메뉴 건너뛰기




Volumn 27, Issue 11-12, 1999, Pages 1208-1218

Glutathione redox potential in response to differentiation and enzyme inducers

Author keywords

Benzyl isothiocyanate; Differentiation; Free radicals; Glutamate:cysteine ligase; Glutathione; Glutathione S transferase; NADPH:quinone reductase; Redox potential

Indexed keywords

BENZYL ISOTHIOCYANATE; BUTYRIC ACID; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0033433972     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(99)00145-8     Document Type: Article
Times cited : (316)

References (43)
  • 1
    • 0025948113 scopus 로고
    • The antioxidant response element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • Rushmore T.H., Morton M.R., Pickett C.B. The antioxidant response element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J. Biol. Chem. 266:1991;11632-11639.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 2
    • 0027318721 scopus 로고
    • Glutathione S-transferases: Gene structure and regulation of expression
    • Daniel V. Glutathione S-transferases gene structure and regulation of expression . Crit. Rev. Biochem. Molec. Biol. 28:1993;173-207.
    • (1993) Crit. Rev. Biochem. Molec. Biol. , vol.28 , pp. 173-207
    • Daniel, V.1
  • 3
    • 0028075841 scopus 로고
    • Quinone-induced oxidative stress elevates glutathione and γ-glutamylcysteine synthetase activity in rat lung epithelial L2 cells
    • Shi M.M., Kugelman A., Iwamoto T., Tian L., Forman H.J. Quinone-induced oxidative stress elevates glutathione and γ-glutamylcysteine synthetase activity in rat lung epithelial L2 cells. J. Biol. Chem. 269:1994;26512-26517.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26512-26517
    • Shi, M.M.1    Kugelman, A.2    Iwamoto, T.3    Tian, L.4    Forman, H.J.5
  • 4
    • 0028318891 scopus 로고
    • Thiol-mediated redox regulation of lymphocyte proliferation. Possible involvement of adult T cell leukemia-derived factor and glutathione in transferrin receptor expression
    • Iwata S., Hori T., Sato N., Ueda-Taniguchi Y., Yamabe T., Nakamura H., Masutani H., Yodoi J. Thiol-mediated redox regulation of lymphocyte proliferation. Possible involvement of adult T cell leukemia-derived factor and glutathione in transferrin receptor expression. J. Immunol. 152:1994;5633-5642.
    • (1994) J. Immunol. , vol.152 , pp. 5633-5642
    • Iwata, S.1    Hori, T.2    Sato, N.3    Ueda-Taniguchi, Y.4    Yamabe, T.5    Nakamura, H.6    Masutani, H.7    Yodoi, J.8
  • 5
    • 0011825635 scopus 로고    scopus 로고
    • Redox signaling and the control of cell growth and death
    • Powis G., Gasdaska J.R., Baker A. Redox signaling and the control of cell growth and death. Adv. Pharmacol. 38:1997;329-359.
    • (1997) Adv. Pharmacol. , vol.38 , pp. 329-359
    • Powis, G.1    Gasdaska, J.R.2    Baker, A.3
  • 6
    • 0027321246 scopus 로고
    • N-acetylcysteine inhibits apoptosis and decreases viral particles in HIV-chronically infected U937 cells
    • Malorni W., Rivabene R., Santini M.T., Donelli G. N-acetylcysteine inhibits apoptosis and decreases viral particles in HIV-chronically infected U937 cells. FEBS Lett. 327:1993;75-78.
    • (1993) FEBS Lett. , vol.327 , pp. 75-78
    • Malorni, W.1    Rivabene, R.2    Santini, M.T.3    Donelli, G.4
  • 7
    • 0028923398 scopus 로고
    • Effects of N-acetyl-L-cysteine on T cell apoptosis are not mediated by increased cellular glutathione
    • Jones D.P., Maellaro E., Jiang S., Slater A.F.G., Orrenius S. Effects of N-acetyl-L-cysteine on T cell apoptosis are not mediated by increased cellular glutathione. Immunmol. Lett. 45:1995;205-209.
    • (1995) Immunmol. Lett. , vol.45 , pp. 205-209
    • Jones, D.P.1    Maellaro, E.2    Jiang, S.3    Slater, A.F.G.4    Orrenius, S.5
  • 9
    • 0030041928 scopus 로고    scopus 로고
