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Volumn 26, Issue 5-6, 1999, Pages 770-776

Thioltransferase overexpression increases resistance of MCF-7 cells to adriamycin

Author keywords

Adriamycin; Ascorbic acid; Free radicals; MCF 7 human breast tumor cells; Reactive oxygen species; Thioltransferase

Indexed keywords

ASCORBIC ACID; COMPLEMENTARY DNA; DOXORUBICIN; FREE RADICAL; THIOLTRANSFERASE; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 0033048005     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(98)00247-0     Document Type: Article
Times cited : (26)

References (45)
  • 2
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells W.W., Xu D.P., Yang Y., Rocque P.A. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J. Biol. Chem. 265:1990;15361-15364.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 3
    • 0000326249 scopus 로고
    • Glutathionyl specificity of thioltransferses: Mechanistic and physiological implications
    • L. Packer, & E. Cadenas. New York: Marcel Dekker, Inc
    • Mieyal J.J., Gravina S., Mieyal P.A., Srinivasan U., Starke D.W. Glutathionyl specificity of thioltransferses 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.2    Mieyal, P.A.3    Srinivasan, U.4    Starke, D.W.5
  • 4
    • 0026468245 scopus 로고
    • On the antioxidant effects of ascorbic acid and glutathione
    • Meister A. On the antioxidant effects of ascorbic acid and glutathione. Biochem. Pharm. 44:1992;1905-1915.
    • (1992) Biochem. Pharm. , vol.44 , pp. 1905-1915
    • Meister, A.1
  • 5
    • 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
  • 6
    • 0345500004 scopus 로고
    • Zum wirkungsmechanismus der ascorbinsäure I. Isolierung einer ascorbinsäureabhängigen DPNH-oxidase aus nebennierenmikrosomen. [On the action mechanism of ascorbic acid I. Isolation of an ascorbic acid dependent DPNH-oxidase from adrenal micosomes]
    • Kersten H., Kersten W., Staudinger H. Zum wirkungsmechanismus der ascorbinsäure I. Isolierung einer ascorbinsäureabhängigen DPNH-oxidase aus nebennierenmikrosomen. [On the action mechanism of ascorbic acid I. Isolation of an ascorbic acid dependent DPNH-oxidase from adrenal micosomes]. Biochim. Biophys. Acta. 27:1958;598-608.
    • (1958) Biochim. Biophys. Acta , vol.27 , pp. 598-608
    • Kersten, H.1    Kersten, W.2    Staudinger, H.3
  • 7
    • 0029872005 scopus 로고    scopus 로고
    • Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: Identification as glutaredoxin
    • Park J.B., Levine M. Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils Identification as glutaredoxin . Biochem. J. 315:1996;931-938.
    • (1996) Biochem. J. , vol.315 , pp. 931-938
    • Park, J.B.1    Levine, M.2
  • 8
    • 0028355875 scopus 로고
    • Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils
    • Chai Y.-C., Hendrich S., Thomas J.A. Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils. Arch. Biochem. Biophys. 310:1994;264-272.
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 264-272
    • Chai, Y.-C.1    Hendrich, S.2    Thomas, J.A.3
  • 9
    • 0026011118 scopus 로고
    • Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III: Characterization of S-thiolation and dethiolation reactions
    • Chai Y.C., Jung C.-H., Lii C.K., Ashraf S.S., Hendrich S., Wolf B., Sies H., Thomas J.A. Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III characterization of S-thiolation and dethiolation reactions . Arch. Biochem. Biophys. 284:1991;270-278.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 270-278
    • Chai, Y.C.1    Jung, C.-H.2    Lii, C.K.3    Ashraf, S.S.4    Hendrich, S.5    Wolf, B.6    Sies, H.7    Thomas, J.A.8
  • 11
    • 0031000775 scopus 로고    scopus 로고
    • PH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • Srinivasan U., Mieyal P.A., Mieyal J.J. pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry. 36:1997;3199-3206.
    • (1997) Biochemistry , vol.36 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 12
    • 0344206281 scopus 로고
    • Free radicals, ageing and disease
