메뉴 건너뛰기




Volumn 67, Issue , 2014, Pages 451-459

S-D-Lactoylglutathione can be an alternative supply of mitochondrial glutathione

Author keywords

Glutathione; Glyoxalase II enzyme; Glyoxalase system; Mitochondria; S D Lactoylglutathione; Thiols

Indexed keywords

DEXTRO LACTATE DEHYDROGENASE; DEXTRO LACTOYLGLUTATHIONE; GLUTAMATE DEHYDROGENASE; GLUTATHIONE DERIVATIVE; GLYOXALASE; HYDROXYACYLGLUTATHIONE HYDROLASE; LIPOSOME; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; CARBON; D-LACTATE DEHYDROGENASE; GLUTATHIONE; LACTATE DEHYDROGENASE; LACTIC ACID; S-LACTOYLGLUTATHIONE; THIOL ESTER HYDROLASE; TRITIUM; S D LACTOYLGLUTATHIONE;

EID: 84893351777     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.12.005     Document Type: Article
Times cited : (45)

References (50)
  • 2
    • 24144467846 scopus 로고    scopus 로고
    • ROS: Really involved in Oxygen Sensing
    • DOI 10.1016/j.cmet.2005.05.006, PII S1550413105001440
    • W.G. Kaelin Jr. ROS: really involved in oxygen sensing Cell Metab. 1 2005 357 358 (Pubitemid 43960628)
    • (2005) Cell Metabolism , vol.1 , Issue.6 , pp. 357-358
    • Kaelin Jr., W.G.1
  • 3
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • E. Cadenas, and K.J. Davies Mitochondrial free radical generation, oxidative stress, and aging Free Radic. Biol Med. 29 2000 222 230
    • (2000) Free Radic. Biol Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 4
    • 84856729192 scopus 로고    scopus 로고
    • Mitochondrial thiols in antioxidant protection and redox signaling: Distinct roles for glutathionylation and other thiol modifications
    • M.P. Murphy Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications Antioxid. Redox Signal. 16 2012 476 495
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 476-495
    • Murphy, M.P.1
  • 5
    • 82955227412 scopus 로고    scopus 로고
    • In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis
    • S.C. Albrecht, A.G. Barata, J. Grosshans, A.A. Teleman, and T.P. Dick In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis Cell Metab. 14 2011 819 829
    • (2011) Cell Metab. , vol.14 , pp. 819-829
    • Albrecht, S.C.1    Barata, A.G.2    Grosshans, J.3    Teleman, A.A.4    Dick, T.P.5
  • 6
    • 84867725042 scopus 로고    scopus 로고
    • Mitochondrial thiols in the regulation of cell death pathways
    • F. Yin, H. Sancheti, and E. Cadenas Mitochondrial thiols in the regulation of cell death pathways Antioxid. Redox Signal. 17 2012 1714 1727
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1714-1727
    • Yin, F.1    Sancheti, H.2    Cadenas, E.3
  • 7
    • 31544467567 scopus 로고    scopus 로고
    • Glutathione depletion by buthionine sulfoximine induces DNA deletions in mice
    • DOI 10.1093/carcin/bgi222
    • R. Reliene, and R.H. Schiestl Glutathione depletion by buthionine sulfoximine induces DNA deletions in mice Carcinogenesis 27 2006 240 244 (Pubitemid 43159875)
    • (2006) Carcinogenesis , vol.27 , Issue.2 , pp. 240-244
    • Reliene, R.1    Schiestl, R.H.2
  • 8
    • 0142210179 scopus 로고    scopus 로고
    • Effect of Glutathione Depletion on Sites and Topology of Superoxide and Hydrogen Peroxide Production in Mitochondria
    • DOI 10.1124/mol.64.5.1136
    • D. Han, R. Canali, D. Rettori, and N. Kaplowitz Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria Mol. Pharmacol. 64 2003 1136 1144 (Pubitemid 37310746)