    • Retinoic acid modulation of glutathione and cysteine metabolism in chondrocytes
    • Teixeira C.C., Shapiro I.M., Hatori M., Rajpurohit R., Koch C. Retinoic acid modulation of glutathione and cysteine metabolism in chondrocytes. Biochem. J. 314:1996;21-26.
    • (1996) Biochem. J. , vol.314 , pp. 21-26
    • Teixeira, C.C.1    Shapiro, I.M.2    Hatori, M.3    Rajpurohit, R.4    Koch, C.5
  • 10
    • 0029933138 scopus 로고    scopus 로고
    • A decrease in glucose 6-phosphate dehydrogenase activity and mRNA is an early event in phorbol ester-induced differentiation of thp-1 promonocytic leukemia cells
    • Bremner T.A., D'Costa N., Dickson L.A., Asseffa A. A decrease in glucose 6-phosphate dehydrogenase activity and mRNA is an early event in phorbol ester-induced differentiation of thp-1 promonocytic leukemia cells. Life Sci. 58:1996;1015-1022.
    • (1996) Life Sci. , vol.58 , pp. 1015-1022
    • Bremner, T.A.1    D'Costa, N.2    Dickson, L.A.3    Asseffa, A.4
  • 11
    • 0024369815 scopus 로고
    • Cytosolic and microsomal glutathione S-transferase isoenzymes in normal human liver and intestinal epithelium
    • Hayes P.C., Harrison D.J., Bouchier I.A.D., McLellan L.I., Hayes J.D. Cytosolic and microsomal glutathione S-transferase isoenzymes in normal human liver and intestinal epithelium. Gut. 30:1989;854-859.
    • (1989) Gut , vol.30 , pp. 854-859
    • Hayes, P.C.1    Harrison, D.J.2    Bouchier, I.A.D.3    McLellan, L.I.4    Hayes, J.D.5
  • 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. Related Areas Molec. Biol. 63:1990;69-172.
    • (1990) Adv. Enzymol. Related Areas Molec. Biol. , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantification 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
  • 17
    • 0028923398 scopus 로고
    • Effects of N-acetyl-L-cysteine on T cell apoptosis are not mediated by increased cellular glutathione
    • Jones D.P., Maellaro E., Jiang S., Slater A.F.G., Orrenius S. Effects of N-acetyl-L-cysteine on T cell apoptosis are not mediated by increased cellular glutathione. Immunmol. Lett. 45:1995;205-209.
    • (1995) Immunmol. Lett. , vol.45 , pp. 205-209
    • Jones, D.P.1    Maellaro, E.2    Jiang, S.3    Slater, A.F.G.4    Orrenius, S.5
  • 18
    • 0021988832 scopus 로고
    • Use of digitonin fractionation to determine mitochondrial transmembrane ion distribution in cells during anoxia
    • Andersson B.S., Jones D.P. Use of digitonin fractionation to determine mitochondrial transmembrane ion distribution in cells during anoxia. Anal. Biochem. 146:1985;164-172.
    • (1985) Anal. Biochem. , vol.146 , pp. 164-172
    • Andersson, B.S.1    Jones, D.P.2
  • 19
    • 0024587609 scopus 로고
    • Heterogeneity of pH in the aqueous cytoplasm of renal proximal tubule cells
    • Aw T.Y., Jones D.P. Heterogeneity of pH in the aqueous cytoplasm of renal proximal tubule cells. FASEB J. 3:1989;52-58.
    • (1989) FASEB J. , vol.3 , pp. 52-58
    • Aw, T.Y.1    Jones, D.P.2
  • 20
    • 70449246776 scopus 로고
    • Calculation of intracellular pH from the distribution of 5,5-dimethyl-2,4-oxazolidinedione (DMO). Application to skeletal muscle of the dog
    • Waddell W.J., Butler T.C. Calculation of intracellular pH from the distribution of 5,5-dimethyl-2,4-oxazolidinedione (DMO). Application to skeletal muscle of the dog. J. Clin. Invest. 38:1959;720-729.
    • (1959) J. Clin. Invest. , vol.38 , pp. 720-729
    • Waddell, W.J.1    Butler, T.C.2
  • 21
    • 0000961989 scopus 로고
    • Purification and properties of glutathione reductase of human erythrocytes
    • Scott E.M., Duncan I.W., Ekstrand V. Purification and properties of glutathione reductase of human erythrocytes. J. Biol. Chem. 238:1963;3928-3933.
    • (1963) J. Biol. Chem. , vol.238 , pp. 3928-3933
    • Scott, E.M.1    Duncan, I.W.2    Ekstrand, V.3
  • 22