    • In: Halliwell, B.; Gutteridge, J. M. C., eds. New York: Oxford University Press
    • Halliwell, B. Free radicals, ageing and disease. In: Halliwell, B.; Gutteridge, J. M. C., eds. Free radicals in biology and medicine, 2nd edn. New York: Oxford University Press; 1995:489-492.
    • (1995) Free Radicals in Biology and Medicine, 2nd Edn. , pp. 489-492
    • Halliwell, B.1
  • 14
    • 0015494420 scopus 로고
    • Sterochemistry of intercalation: Interaction of daunomycin with DNA
    • Pigram W.J., Fuller W., Hamilton L.D. Sterochemistry of intercalation interaction of daunomycin with DNA . Nature New Biol. 235:1972;17-19.
    • (1972) Nature New Biol. , vol.235 , pp. 17-19
    • Pigram, W.J.1    Fuller, W.2    Hamilton, L.D.3
  • 15
    • 0022356520 scopus 로고
    • Effects of DNA intercalating agents on topoisomerase II induced DNA strand cleavage in isolated mammalian cell nuclei
    • Pommier Y., Schwartz R.E., Zwelling L.A., Kohn K.W. Effects of DNA intercalating agents on topoisomerase II induced DNA strand cleavage in isolated mammalian cell nuclei. Cancer Res. 24:1985;6406-6410.
    • (1985) Cancer Res. , vol.24 , pp. 6406-6410
    • Pommier, Y.1    Schwartz, R.E.2    Zwelling, L.A.3    Kohn, K.W.4
  • 16
    • 0019986638 scopus 로고
    • The anticancer drug Adriamycin can be actively cytotoxic without entering cells
    • Tritton T.R., Yee G. The anticancer drug Adriamycin can be actively cytotoxic without entering cells. Science. 217:1982;248-250.
    • (1982) Science , vol.217 , pp. 248-250
    • Tritton, T.R.1    Yee, G.2
  • 17
    • 0017595763 scopus 로고
    • Adriamycin stimulated superoxide formation in submitochondrial particles
    • Thayer W.S. Adriamycin stimulated superoxide formation in submitochondrial particles. Chem. Biol. Interact. 19:1977;265-278.
    • (1977) Chem. Biol. Interact. , vol.19 , pp. 265-278
    • Thayer, W.S.1
  • 18
    • 0022967083 scopus 로고
    • Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase
    • Davies K.J.A., Doroshow J.H. Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase. J. Biol. Chem. 261:1986;3060-3067.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3060-3067
    • Davies, K.J.A.1    Doroshow, J.H.2
  • 19
    • 0023028913 scopus 로고
    • Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide, and hydroxyl radical
    • Doroshow J.H., Davies K.J.A. Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide, and hydroxyl radical. J. Biol. Chem. 261:1986;3068-3074.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3068-3074
    • Doroshow, J.H.1    Davies, K.J.A.2
  • 20
    • 0024819898 scopus 로고
    • Improved cellular accumulation is characteristic of anthracyclines which retain high activity in multidrug resistant cell lines, alone or in combination with verapamil or cyclosporin A
    • Coley H.M., Twentyman P.R., Workman P. Improved cellular accumulation is characteristic of anthracyclines which retain high activity in multidrug resistant cell lines, alone or in combination with verapamil or cyclosporin A. Biochem. Pharmacol. 38:1989;4467-4475.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 4467-4475
    • Coley, H.M.1    Twentyman, P.R.2    Workman, P.3
  • 21
    • 0028128073 scopus 로고
    • Intracellular pH and the control of multidrug resistance
    • Simon S.M., Roy D., Schindler M.S. Intracellular pH and the control of multidrug resistance. Proc. Natl. Acad. Sci. USA. 91:1994;1128-1132.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1128-1132
    • Simon, S.M.1    Roy, D.2    Schindler, M.S.3
  • 22
    • 0024493715 scopus 로고
    • Differential oxygen radical susceptibility of Adriamycin-sensitive MCF-7 human breast tumor cells
    • Mimnaugh E.G., Dusre L., Atwell J., Myers C.E. Differential oxygen radical susceptibility of Adriamycin-sensitive MCF-7 human breast tumor cells. Cancer Res. 49:1989;8-15.
    • (1989) Cancer Res. , vol.49 , pp. 8-15
    • Mimnaugh, E.G.1    Dusre, L.2    Atwell, J.3    Myers, C.E.4
  • 23
    • 0026775053 scopus 로고
    • Separation of drug transport and chloride channel functions of human multidrug resistance P-glycoprotein
