메뉴 건너뛰기




Volumn 130, Issue 1, 1998, Pages 1-15

Cellular and subcellular heterogeneity of glutathione metabolism and transport in rat kidney cells

Author keywords

Digitonin fractionation; Glutathione; Mitochondrial GSH transport; Redox status; Renal distal tubular cells; Renal proximal tubular cells

Indexed keywords

DICARBOXYLIC ACID; DIGITONIN; GLUTATHIONE; MALIC ACID; POLYCARBONATE; REACTIVE OXYGEN METABOLITE; SUBTILISIN;

EID: 0031769774     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-483X(98)00093-6     Document Type: Article
Times cited : (38)

References (52)
  • 1
    • 0000024076 scopus 로고
    • Catalase
    • H.U. Bergmeyer. Deerfield Beach, FL: Verlag Chemie
    • Aebi H.E. Catalase. Bergmeyer H.U. Methods of Enzymatic Analysis. 3rd edn. 1983;273-286 Verlag Chemie, Deerfield Beach, FL.
    • (1983) Methods of Enzymatic Analysis 3rd Edn. , pp. 273-286
    • Aebi, H.E.1
  • 2
    • 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
  • 3
    • 0024413816 scopus 로고
    • Nutrient supply and mitochondrial function
    • Aw T.Y., Jones D.P. Nutrient supply and mitochondrial function. Annu. Rev. Nutr. 9:1989;229-251.
    • (1989) Annu. Rev. Nutr. , vol.9 , pp. 229-251
    • Aw, T.Y.1    Jones, D.P.2
  • 5
    • 0024315568 scopus 로고
    • Fractionation and analysis of mitochondria with polycarbonate membrane filters
    • Bai C., Slife C.W., Aw T.Y., Jones D.P. Fractionation and analysis of mitochondria with polycarbonate membrane filters. Anal. Biochem. 179:1989;114-119.
    • (1989) Anal. Biochem. , vol.179 , pp. 114-119
    • Bai, C.1    Slife, C.W.2    Aw, T.Y.3    Jones, D.P.4
  • 6
    • 0031836944 scopus 로고    scopus 로고
    • Evidence for mitochondrial uptake of glutathione by dicarboxylate and 2-oxoglutarate carriers
    • Chen Z., Lash L.H. Evidence for mitochondrial uptake of glutathione by dicarboxylate and 2-oxoglutarate carriers. J. Pharmacol. Exp. Ther. 285:1998;608-618.
    • (1998) J. Pharmacol. Exp. Ther. , vol.285 , pp. 608-618
    • Chen, Z.1    Lash, L.H.2
  • 7
    • 0027418625 scopus 로고
    • Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes
    • Dawson T.L., Gores G.J., Nieminen A.-L., Herman B., Lemasters J.J. Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes. Am. J. Physiol. 264:1993;C961-C967.
    • (1993) Am. J. Physiol. , vol.264
    • Dawson, T.L.1    Gores, G.J.2    Nieminen, A.-L.3    Herman, B.4    Lemasters, J.J.5
  • 8
    • 0021345735 scopus 로고
    • Oxidation of glutathione during hydroperoxide metabolism: A study using isolated hepatocytes and the glutathione reductase inhibitor 1,3-bis(2chloroethyl)-1-nitrosourea
    • Eklöw L., Moldéus P., Orrenius S. Oxidation of glutathione during hydroperoxide metabolism: A study using isolated hepatocytes and the glutathione reductase inhibitor 1,3-bis(2chloroethyl)-1-nitrosourea. Eur. J. Biochem. 138:1984;459-463.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 459-463
    • Eklöw, L.1    Moldéus, P.2    Orrenius, S.3
  • 10
    • 77957003282 scopus 로고
    • Mitochondrial respiratory control and the polarographic measurement of ADP: O ratios
    • Estabrook R.W. Mitochondrial respiratory control and the polarographic measurement of ADP: O ratios. Methods Enzymol. 10:1967;41-47.
    • (1967) Methods Enzymol. , vol.10 , pp. 41-47
    • Estabrook, R.W.1
  • 11
    • 0023079953 scopus 로고
    • High-performance liquid chromatography of thiols and disulfides: Dinitrophenyl derivatives
    • Fariss M.W., Reed D.J. High-performance liquid chromatography of thiols and disulfides: dinitrophenyl derivatives. Methods Enzymol. 143:1987;101-109.
    • (1987) Methods Enzymol. , vol.143 , pp. 101-109
    • Fariss, M.W.1    Reed, D.J.2
  • 12
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske C.H., SubbaRow Y. The colorimetric determination of phosphorus. J. Biol. Chem. 66:1925;375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 14
