메뉴 건너뛰기




Volumn 150, Issue 2, 2009, Pages 322-328

Exogenous glutathione can increase glutathione levels in tissues of rainbow trout (Oncorhynchus mykiss) through extracellular breakdown and intracellular synthesis

Author keywords

Acivicin; Brain; Buthionine sulfoximide; Fish; glutamylcysteine synthetase; glutamyltranspeptidase

Indexed keywords

ACIVICIN; BUTHIONINE SULFOXIMINE; CELL PROTEIN; GAMMA GLUTAMYLTRANSFERASE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; SODIUM CHLORIDE;

EID: 67649804608     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2009.05.010     Document Type: Article
Times cited : (8)

References (34)
  • 1
    • 0019173673 scopus 로고
    • Dynamic state of glutathione in blood plasma
    • Anderson M.E., and Meister A. Dynamic state of glutathione in blood plasma. J. Biol. Chem. 255 (1980) 9530-9533
    • (1980) J. Biol. Chem. , vol.255 , pp. 9530-9533
    • Anderson, M.E.1    Meister, A.2
  • 2
    • 0020662578 scopus 로고
    • Transport and direct utilization of γ-glutamylcyst(e)ine for glutathione synthesis
    • Anderson M.E., and Meister A. Transport and direct utilization of γ-glutamylcyst(e)ine for glutathione synthesis. Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 707-711
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 707-711
    • Anderson, M.E.1    Meister, A.2
  • 3
    • 0019194680 scopus 로고
    • Direct evidence for inter-organ transport of glutathione and that the non-filtration renal mechanism for glutathione utilization involves γ-glutamyl transpeptidase
    • Anderson M.E., Bridges R.J., and Meister A. Direct evidence for inter-organ transport of glutathione and that the non-filtration renal mechanism for glutathione utilization involves γ-glutamyl transpeptidase. Biochem. Biophys. Res. Commun. 96 (1980) 848-853
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 848-853
    • Anderson, M.E.1    Bridges, R.J.2    Meister, A.3
  • 4
    • 0027953099 scopus 로고
    • Glutathione transport by type II cells in perfused rat lung
    • Bai C., Brown L.A.S., and Jones D.P. Glutathione transport by type II cells in perfused rat lung. Am. J. Physiol. 267 (1994) L447-L455
    • (1994) Am. J. Physiol. , vol.267
    • Bai, C.1    Brown, L.A.S.2    Jones, D.P.3
  • 5
    • 17444419342 scopus 로고    scopus 로고
    • Molecular mechanisms of reduced glutathione transport: role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins
    • Ballatori N., Hammond C.L., Cunningham J.B., Krance S.M., and Marchan R. Molecular mechanisms of reduced glutathione transport: role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins. Toxicol. Appl. Pharmacol. 204 (2005) 238-255
    • (2005) Toxicol. Appl. Pharmacol. , vol.204 , pp. 238-255
    • Ballatori, N.1    Hammond, C.L.2    Cunningham, J.B.3    Krance, S.M.4    Marchan, R.5
  • 6
    • 0003004587 scopus 로고
    • Physiological changes in fish from stress in aquaculture with emphasis on the response and effects of corticosteroids
    • Barton B.A., and Iwama G.K. Physiological changes in fish from stress in aquaculture with emphasis on the response and effects of corticosteroids. Annu. Rev. Fish Dis. 1 (1991) 3-26
    • (1991) Annu. Rev. Fish Dis. , vol.1 , pp. 3-26
    • Barton, B.A.1    Iwama, G.K.2
  • 7
    • 0031834260 scopus 로고    scopus 로고
    • Tissue and whole-body extracellular, red blood cell and albumin spaces in the rainbow trout as a function of time: a reappraisal of the volume of the secondary circulation
    • Bushnell P.G., Conklin D.J., Duff D.W., and Olson K.R. Tissue and whole-body extracellular, red blood cell and albumin spaces in the rainbow trout as a function of time: a reappraisal of the volume of the secondary circulation. J. Exp. Biol. 201 (1998) 1381-1391