    • Gill D.R., Hyde S.C., Higgins C.F., Valverde M.A., Mintenig G.M., Sepulveda F.V. Separation of drug transport and chloride channel functions of human multidrug resistance P-glycoprotein. Cell. 71:1992;23-32.
    • (1992) Cell , vol.71 , pp. 23-32
    • Gill, D.R.1    Hyde, S.C.2    Higgins, C.F.3    Valverde, M.A.4    Mintenig, G.M.5    Sepulveda, F.V.6
  • 24
    • 0025268206 scopus 로고
    • Antioxidant and xenobiotic-metabolizing enzyme gene expression in Doxorubicin-resistant MCF-7 breast cancer cells
    • Akman S.A., Forrest G., Chu F.-F., Esworthy S., Doroshow J. Antioxidant and xenobiotic-metabolizing enzyme gene expression in Doxorubicin-resistant MCF-7 breast cancer cells. Cancer Res. 50:1990;1397-1402.
    • (1990) Cancer Res. , vol.50 , pp. 1397-1402
    • Akman, S.A.1    Forrest, G.2    Chu, F.-F.3    Esworthy, S.4    Doroshow, J.5
  • 25
    • 0023037085 scopus 로고
    • Overexpression of a novel anionic glutathione transferase in multidrug-resistant human breast cancer cells
    • Batist G., Tulpule A., Sinha B.K., Katki A.G., Myers C.E., Cowan K.H. Overexpression of a novel anionic glutathione transferase in multidrug-resistant human breast cancer cells. J. Biol. Chem. 261:1986;15544-15549.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15544-15549
    • Batist, G.1    Tulpule, A.2    Sinha, B.K.3    Katki, A.G.4    Myers, C.E.5    Cowan, K.H.6
  • 28
    • 0028128073 scopus 로고
    • Intracellular pH and the control of multidrug resistance
    • Simon S.M., Roy D., Schindler M.S. Intracellular pH and the control of multidrug resistance. Proc. Natl. Acad. Sci. USA. 91:1994;1128-1132.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1128-1132
    • Simon, S.M.1    Roy, D.2    Schindler, M.S.3
  • 29
    • 0024316113 scopus 로고
    • Elevation of pi class glutathione S-transferase activity in human breast cancer cells by transfection of the GST-pi gene and its effect on sensitivity to toxins
    • Moscow J.A., Townsend A.J., Cowan K.H. Elevation of pi class glutathione S-transferase activity in human breast cancer cells by transfection of the GST-pi gene and its effect on sensitivity to toxins. Mol. Pharm. 36:1989;22-28.
    • (1989) Mol. Pharm. , vol.36 , pp. 22-28
    • Moscow, J.A.1    Townsend, A.J.2    Cowan, K.H.3
  • 30
    • 0026517941 scopus 로고
    • Expression of human μ and α class glutathione S-transferases in stably transfected human breast cancer cells: Effect on cellular sensitivity to cytotoxic agents
    • Townsend A.J., Tu C.-P.D., Cowan K.H. Expression of human μ and α class glutathione S-transferases in stably transfected human breast cancer cells effect on cellular sensitivity to cytotoxic agents . Mol. Pharm. 41:1992;230-236.
    • (1992) Mol. Pharm. , vol.41 , pp. 230-236
    • Townsend, A.J.1    Tu, C.-P.D.2    Cowan, K.H.3
  • 32
    • 0025309530 scopus 로고
    • The cytomegalovirus enhancer: A pan-active control element in transgenic mice
    • Schmidt E., Christoph G., Zeller R., Leder P. The cytomegalovirus enhancer a pan-active control element in transgenic mice . Mol. Cell Biol. 10:1990;4406-4411.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 4406-4411
    • Schmidt, E.1    Christoph, G.2    Zeller, R.3    Leder, P.4
  • 33
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 34
    • 0002373902 scopus 로고
    • Amplification of RNA
    • In: Innis, M. A.; Gelfand, D. H.; Sninsky, J. J.; White, T.J., eds. San Diego: Academic Press
    • Kawasaki, E. Amplification of RNA. In: Innis, M. A.; Gelfand, D. H.; Sninsky, J. J.; White, T.J., eds. PCR protocols. San Diego: Academic Press; 1990:21-27.
    • (1990) PCR Protocols , pp. 21-27
    • Kawasaki, E.1
  • 35
    • 0023654889 scopus 로고
    • Identification and reactivity of the catalytic site of pig liver thioltransferase
    • Gan Z.-R., Wells W.W. Identification and reactivity of the catalytic site of pig liver thioltransferase. J. Biol. Chem. 262:1987;6704-6707.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6704-6707
    • Gan, Z.-R.1    Wells, W.W.2
  • 36
    • 0000630221 scopus 로고