    • 0001268903 scopus 로고
    • Removal and binding of polar lipids in mitochondria and other membrane systems
    • Fleischer S., Fleischer B. Removal and binding of polar lipids in mitochondria and other membrane systems. Methods Enzymol. 10:1967;406-433.
    • (1967) Methods Enzymol. , vol.10 , pp. 406-433
    • Fleischer, S.1    Fleischer, B.2
  • 15
    • 0028788763 scopus 로고
    • Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial glutathione status in loss of mitochondrial function and activation of transcription factor nuclear factor-kB: Studies with isolated mitochondria and rat hepatocytes
    • Garcia-Ruiz C., Colell A., Morales A., Kaplowitz N., Fernandez-Checa J.C Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial glutathione status in loss of mitochondrial function and activation of transcription factor nuclear factor-kB: studies with isolated mitochondria and rat hepatocytes. Mol. Pharmacol. 48:1995;825-834.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 825-834
    • Garcia-Ruiz, C.1    Colell, A.2    Morales, A.3    Kaplowitz, N.4    Fernandez-Checa, J.C.5
  • 16
    • 0012971643 scopus 로고
    • Translocation of intracellular glutathione to membrane-bound γ-glutamyl transpeptidase as a discrete step in the γ-glutamyl cycle: Glutathionuria after inhibition of transpeptidase
    • Griffith O.W., Meister A. Translocation of intracellular glutathione to membrane-bound γ-glutamyl transpeptidase as a discrete step in the γ-glutamyl cycle: glutathionuria after inhibition of transpeptidase. Proc. Natl. Acad. Sci. USA. 76:1979;268-272.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 268-272
    • Griffith, O.W.1    Meister, A.2
  • 17
    • 0021619876 scopus 로고
    • Enzyme distribution along the nephron
    • Guder W.G., Ross B.D. Enzyme distribution along the nephron. Kidney Int. 26:1984;101-111.
    • (1984) Kidney Int. , vol.26 , pp. 101-111
    • Guder, W.G.1    Ross, B.D.2
  • 18
    • 0016275313 scopus 로고
    • Glutathione S-transferases: The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., Jakoby W.B. Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:1974;7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 19
    • 0023813831 scopus 로고
    • Glutathione uptake and protection against oxidative injury in isolated kidney cells
    • Hagen T.M., Aw T.Y, 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
  • 20
    • 0021969994 scopus 로고
    • Direct evidence for the role of the membrane potential in glutathione transport by renal brush-border membranes
    • Inoue M., Morino Y. Direct evidence for the role of the membrane potential in glutathione transport by renal brush-border membranes. J. Biol. Chem. 260:1985;326-331.
    • (1985) J. Biol. Chem. , vol.260 , pp. 326-331
    • Inoue, M.1    Morino, Y.2
  • 21
    • 0021467110 scopus 로고
    • Effect of mitochondrial clustering on oxygen supply in hepatocytes
    • Jones D.P. Effect of mitochondrial clustering on oxygen supply in hepatocytes. Am. J. Physiol. 247:1984;C83-C89.
    • (1984) Am. J. Physiol. , vol.247
    • Jones, D.P.1
  • 23
    • 77957003298 scopus 로고
    • Lactic dehydrogenase of muscle
    • Kornberg A. Lactic dehydrogenase of muscle. Methods Enzymol. 1:1955;441-454.
    • (1955) Methods Enzymol. , vol.1 , pp. 441-454
    • Kornberg, A.1
  • 24
    • 0002969827 scopus 로고
    • Isolated kidney cells in the study of chemical toxicity
    • C.A. McQueen. Caldwell, NJ: Telford Press
    • Lash L.H. Isolated kidney cells in the study of chemical toxicity. McQueen C.A. In Vitro Toxicology: Model Systems and Methods. 1989;231-262 Telford Press, Caldwell, NJ.
    • (1989) In Vitro Toxicology: Model Systems and Methods , pp. 231-262
    • Lash, L.H.1
  • 25
    • 0025146446 scopus 로고
    • Susceptibility to toxic injury in different nephron cell populations