    • (2003) Molecular Pharmacology , vol.64 , Issue.5 , pp. 1136-1144
    • Han, D.1    Canali, R.2    Rettori, D.3    Kaplowitz, N.4
  • 9
    • 33747618005 scopus 로고    scopus 로고
    • Mitochondrial glutathione: Hepatocellular survival-death switch
    • C. Garcia-Ruiz, and J.C. Fernandez-Checa Mitochondrial glutathione: hepatocellular survival-death switch J. Gastroenterol. Hepatol. 21 Suppl. 3 2006 S3 S6
    • (2006) J. Gastroenterol. Hepatol. , vol.21 , Issue.SUPPL. 3
    • Garcia-Ruiz, C.1    Fernandez-Checa, J.C.2
  • 10
    • 17444381536 scopus 로고    scopus 로고
    • Hepatic mitochondrial glutathione: Transport and role in disease and toxicity
    • DOI 10.1016/j.taap.2004.10.001, Membrane Transporters in Toxicology
    • J.C. Fernandez-Checa, and N. Kaplowitz Hepatic mitochondrial glutathione: transport and role in disease and toxicity Toxicol. Appl. Pharmacol. 204 2005 263 273 (Pubitemid 40545231)
    • (2005) Toxicology and Applied Pharmacology , vol.204 , Issue.3 , pp. 263-273
    • Fernandez-Checa, J.C.1    Kaplowitz, N.2
  • 12
    • 70349172938 scopus 로고    scopus 로고
    • Apoptosis and glutathione: Beyond an antioxidant
    • R. Franco, and J.A. Cidlowski Apoptosis and glutathione: beyond an antioxidant Cell Death Differ. 16 2009 1303 1314
    • (2009) Cell Death Differ. , vol.16 , pp. 1303-1314
    • Franco, R.1    Cidlowski, J.A.2
  • 14
    • 0033763930 scopus 로고    scopus 로고
    • Biochemical changes in transplanted rat liver stored in University of Wisconsin and Euro-Collins solutions
    • W. Jassem, M. Battino, C. Cinti, S.J. Norton, V. Saba, and G. Principato Biochemical changes in transplanted rat liver stored in University of Wisconsin and Euro-Collins solutions J. Surg. Res. 94 2000 68 73
    • (2000) J. Surg. Res. , vol.94 , pp. 68-73
    • Jassem, W.1    Battino, M.2    Cinti, C.3    Norton, S.J.4    Saba, V.5    Principato, G.6
  • 15
    • 0003113205 scopus 로고    scopus 로고
    • Studies on the life prolonging effect of food restriction: Glutathione levels and glyoxalase enzymes in rat liver
    • DOI 10.1016/S0047-6374(97)00167-X, PII S004763749700167X
    • T. Armeni, C. Pieri, M. Marra, F. Saccucci, and G. Principato Studies on the life prolonging effect of food restriction: glutathione levels and glyoxalase enzymes in rat liver Mech. Ageing Dev. 101 1998 101 110 (Pubitemid 28165637)
    • (1998) Mechanisms of Ageing and Development , vol.101 , Issue.1-2 , pp. 101-110
    • Armeni, T.1    Pieri, C.2    Marra, M.3    Saccucci, F.4    Principato, G.5
  • 17
    • 33750011601 scopus 로고    scopus 로고
    • Mitochondrial glutathione transport: Physiological, pathological and toxicological implications
    • DOI 10.1016/j.cbi.2006.03.001, PII S0009279706000536
    • L.H. Lash Mitochondrial glutathione transport: physiological, pathological and toxicological implications Chem. Biol. Interact. 163 2006 54 67 (Pubitemid 44572210)
    • (2006) Chemico-Biological Interactions , vol.163 , Issue.1-2 , pp. 54-67
    • Lash, L.H.1
  • 18
    • 0031836944 scopus 로고    scopus 로고
    • Evidence for mitochondrial uptake of glutathione by dicarboxylate and 2- oxoglutarate carriers
    • Z. Chen, and L.H. Lash Evidence for mitochondrial uptake of glutathione by dicarboxylate and 2-oxoglutarate carriers J. Pharmacol. Exp. Ther. 285 1998 608 618 (Pubitemid 28237440)
    • (1998) Journal of Pharmacology and Experimental Therapeutics , vol.285 , Issue.2 , pp. 608-618
