by the metabolic antioxidant alpha-lipoic acid
    • Packer L., Tritschler H.J., Wessel K. Neuroprotection by the metabolic antioxidant alpha-lipoic acid. Free Radic. Biol. Med. 1997, 22:359-378.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 359-378
    • Packer, L.1    Tritschler, H.J.2    Wessel, K.3
  • 41
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
    • Sedlak J., Lindsay R.H. Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal. Biochem. 1968, 25:192-205.
    • (1968) Anal. Biochem. , vol.25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 42
    • 17644392112 scopus 로고    scopus 로고
    • Beneficial effects of dl-alpha-lipoic acid on cyclophosphamide-induced oxidative stress in mitochondrial fractions of rat testis
    • Selvakumar E., Prahalathan C., Mythili Y., Varalakshmi P. Beneficial effects of dl-alpha-lipoic acid on cyclophosphamide-induced oxidative stress in mitochondrial fractions of rat testis. Chem. Biol. Interact. 2005, 152:59-66.
    • (2005) Chem. Biol. Interact. , vol.152 , pp. 59-66
    • Selvakumar, E.1    Prahalathan, C.2    Mythili, Y.3    Varalakshmi, P.4
  • 43
    • 31344439942 scopus 로고    scopus 로고
    • Effect of coenzyme Q10 intake on endogenous coenzyme Q content, mitochondrial electron transport chain, antioxidative defenses, and life span of mice
    • Sohal R.S., Kamzalov S., Sumien N., Ferguson M., Rebrin I., Heinrich K.R., Forster M.J. Effect of coenzyme Q10 intake on endogenous coenzyme Q content, mitochondrial electron transport chain, antioxidative defenses, and life span of mice. Free Radic. Biol. Med. 2006, 40:480-487.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 480-487
    • Sohal, R.S.1    Kamzalov, S.2    Sumien, N.3    Ferguson, M.4    Rebrin, I.5    Heinrich, K.R.6    Forster, M.J.7
  • 44
    • 0037738907 scopus 로고    scopus 로고
    • Effects of amifostine on liver oxidative stress caused by cyclophosphamide administration to rats
    • Stankiewicz A., Skrzydlewska E., Makieła M. Effects of amifostine on liver oxidative stress caused by cyclophosphamide administration to rats. Drug Metabol. Drug Interact. 2002, 19:67-82.
    • (2002) Drug Metabol. Drug Interact. , vol.19 , pp. 67-82
    • Stankiewicz, A.1    Skrzydlewska, E.2    Makieła, M.3
  • 45
    • 0036209605 scopus 로고    scopus 로고
    • Structural determinants of fluorochemical-induced mitochondrial dysfunction
    • Starkov A.A., Wallace K.B. Structural determinants of fluorochemical-induced mitochondrial dysfunction. Toxicol. Sci. 2002, 66:244-252.
    • (2002) Toxicol. Sci. , vol.66 , pp. 244-252
    • Starkov, A.A.1    Wallace, K.B.2
  • 46
    • 0036194529 scopus 로고    scopus 로고
    • Mitochondria as a pharmacological target
    • Szewczyk A., Wojtczak L. Mitochondria as a pharmacological target. Pharmacol. Rev. 2002, 54:101-127.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 101-127
    • Szewczyk, A.1    Wojtczak, L.2
  • 48
    • 0030217848 scopus 로고    scopus 로고
    • Inhibition of Pgp activity and cell cycle-dependent chemosensitivity to doxorubicin in the multidrug-resistant LoVo human colon cancer cell line
    • Toffoli G., Corona G., Gigante M., Boiocchi M. Inhibition of Pgp activity and cell cycle-dependent chemosensitivity to doxorubicin in the multidrug-resistant LoVo human colon cancer cell line. Eur. J. Cancer 1996, 32:1591-1597.
    • (1996) Eur. J. Cancer , vol.32 , pp. 1591-1597
    • Toffoli, G.1    Corona, G.2    Gigante, M.3    Boiocchi, M.4
  • 49
  • 50
    • 65949121134 scopus 로고    scopus 로고
    • Oxidative stress and neurodegenerative diseases: a review of upstream and downstream antioxidant therapeutic options
    • Uttara B., Singh A.V., Zamboni P., Mahajan R.T. Oxidative stress and neurodegenerative diseases: a review of upstream and downstream antioxidant therapeutic options. Curr. Neuropharmacol. 2009, 7:65-74.
    • (2009) Curr. Neuropharmacol. , vol.7 , pp. 65-74
    • Uttara, B.1    Singh, A.V.2    Zamboni, P.3    Mahajan, R.T.4
  • 51
    • 0024549053 scopus 로고
    • Methotrexate: studies on cellular metabolism. II - Effects on mitochondrial oxidative metabolism and ion transport
    • Yamamoto N., Lopes L.C., Campello A.P., Klüppel M.L. Methotrexate: studies on cellular metabolism. II - Effects on mitochondrial oxidative metabolism and ion transport. Cell Biochem. Funct. 1989, 7:129-134.
    • (1989) Cell Biochem. Funct. , vol.7 , pp. 129-134
    • Yamamoto, N.1    Lopes, L.C.2    Campello, A.P.3    Klüppel, M.L.4
  • 52
    • 0026699971 scopus 로고
    • Activation of glycogenolysis by methotrexate. Influence of calcium and inhibitors of hormone action
    • Yamamoto N.S., Ishii-Iwamoto E.L., Bracht A. Activation of glycogenolysis by methotrexate. Influence of calcium and inhibitors of hormone action. Biochem. Pharmacol. 1992, 44:761-767.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 761-767
    • Yamamoto, N.S.1    Ishii-Iwamoto, E.L.2    Bracht, A.3


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