    • (1998) J. Exp. Biol. , vol.201 , pp. 1381-1391
    • Bushnell, P.G.1    Conklin, D.J.2    Duff, D.W.3    Olson, K.R.4
  • 8
    • 0010508753 scopus 로고
    • Glutathione synthesis in oxidative stress
    • Packer L., and Cadenas E. (Eds), Marcel Dekker, New York
    • Forman H.F., Liu R.-M., and Shi M.M. Glutathione synthesis in oxidative stress. In: Packer L., and Cadenas E. (Eds). Biothiols in Health and Disease. (1995), Marcel Dekker, New York 189-212
    • (1995) Biothiols in Health and Disease. , pp. 189-212
    • Forman, H.F.1    Liu, R.-M.2    Shi, M.M.3
  • 9
    • 0026717124 scopus 로고
    • Effects of buthionine sulfoximine and diethyl maleate on glutathione turnover in the channel catfish
    • Gallagher E.P., Hasspieler B.M., and Di Giulio R.T. Effects of buthionine sulfoximine and diethyl maleate on glutathione turnover in the channel catfish. Biochem. Pharmacol. 43 (1992) 2209-2215
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 2209-2215
    • Gallagher, E.P.1    Hasspieler, B.M.2    Di Giulio, R.T.3
  • 10
    • 0026564310 scopus 로고
    • Bidirectional mechanism of plasma membrane transport of reduced glutathione in intact rat hepatocytes and membrane vesicles
    • Garcia-Ruiz C., Fernandez-Checa J.C., and Kaplowitz N. Bidirectional mechanism of plasma membrane transport of reduced glutathione in intact rat hepatocytes and membrane vesicles. J. Biol. Chem. 267 (1992) 22256-22264
    • (1992) J. Biol. Chem. , vol.267 , pp. 22256-22264
    • Garcia-Ruiz, C.1    Fernandez-Checa, J.C.2    Kaplowitz, N.3
  • 11
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine
    • Griffith O.W. Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal. Biochem. 106 (1980) 207-212
    • (1980) Anal. Biochem. , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 12
    • 0023813831 scopus 로고
    • Glutathione uptake and protection against oxidative injury in isolated kidney cells
    • Hagen T.M., Aw T.Y., and Jones D.P. Glutathione uptake and protection against oxidative injury in isolated kidney cells. Kidney Int. 34 (1988) 74-81
    • (1988) Kidney Int. , vol.34 , pp. 74-81
    • Hagen, T.M.1    Aw, T.Y.2    Jones, D.P.3
  • 13
    • 0032575366 scopus 로고    scopus 로고
    • Glutathione measurement in human plasma. Evaluation of sample collection, storage and derivatization conditions for analysis of dansyl derivatives by HPLC
    • Jones D.P., Carlson J.L., Samiec P.S., Sternberg Jr. P., Moody Jr. V.C., Reed R.L., and Brown L.A.S. Glutathione measurement in human plasma. Evaluation of sample collection, storage and derivatization conditions for analysis of dansyl derivatives by HPLC. Clin. Chim. Acta 275 (1998) 175-184
    • (1998) Clin. Chim. Acta , vol.275 , pp. 175-184
    • Jones, D.P.1    Carlson, J.L.2    Samiec, P.S.3    Sternberg Jr., P.4    Moody Jr., V.C.5    Reed, R.L.6    Brown, L.A.S.7
  • 14
    • 0034775037 scopus 로고    scopus 로고
    • Glutathione transport in human retinal pigment epithelial (HRPE) cells: apical localization of sodium-dependent GSH transport
    • Kannan R., Tang D., Hu J., and Bok D. Glutathione transport in human retinal pigment epithelial (HRPE) cells: apical localization of sodium-dependent GSH transport. Exp. Eye Res. 72 (2001) 661-666
    • (2001) Exp. Eye Res. , vol.72 , pp. 661-666
    • Kannan, R.1    Tang, D.2    Hu, J.3    Bok, D.4
  • 15
    • 0000320310 scopus 로고    scopus 로고
    • Glutathione: systemic protectant against oxidative and free radical damage