    • Chen, Z.1    Lash, L.H.2
  • 19
    • 0033963540 scopus 로고    scopus 로고
    • Enrichment and functional reconstitution of glutathione transport activity from rabbit kidney mitochondria. Further evidence for the role of the dicarboxylate and 2-oxoglutarate carriers in mitochondrial glutathione transport
    • DOI 10.1006/abbi.1999.1527
    • Z. Chen, D.A. Putt, and L.H. Lash Enrichment and functional reconstitution of glutathione transport activity from rabbit kidney mitochondria: further evidence for the role of the dicarboxylate and 2-oxoglutarate carriers in mitochondrial glutathione transport Arch. Biochem. Biophys. 373 2000 193 202 (Pubitemid 30046504)
    • (2000) Archives of Biochemistry and Biophysics , vol.373 , Issue.1 , pp. 193-202
    • Chen, Z.1    Putt, D.A.2    Lash, L.H.3
  • 20
    • 43949146899 scopus 로고    scopus 로고
    • Hepatic mitochondrial transport of glutathione: Studies in isolated rat liver mitochondria and H4IIE rat hepatoma cells
    • Q. Zhong, D.A. Putt, F. Xu, and L.H. Lash Hepatic mitochondrial transport of glutathione: studies in isolated rat liver mitochondria and H4IIE rat hepatoma cells Arch. Biochem. Biophys. 474 2008 119 127
    • (2008) Arch. Biochem. Biophys. , vol.474 , pp. 119-127
    • Zhong, Q.1    Putt, D.A.2    Xu, F.3    Lash, L.H.4
  • 21
    • 84874045170 scopus 로고    scopus 로고
    • Mitochondrial glutathione transport is a key determinant of neuronal susceptibility to oxidative and nitrosative stress
    • H.M. Wilkins, D. Kirchhof, E. Manning, J.W. Joseph, and D.A. Linseman Mitochondrial glutathione transport is a key determinant of neuronal susceptibility to oxidative and nitrosative stress J. Biol. Chem. 288 2013 5091 5101
    • (2013) J. Biol. Chem. , vol.288 , pp. 5091-5101
    • Wilkins, H.M.1    Kirchhof, D.2    Manning, E.3    Joseph, J.W.4    Linseman, D.A.5
  • 24
    • 84875723942 scopus 로고    scopus 로고
    • Glutathione and glutathione analogues; Therapeutic potentials
    • J.H. Wu, and G. Batist Glutathione and glutathione analogues; therapeutic potentials Biochim. Biophys. Acta 1830 2013 3350 3353
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3350-3353
    • Wu, J.H.1    Batist, G.2
  • 25
    • 43449110448 scopus 로고    scopus 로고
    • Molecular enzymology of the glyoxalase system
    • B. Mannervik Molecular enzymology of the glyoxalase system Drug Metab. Drug Interact. 23 2008 13 27 (Pubitemid 351669563)
    • (2008) Drug Metabolism and Drug Interactions , vol.23 , Issue.1-2 , pp. 13-27
    • Mannervik, B.1
  • 26
    • 0347419281 scopus 로고    scopus 로고
    • Glyoxalase I - Structure, function and a critical role in the enzymatic defence against glycation
    • P.J. Thornalley Glyoxalase I - structure, function and a critical role in the enzymatic defence against glycation Biochem. Soc. Trans. 31 2003 1343 1348 (Pubitemid 38030973)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.6 , pp. 1343-1348
    • Thornalley, P.J.1
  • 28
    • 0000479795 scopus 로고
    • Thioesters of glutathione
    • L. Uotila Thioesters of glutathione Methods Enzymol. 77 1981 424 430
    • (1981) Methods Enzymol. , vol.77 , pp. 424-430
    • Uotila, L.1
  • 30
    • 84893355446 scopus 로고    scopus 로고
    • Guide for the care and use laboratory animals. Washingthon DC; 1985
    • Guide for the care and use laboratory animals. Washingthon DC; 1985.