    • 0000519682 scopus 로고
    • Reduction potential of glutathione
    • Rost J., Rapoport S. Reduction potential of glutathione. Nature. 201:1964;185.
    • (1964) Nature , vol.201 , pp. 185
    • Rost, J.1    Rapoport, S.2
  • 23
    • 0020379671 scopus 로고
    • Enterocytic differentiation of cultured human colon cancer cells by replacement of glucose by galactose in the medium
    • Pinto M., Appay M.-D., Simon-Assmann P., Chevalier G., Dracopoli N., Fogh J., Zweibaum A. Enterocytic differentiation of cultured human colon cancer cells by replacement of glucose by galactose in the medium. Biol. Cell. 44:1982;193-196.
    • (1982) Biol. Cell , vol.44 , pp. 193-196
    • Pinto, M.1    Appay, M.-D.2    Simon-Assmann, P.3    Chevalier, G.4    Dracopoli, N.5    Fogh, J.6    Zweibaum, A.7
  • 24
    • 0018876427 scopus 로고
    • Effects of sodium butyrate and dimethylsulfoxide on biochemical properties of human colon cancer cells
    • Kim Y.S., Tsao D., Siddiqui B., Whitehead J.S., Arnstein P., Bennett J., Hicks J. Effects of sodium butyrate and dimethylsulfoxide on biochemical properties of human colon cancer cells. Cancer. 45:(Phila.):1980;1185-1192.
    • (1980) Cancer , vol.45 , Issue.PHILA. , pp. 1185-1192
    • Kim, Y.S.1    Tsao, D.2    Siddiqui, B.3    Whitehead, J.S.4    Arnstein, P.5    Bennett, J.6    Hicks, J.7
  • 25
    • 0019741605 scopus 로고
    • Assays for differentiation of glutathione S-transferases
    • Habig W.H., Jakoby W.B. Assays for differentiation of glutathione S-transferases. Methods Enzymol. 77:1981;398-405.
    • (1981) Methods Enzymol. , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 26
    • 0019142866 scopus 로고
    • Increase of NAD(P)H:quinone reductase by dietary antioxidants: Possible role in protection against carcinogenesis and toxicity
    • Benson A.M., Hunkeler M.J., Talalay P. Increase of NAD(P)H:quinone reductase by dietary antioxidants possible role in protection against carcinogenesis and toxicity . Proc. Natl. Acad. Sci USA. 77:1980;5216-5220.
    • (1980) Proc. Natl. Acad. Sci USA , vol.77 , pp. 5216-5220
    • Benson, A.M.1    Hunkeler, M.J.2    Talalay, P.3
  • 27
    • 0027052233 scopus 로고
    • Loss of suppression of GSH synthesis at low cell density in primary cultures of rat hepatocytes
    • Lu S.C., Ge J.-L. Loss of suppression of GSH synthesis at low cell density in primary cultures of rat hepatocytes. Am. J. Physiol. 263:1992;C1181-C1189.
    • (1992) Am. J. Physiol. , vol.263
    • Lu, S.C.1    Ge, J.-L.2
  • 28
    • 4243424292 scopus 로고
    • Induction of detoxification enzymes by sodium butyrate and benzyl isothiocyanate in human colon cells
    • Kirlin W.G., De Long M.J., Jones D.P. Induction of detoxification enzymes by sodium butyrate and benzyl isothiocyanate in human colon cells. FASEB J. 9:1995;A989.
    • (1995) FASEB J. , vol.9 , pp. 989
    • Kirlin, W.G.1    De Long, M.J.2    Jones, D.P.3
  • 29
    • 0002703923 scopus 로고
    • Nicotinamide nucleotide compartmentation
    • H. Sies. London: Academic Press
    • Sies H. Nicotinamide nucleotide compartmentation. Sies H. Metabolic compartmentation. 1981;205-231 Academic Press, London.
    • (1981) Metabolic Compartmentation , pp. 205-231
    • Sies, H.1
  • 31
    • 0031149804 scopus 로고    scopus 로고
    • Redox state changes in density-dependent regulation of proliferation
    • Hutter D.E., Till B.G., Greene J.J. Redox state changes in density-dependent regulation of proliferation. Exp. Cell Res. 232:1997;435-438.
    • (1997) Exp. Cell Res. , vol.232 , pp. 435-438
    • Hutter, D.E.1    Till, B.G.2    Greene, J.J.3
  • 32
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai J., Jones D.P. Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J. Biol. Chem. 273:1998;11401-11404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 35