    • Kidd P.M. Glutathione: systemic protectant against oxidative and free radical damage. Altern. Med. Rev. 2 (1997) 155-176
    • (1997) Altern. Med. Rev. , vol.2 , pp. 155-176
    • Kidd, P.M.1
  • 16
    • 1542285469 scopus 로고    scopus 로고
    • Acivicin-induced alterations in renal and hepatic glutathione concentrations and in γ-glutamyltransferase activities
    • Lantum H.B.M., Iyer R.A., and Anders M.W. Acivicin-induced alterations in renal and hepatic glutathione concentrations and in γ-glutamyltransferase activities. Biochem. Pharmacol. 67 (2004) 1421-1426
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 1421-1426
    • Lantum, H.B.M.1    Iyer, R.A.2    Anders, M.W.3
  • 17
    • 0021750411 scopus 로고
    • Renal glutathione transport - characteristics of the sodium-dependent system in the basal-lateral membrane
    • Lash L.H., and Jones D.P. Renal glutathione transport - characteristics of the sodium-dependent system in the basal-lateral membrane. J. Biol. Chem. 259 (1984) 14508-14514
    • (1984) J. Biol. Chem. , vol.259 , pp. 14508-14514
    • Lash, L.H.1    Jones, D.P.2
  • 18
    • 0021216714 scopus 로고
    • Hepatic glutathione homeostasis in the rat: efflux accounts for glutathione turnover
    • Lauterburg B.H., Adams J.D., and Mitchell J.R. Hepatic glutathione homeostasis in the rat: efflux accounts for glutathione turnover. Hepatology 4 (1984) 586-590
    • (1984) Hepatology , vol.4 , pp. 586-590
    • Lauterburg, B.H.1    Adams, J.D.2    Mitchell, J.R.3
  • 19
    • 34247272942 scopus 로고    scopus 로고
    • The glutathione antioxidant system is enhanced in growth hormone transgenic coho salmon (Oncorhynchus kisutch)
    • Leggatt R.A., Brauner C.J., Iwama G.K., and Devlin R.H. The glutathione antioxidant system is enhanced in growth hormone transgenic coho salmon (Oncorhynchus kisutch). J. Comp. Physiol. 177B (2007) 413-422
    • (2007) J. Comp. Physiol. , vol.177 B , pp. 413-422
    • Leggatt, R.A.1    Brauner, C.J.2    Iwama, G.K.3    Devlin, R.H.4
  • 20
    • 0027934244 scopus 로고
    • Specificity and directionality of thiol effects on sinusoidal glutathione transport in rat liver
    • Lu S.C., Kuhlenkamp J., Ge J.L., Sun W.M., and Kaplowitz N. Specificity and directionality of thiol effects on sinusoidal glutathione transport in rat liver. Mol. Pharmacol. 46 (1994) 578-585
    • (1994) Mol. Pharmacol. , vol.46 , pp. 578-585
    • Lu, S.C.1    Kuhlenkamp, J.2    Ge, J.L.3    Sun, W.M.4    Kaplowitz, N.5
  • 21
    • 0010478667 scopus 로고
    • Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester
    • Mårtensson J., and Meister A. Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 471-475
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 471-475
    • Mårtensson, J.1    Meister, A.2
  • 22
    • 0011888533 scopus 로고
    • Glutathione metabolism in the lung: inhibition of its synthesis leads to lamellar body and mitochondrial defects
    • Mårtensson J., Jain A., Frayer W., and Meister A. Glutathione metabolism in the lung: inhibition of its synthesis leads to lamellar body and mitochondrial defects. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 5296-5300
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5296-5300
    • Mårtensson, J.1    Jain, A.2    Frayer, W.3    Meister, A.4
  • 23
    • 0001224074 scopus 로고
    • Strategies for increasing cellular glutathione
    • Packer L., and Cadenas E. (Eds), Marcel Dekker, New York
    • Meister A. Strategies for increasing cellular glutathione. In: Packer L., and Cadenas E. (Eds). Biothiols in Health and Disease. (1995), Marcel Dekker, New York 165-188
    • (1995) Biothiols in Health and Disease. , pp. 165-188