  • 31
    • 0019740345 scopus 로고
    • Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples
    • T.P. Akerboom, and H. Sies Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples Methods Enzymol. 77 1981 373 382
    • (1981) Methods Enzymol. , vol.77 , pp. 373-382
    • Akerboom, T.P.1    Sies, H.2
  • 33
    • 0014747124 scopus 로고
    • Inhibition of yeast S-lactylglutathione lyase (glyoxalase I) by sulfhydryl reagents
    • K. Ekwall, and B. Mannervik Inhibition of yeast S-lactylglutathione lyase (glyoxalase I) by sulfhydryl reagents Arch. Biochem. Biophys. 137 1970 128 132
    • (1970) Arch. Biochem. Biophys. , vol.137 , pp. 128-132
    • Ekwall, K.1    Mannervik, B.2
  • 34
    • 0016773981 scopus 로고
    • Effects of pH and thiols on the kinetics of yeast glyoxalase I. An evaluation of the random pathway mechanism
    • D.L. Vander Jagt, E. Daub, J.A. Krohn, and L.P. Han Effects of pH and thiols on the kinetics of yeast glyoxalase I. An evaluation of the random pathway mechanism Biochemistry 14 1975 3669 3675
    • (1975) Biochemistry , vol.14 , pp. 3669-3675
    • Vander Jagt, D.L.1    Daub, E.2    Krohn, J.A.3    Han, L.P.4
  • 35
    • 0033619153 scopus 로고    scopus 로고
    • Signalling between mitochondria and the nucleus regulates the expression of a new D-lactate dehydrogenase activity in yeast
    • DOI 10.1002/(SICI)1097-0061(19990930)15:13<1377::AID-YEA473>3.0. CO;2-0
    • A. Chelstowska, Z. Liu, Y. Jia, D. Amberg, and R.A. Butow Signalling between mitochondria and the nucleus regulates the expression of a new D-lactate dehydrogenase activity in yeast Yeast 15 1999 1377 1391 (Pubitemid 29445810)
    • (1999) Yeast , vol.15 , Issue.13 , pp. 1377-1391
    • Chelstowska, A.1    Liu, Z.2    Jia, Y.3    Amberg, D.4    Butow, R.A.5
  • 36
    • 0024435739 scopus 로고
    • Cyclosporin A-sensitive and insensitive mechanisms produce the permeability transition in mitochondria
    • K.M. Broekemeier, and D.R. Pfeiffer Cyclosporin A-sensitive and insensitive mechanisms produce the permeability transition in mitochondria Biochem. Biophys. Res. Commun. 163 1989 561 566 (Pubitemid 19227343)
    • (1989) Biochemical and Biophysical Research Communications , vol.163 , Issue.1 , pp. 561-566
    • Broekemeier, K.M.1    Pfeiffer, D.R.2
  • 37
    • 82355170968 scopus 로고    scopus 로고
    • Safranine as a fluorescent probe for the evaluation of mitochondrial membrane potential in isolated organelles and permeabilized cells
    • T.R. Figueira, D.R. Melo, A.E. Vercesi, and R.F. Castilho Safranine as a fluorescent probe for the evaluation of mitochondrial membrane potential in isolated organelles and permeabilized cells Methods Mol. Biol. 810 2012 103 117
    • (2012) Methods Mol. Biol. , vol.810 , pp. 103-117
    • Figueira, T.R.1    Melo, D.R.2    Vercesi, A.E.3    Castilho, R.F.4
  • 38
    • 58149399716 scopus 로고    scopus 로고
    • Preparation, characterization, and use of antioxidant-liposomes
    • H. Yang, V. Paromov, M. Smith, and W.L. Stone Preparation, characterization, and use of antioxidant-liposomes Methods Mol. Biol. 477 2008 277 292
    • (2008) Methods Mol. Biol. , vol.477 , pp. 277-292
    • Yang, H.1    Paromov, V.2    Smith, M.3    Stone, W.L.4
  • 39
    • 79955945923 scopus 로고    scopus 로고
    • Glyoxalase in diabetes, obesity and related disorders