    • Lash L.H. Susceptibility to toxic injury in different nephron cell populations. Toxicol. Lett. 53:1990;97-104.
    • (1990) Toxicol. Lett. , vol.53 , pp. 97-104
    • Lash, L.H.1
  • 26
    • 0021750411 scopus 로고
    • Renal glutathione transport: Characteristics of the sodium-dependent system in the basal-lateral membrane
    • Lash L.H., 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
  • 27
    • 0024455217 scopus 로고
    • Isolation of two distinct populations of cells from rat kidney cortex and their use in the study of chemical-induced toxicity
    • Lash L.H., Tokarz J.J. Isolation of two distinct populations of cells from rat kidney cortex and their use in the study of chemical-induced toxicity. Anal. Biochem. 182:1989;271-279.
    • (1989) Anal. Biochem. , vol.182 , pp. 271-279
    • Lash, L.H.1    Tokarz, J.J.2
  • 28
    • 0025144243 scopus 로고
    • Oxidative stress in isolated rat proximal and distal tubular cells
    • Lash L.H., Tokarz J.J. Oxidative stress in isolated rat proximal and distal tubular cells. Am. J. Physiol. 259:1990;F338-F347.
    • (1990) Am. J. Physiol. , vol.259
    • Lash, L.H.1    Tokarz, J.J.2
  • 29
    • 0025860602 scopus 로고
    • Cytotoxicity of alkylating agents in isolated rat kidney proximal tubular and distal tubular cells
    • Lash L.H., Woods E.B. Cytotoxicity of alkylating agents in isolated rat kidney proximal tubular and distal tubular cells. Arch. Biochem. Biophys. 286:1991;46-56.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 46-56
    • Lash, L.H.1    Woods, E.B.2
  • 30
    • 0002675717 scopus 로고
    • Mitochondrial isolation from liver and kidney: Strategy, techniques, and criteria for purity
    • L.H. Lash, & D.P. Jones. San Diego: Academic Press
    • Lash L.H., Sall J.M. Mitochondrial isolation from liver and kidney: strategy, techniques, and criteria for purity. Lash L.H., Jones D.P. Mitochondrial Dysfunction. 1993;8-28 Academic Press, San Diego.
    • (1993) Mitochondrial Dysfunction , pp. 8-28
    • Lash, L.H.1    Sall, J.M.2
  • 31
    • 0027391651 scopus 로고
    • Hypoxia and oxygen dependence of cytotoxicity in renal proximal tubular and distal tubular cells
    • Lash L.H., Tokarz J.J., Woods E.B., Pedrosi B.M. Hypoxia and oxygen dependence of cytotoxicity in renal proximal tubular and distal tubular cells. Biochem. Pharmacol. 45:1993;191200.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 191200
    • Lash, L.H.1    Tokarz, J.J.2    Woods, E.B.3    Pedrosi, B.M.4
  • 33
    • 0017067418 scopus 로고
    • Glutathione peroxidase activity in selenium-deficient rat liver
    • Lawrence R.A., Burk R.F. Glutathione peroxidase activity in selenium-deficient rat liver. Biochem. Biophys. Res. Commun. 71:1976;952-958.
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 952-958
    • Lawrence, R.A.1    Burk, R.F.2
  • 35
    • 0015694375 scopus 로고
    • 2 formation: Relationship with energy conservation
    • 2 formation: relationship with energy conservation. FEBS Lett. 33:1973;84-88.
    • (1973) FEBS Lett. , vol.33 , pp. 84-88
    • Loschen, G.1    Azzi, A.2    Flohé, L.3
  • 38
    • 50549161676 scopus 로고
    • Glutamyl-p-nitroanilide: A new convenient substrate for determination and study of L- And D-γ-glutamyltranspeptidase activities
    • Orlowski M., Meister A. Glutamyl-p-nitroanilide: a new convenient substrate for determination and study of L- and D-γ-glutamyltranspeptidase activities. Biochim. Biophys. Acta. 73:1963;679-681.
    • (1963) Biochim. Biophys. Acta , vol.73 , pp. 679-681
    • Orlowski, M.1    Meister, A.2
  • 40
    • 0018866620 scopus 로고
    • A simple and fast method for the isolation of basolateral plasma membranes from rat small-intestinal epithelial cells
    • Scalera V., Storelli C., Storelli-Joss C., Haase W., Murer H. A simple and fast method for the isolation of basolateral plasma membranes from rat small-intestinal epithelial cells. Biochem. J. 186:1980;177-181.