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A.J., Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science. 257:1992;1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 36
    • 0031447479 scopus 로고    scopus 로고
    • Regulated exocytosis in vascular endothelial cells can be triggered by intracellular guanine nucleotides and requires a hydrophobic, thiol-sensitive component. Studies of regulated von Willebrand factor secretion from digitonin permeabilized endothelial cells
    • Fayos B.E., Wattenberg B.W. Regulated exocytosis in vascular endothelial cells can be triggered by intracellular guanine nucleotides and requires a hydrophobic, thiol-sensitive component. Studies of regulated von Willebrand factor secretion from digitonin permeabilized endothelial cells. Endothelium. 5:1997;339-350.
    • (1997) Endothelium , vol.5 , pp. 339-350
    • Fayos, B.E.1    Wattenberg, B.W.2
  • 37
    • 0025267740 scopus 로고
    • Growth-associated modifications of low-molecular-weight thiols and protein sulfhydryls in human bronchial fibroblasts
    • Atzori L., Dypbukt J.M., Sundqvist K., Cotgreave I., Edman C.C., Moldeus P., Grafstrom R.C. Growth-associated modifications of low-molecular-weight thiols and protein sulfhydryls in human bronchial fibroblasts. J. Cell. Physiol. 143:1990;165-171.
    • (1990) J. Cell. Physiol. , vol.143 , pp. 165-171
    • Atzori, L.1    Dypbukt, J.M.2    Sundqvist, K.3    Cotgreave, I.4    Edman, C.C.5    Moldeus, P.6    Grafstrom, R.C.7
  • 38
    • 0024850422 scopus 로고
    • Lymphocyte proliferation in glutathione-depleted lymphocytes: Direct relationship between glutathione availability and the proliferative response
    • Hamilos D.L., Zelarney P., Mascali J.J. Lymphocyte proliferation in glutathione-depleted lymphocytes direct relationship between glutathione availability and the proliferative response . Immunopharmacology. 18:1989;223-235.
    • (1989) Immunopharmacology , vol.18 , pp. 223-235
    • Hamilos, D.L.1    Zelarney, P.2    Mascali, J.J.3
  • 40
    • 0027415692 scopus 로고
    • The effect of 1-chloro-2,4-dinitrobenzene exposure on antigen receptor (CD3)-stimulated transmembrane signal transduction in purified subsets of human peripheral blood lymphocytes
    • Kavanagh T.J., Grossman A., Jinneman J.C., Kanner S.B., White D.L., Eaton D.L., Ledbetter J.A., Rabinovitch P.S. The effect of 1-chloro-2,4-dinitrobenzene exposure on antigen receptor (CD3)-stimulated transmembrane signal transduction in purified subsets of human peripheral blood lymphocytes. Toxicol. Appl. Pharmacol. 119:1993;91-99.
    • (1993) Toxicol. Appl. Pharmacol. , vol.119 , pp. 91-99
    • Kavanagh, T.J.1    Grossman, A.2    Jinneman, J.C.3    Kanner, S.B.4    White, D.L.5    Eaton, D.L.6    Ledbetter, J.A.7    Rabinovitch, P.S.8
  • 42
    • 0026021032 scopus 로고
    • Lymphocyte proliferation in glutathione-depleted lymphocytes: Direct relationship between glutathione availability and the proliferative response
    • Hamilos D.L., Mascali J.J., Wedner H.J. Lymphocyte proliferation in glutathione-depleted lymphocytes direct relationship between glutathione availability and the proliferative response . Int. J. Immunopharmacol. 13:1991;75-90.
    • (1991) Int. J. Immunopharmacol. , vol.13 , pp. 75-90
    • Hamilos, D.L.1    Mascali, J.J.2    Wedner, H.J.3
  • 43
    • 33751155885 scopus 로고
    • Intracellular glutathione levels regulate Fos/Jun induction and activation of glutathione S-transferase gene expression
    • Pinkus R., Weiner L.M., Daniel V. Intracellular glutathione levels regulate Fos/Jun induction and activation of glutathione S-transferase gene expression. Biochemistry. 34:1995;81-88.
    • (1995) Biochemistry , vol.34 , pp. 81-88
    • Pinkus, R.1    Weiner, L.M.2    Daniel, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.