    • Meister, A.1
  • 25
    • 0036158009 scopus 로고    scopus 로고
    • The thiol sensitivity of glutathione transport in sidedness-sorted basolateral liver plasma membrane and in Oatp1-expressing HeLa cell membrane
    • Mittur A., Wolkoff A.W., and Kaplowitz N. The thiol sensitivity of glutathione transport in sidedness-sorted basolateral liver plasma membrane and in Oatp1-expressing HeLa cell membrane. Mol. Pharmacol. 61 (2002) 425-435
    • (2002) Mol. Pharmacol. , vol.61 , pp. 425-435
    • Mittur, A.1    Wolkoff, A.W.2    Kaplowitz, N.3
  • 26
    • 0003460524 scopus 로고    scopus 로고
    • Role of exogenous glutathione in teleost fish and its effects on antioxidant defense responses in rainbow trout exposed to 3,3′,4,4′-tetrachlorobiphenyl
    • Otto D.M.E., Sen C.K., Hidiroglou N., Madere R., and Moon T.W. Role of exogenous glutathione in teleost fish and its effects on antioxidant defense responses in rainbow trout exposed to 3,3′,4,4′-tetrachlorobiphenyl. Fish Physiol. Biochem. 16 (1997) 449-457
    • (1997) Fish Physiol. Biochem. , vol.16 , pp. 449-457
    • Otto, D.M.E.1    Sen, C.K.2    Hidiroglou, N.3    Madere, R.4    Moon, T.W.5
  • 27
    • 0343763837 scopus 로고
    • Transport of glutathione, as gamma-glutamylcysteinylglycyl ester, into liver and kidney
    • Puri R.N., and Meister A. Transport of glutathione, as gamma-glutamylcysteinylglycyl ester, into liver and kidney. Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 5258-5260
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 5258-5260
    • Puri, R.N.1    Meister, A.2
  • 28
    • 0016635533 scopus 로고
    • Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione
    • Richman P.G., and Meister A. Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione. J. Biol. Chem. 250 (1975) 1422-1426
    • (1975) J. Biol. Chem. , vol.250 , pp. 1422-1426
    • Richman, P.G.1    Meister, A.2
  • 29
    • 0027140175 scopus 로고
    • Role of apical and basolateral secretion in turnover of glutathione in LlC-PK(1) cells
    • Scott R.D., Hughey R.P., and Curthoys N.P. Role of apical and basolateral secretion in turnover of glutathione in LlC-PK(1) cells. Am. J. Physiol. 265 (1993) F723-F728
    • (1993) Am. J. Physiol. , vol.265
    • Scott, R.D.1    Hughey, R.P.2    Curthoys, N.P.3
  • 31
    • 0000384670 scopus 로고
    • Glutathione-dependent metabolism in fish and rodents
    • Wallace K.B. Glutathione-dependent metabolism in fish and rodents. Environ. Toxicol. Chem. 8 (1989) 1049-1055
    • (1989) Environ. Toxicol. Chem. , vol.8 , pp. 1049-1055
    • Wallace, K.B.1
  • 32
    • 0011889814 scopus 로고
    • Radioprotection by glutathione ester: transport of glutathione ester into human lymphoid cells and fibroblasts
    • Wellner V.P., Anderson M.E., Puri R.N., Jensen G.L., and Meister A. Radioprotection by glutathione ester: transport of glutathione ester into human lymphoid cells and fibroblasts. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 4732-4735
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 4732-4735
    • Wellner, V.P.1    Anderson, M.E.2    Puri, R.N.3    Jensen, G.L.4    Meister, A.5
  • 33
    • 0031903998 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase does not act as a cystine transporter in brain microvessels
    • Wolff J.E.A., Münstermann G., Grebenkämper K., and Erben M. Gamma-glutamyl transpeptidase does not act as a cystine transporter in brain microvessels. Neurochem. Res. 23 (1998) 1175-1178
    • (1998) Neurochem. Res. , vol.23 , pp. 1175-1178
    • Wolff, J.E.A.1    Münstermann, G.2    Grebenkämper, K.3    Erben, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.