    • (1980) Biochem. J. , vol.186 , pp. 177-181
    • Scalera, V.1    Storelli, C.2    Storelli-Joss, C.3    Haase, W.4    Murer, H.5
  • 41
    • 0014068230 scopus 로고
    • The submitochondrial localization of monoamine oxidase: An enzymatic marker for the outer membrane of rat liver mitochondria
    • Schnaitman C., Erwin V.G., Greenawalt J.W. The submitochondrial localization of monoamine oxidase: an enzymatic marker for the outer membrane of rat liver mitochondria. J. Cell. Biol. 32:1967;719-735.
    • (1967) J. Cell. Biol. , vol.32 , pp. 719-735
    • Schnaitman, C.1    Erwin, V.G.2    Greenawalt, J.W.3
  • 42
    • 0025827155 scopus 로고
    • Renal mitochondrial glutathione transport
    • Schnellmann R.G. Renal mitochondrial glutathione transport. Life. Sci. 49:1991;393-398.
    • (1991) Life. Sci. , vol.49 , pp. 393-398
    • Schnellmann, R.G.1
  • 43
    • 0021151662 scopus 로고
    • Glutamylcysteine synthetase from erythrocytes
    • Seelig G.F., Meister A. Glutamylcysteine synthetase from erythrocytes. Anal. Biochem. 141:1984;510-514.
    • (1984) Anal. Biochem. , vol.141 , pp. 510-514
    • Seelig, G.F.1    Meister, A.2
  • 46
    • 0017893011 scopus 로고
    • Subcellular metabolise concentrations: Dependence of mitochondrial and cytosolic ATP systems on the metabolic state of perfused rat liver
    • Soboll S., Scholz R., Heldt H.W. Subcellular metabolise concentrations: dependence of mitochondrial and cytosolic ATP systems on the metabolic state of perfused rat liver. Eur. J. Biochem. 87:1978;377-390.
    • (1978) Eur. J. Biochem. , vol.87 , pp. 377-390
    • Soboll, S.1    Scholz, R.2    Heldt, H.W.3
  • 47
    • 77957010982 scopus 로고
    • Citrate synthase
    • Srere P.A. Citrate synthase. Methods Enzymol. 13:1969;3-11.
    • (1969) Methods Enzymol. , vol.13 , pp. 3-11
    • Srere, P.A.1
  • 48
    • 77957006891 scopus 로고
    • Glucose-6-phosphatase from liver
    • Swanson M.A. Glucose-6-phosphatase from liver. Methods Enzymol. 2:1955;541-543.
    • (1955) Methods Enzymol. , vol.2 , pp. 541-543
    • Swanson, M.A.1
  • 49
    • 0014084758 scopus 로고
    • A kinetic photometric method for serum leucine aminopeptidase
    • Szasz G. A kinetic photometric method for serum leucine aminopeptidase. Am. J. Clin. Pathol. 47:1967;607-611.
    • (1967) Am. J. Clin. Pathol. , vol.47 , pp. 607-611
    • Szasz, G.1
  • 50
    • 0017399084 scopus 로고
    • Determination of mitochondrial/cytosolic metabolise gradients in isolated rat liver cells by cell disruption
    • Tischler M.E., Hecht P., Williamson J.R. Determination of mitochondrial/cytosolic metabolise gradients in isolated rat liver cells by cell disruption. Arch. Biochem. Biophys. 181:1977;278-292.
    • (1977) Arch. Biochem. Biophys. , vol.181 , pp. 278-292
    • Tischler, M.E.1    Hecht, P.2    Williamson, J.R.3
  • 51
    • 0030602861 scopus 로고    scopus 로고
    • Pathways of glutathione metabolism and transport in isolated proximal tubular cells from rat kidney
    • Visarius T.M., Putt D.A., Schare J.M., Pegouske D.M., Lash L.H. Pathways of glutathione metabolism and transport in isolated proximal tubular cells from rat kidney. Biochem. Pharmacol. 52:1996;259-272.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 259-272
    • Visarius, T.M.1    Putt, D.A.2    Schare, J.M.3    Pegouske, D.M.4    Lash, L.H.5
  • 52
    • 0015954423 scopus 로고
    • Rapid separation of particulate components and soluble cytoplasm of isolated rat liver cells
    • Zuurendonk P.F., Tager J.M. Rapid separation of particulate components and soluble cytoplasm of isolated rat liver cells. Biochim. Biophys. Acta. 333:1974;393-399.
    • (1974) Biochim. Biophys. Acta , vol.333 , pp. 393-399
    • Zuurendonk, P.F.1    Tager, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.