    • Synthesis and characterization of sodium cysteine-S-sulfate monohydrate
    • Segle J.H., Johnson M.J. Synthesis and characterization of sodium cysteine-S-sulfate monohydrate. Anal. Biochem. 5:1963;330-337.
    • (1963) Anal. Biochem. , vol.5 , pp. 330-337
    • Segle, J.H.1    Johnson, M.J.2
  • 37
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: Elimination of interfering substances
    • Brown R.E., Jarvis K.L., Hyland K.J. Protein measurement using bicinchoninic acid elimination of interfering substances . Anal. Biochem. 180:1989;136-139.
    • (1989) Anal. Biochem. , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvis, K.L.2    Hyland, K.J.3
  • 39
    • 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. Tokyo. 111:1992;688-692.
    • (1992) J. Biochem. Tokyo , 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
  • 40
    • 0025823045 scopus 로고
    • Doxorubicin resistance conferred by selective enhancement of intracellular glutathione peroxidase or superoxide dismutase content in human MCF-7 breast cancer cells
    • Doroshow J., Esworthy S., Burke T., Chu F.-F., Akman S. Doxorubicin resistance conferred by selective enhancement of intracellular glutathione peroxidase or superoxide dismutase content in human MCF-7 breast cancer cells. Free Radic. Res. Commun. 12-13:1991;779-781.
    • (1991) Free Radic. Res. Commun. , vol.1213 , pp. 779-781
    • Doroshow, J.1    Esworthy, S.2    Burke, T.3    Chu, F.-F.4    Akman, S.5
  • 41
    • 0028037601 scopus 로고
    • Possible differences in regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins
    • Yoshitake S., Nanri H., Fernando M.R., Minakami S. Possible differences in regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J. Biochem. 166:1994;42-46.
    • (1994) J. Biochem. , vol.166 , pp. 42-46
    • Yoshitake, S.1    Nanri, H.2    Fernando, M.R.3    Minakami, S.4
  • 42
    • 0029051872 scopus 로고
    • Cellular levels of thioredoxin associated with drug sensitivity to cisplatin, mitomycin C, doxorubicin, and etoposide
    • Yokimozo A., Ono M., Nanri H., Makino Y., Ohga T., Wada M., Okamoto T., Yodoi J., Kuwano M., Kohno K. Cellular levels of thioredoxin associated with drug sensitivity to cisplatin, mitomycin C, doxorubicin, and etoposide. Cancer Res. 55:1995;4293-4296.
    • (1995) Cancer Res. , vol.55 , pp. 4293-4296
    • Yokimozo, A.1    Ono, M.2    Nanri, H.3    Makino, Y.4    Ohga, T.5    Wada, M.6    Okamoto, T.7    Yodoi, J.8    Kuwano, M.9    Kohno, K.10
  • 43
    • 0029778527 scopus 로고    scopus 로고
    • Transfection with human thioredoxin increases cell proliferation and a dominant-negative mutant thioredoxin reverses the transformed phenotype of human breast cancer cells
    • Gallegos A., Gasdaska J.R., Taylor C.W., Paine-Murrieta G.D., Goodman D., Gasdaska P.Y., Berggren M., Briehl M.M., Powis G. Transfection with human thioredoxin increases cell proliferation and a dominant-negative mutant thioredoxin reverses the transformed phenotype of human breast cancer cells. Cancer Res. 56:1996;5765-5770.
    • (1996) Cancer Res. , vol.56 , pp. 5765-5770
    • Gallegos, A.1    Gasdaska, J.R.2    Taylor, C.W.3    Paine-Murrieta, G.D.4    Goodman, D.5    Gasdaska, P.Y.6    Berggren, M.7    Briehl, M.M.8    Powis, G.9
  • 44
    • 0028920040 scopus 로고
    • UVB radiation-activated genes induced by transcription of and posttranslational mechanisms in rat keratinoctyes
    • Rosen C.F., Poon R., Drucker D.J. UVB radiation-activated genes induced by transcription of and posttranslational mechanisms in rat keratinoctyes. Am. J. Physiol. 268:1995;C846-C855.
    • (1995) Am. J. Physiol. , vol.268
    • Rosen, C.F.1    Poon, R.2    Drucker, D.J.3
  • 45
    • 25044438840 scopus 로고
    • Cloning, sequencing and expression of human placental thioltransferase
    • abstr.
    • Meyer E.B., Wells W.W. Cloning, sequencing and expression of human placental thioltransferase. FASEB J. 9:1995;1195. abstr.
    • (1995) FASEB J. , vol.9 , pp. 1195
    • Meyer, E.B.1    Wells, W.W.2


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