    • N. Rabbani, and P.J. Thornalley Glyoxalase in diabetes, obesity and related disorders Semin. Cell Dev. Biol. 22 2011 309 317
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 309-317
    • Rabbani, N.1    Thornalley, P.J.2
  • 40
    • 79955945922 scopus 로고    scopus 로고
    • Glyoxalase in tumourigenesis and multidrug resistance
    • P.J. Thornalley, and N. Rabbani Glyoxalase in tumourigenesis and multidrug resistance Semin. Cell Dev. Biol. 22 2011 318 325
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 318-325
    • Thornalley, P.J.1    Rabbani, N.2
  • 41
    • 4244040278 scopus 로고    scopus 로고
    • Glutathione-dependent detoxification of α-oxoaldehydes by the glyoxalase system: Involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors
    • DOI 10.1016/S0009-2797(97)00157-9, PII S0009279797001579
    • P.J. Thornalley Glutathione-dependent detoxification of alpha-oxoaldehydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors Chem. Biol. Interact. 111-112 1998 137 151 (Pubitemid 28271940)
    • (1998) Chemico-Biological Interactions , vol.111-112 , pp. 137-151
    • Thornalley, P.J.1
  • 42
    • 0023893522 scopus 로고
    • Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms
    • V. Talesa, L. Uotila, M. Koivusalo, G. Principato, E. Giovannini, and G. Rosi Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms Biochim. Biophys. Acta 955 1988 103 110
    • (1988) Biochim. Biophys. Acta , vol.955 , pp. 103-110
    • Talesa, V.1    Uotila, L.2    Koivusalo, M.3    Principato, G.4    Giovannini, E.5    Rosi, G.6
  • 43
    • 0031728459 scopus 로고    scopus 로고
    • A zinc-binding motif conserved in glyoxalase II, β-lactamase and arylsulfatases
    • DOI 10.1016/S0968-0004(98)01264-X, PII S096800049801264X
    • S. Melino, C. Capo, B. Dragani, A. Aceto, and R. Petruzzelli A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases Trends Biochem. Sci. 23 1998 381 382 (Pubitemid 28511377)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.10 , pp. 381-382
    • Melino, S.1    Capo, C.2    Dragani, B.3    Aceto, A.4    Petruzzelli, R.5
  • 46
    • 0034308191 scopus 로고    scopus 로고
    • Specific interaction of cytosolic and mitochondrial glyoxalase II with acidic phospholipids in form of liposomes results in the inhibition of the cytosolic enzyme only
    • A. Scirè, F. Tanfani, F. Saccucci, E. Bertoli, and G. Principato Specific interaction of cytosolic and mitochondrial glyoxalase II with acidic phospholipids in form of liposomes results in the inhibition of the cytosolic enzyme only Proteins 41 2000 33 39
    • (2000) Proteins , vol.41 , pp. 33-39
    • Scirè, A.1    Tanfani, F.2    Saccucci, F.3    Bertoli, E.4    Principato, G.5
  • 47
  • 48
    • 84875700217 scopus 로고    scopus 로고
    • Protein glutathionylation in health and disease
    • P. Ghezzi Protein glutathionylation in health and disease Biochim. Biophys. Acta 1830 2013 3165 3172
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3165-3172
    • Ghezzi, P.1
  • 50
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • DOI 10.1016/S0891-5849(01)00480-4, PII S0891584901004804
    • F.Q. Schafer, and G.R. Buettner Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radic. Biol. Med. 30 2001 1191 1212 (Pubitemid 32463931)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.11 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.