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Volumn 7, Issue 2, 2011, Pages 71-78

Inhibiting glutathione metabolism in lung lining fluid as a strategy to augment antioxidant defense

Author keywords

Antioxidant; Gamma glutamyl transferase; Glutathione; Lung lining fluid; Metabolism

Indexed keywords

6 DIAZO 5 OXONORLEUCINE; ACIVICIN; ACYLTRANSFERASE INHIBITOR; ANTIOXIDANT; AZASERINE; CYSTEINE; GAMMA GLUTAMYLTRANSFERASE; GLUTATHIONE;

EID: 79960995443     PISSN: 15734080     EISSN: 18756662     Source Type: Journal    
DOI: 10.2174/157340811796575308     Document Type: Article
Times cited : (18)

References (90)
  • 1
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • Kensler, T.W.; Wakabayashi, N.; Biswal, S. Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu. Rev. Pharmacol. Toxicol., 2007, 47, 89-116.
    • (2007) Annu. Rev. Pharmacol. Toxicol , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 5
    • 0023263523 scopus 로고
    • Normal alveolar epithelial lining fluid contains high-levels of glutathione
    • Cantin, A.M.; North, S.L.; Hubbard, R.C.; Crystal, R.G. Normal alveolar epithelial lining fluid contains high-levels of glutathione. J. Appl. Physiol., 1987, 63, 152-157.
    • (1987) J. Appl. Physiol , vol.63 , pp. 152-157
    • Cantin, A.M.1    North, S.L.2    Hubbard, R.C.3    Crystal, R.G.4
  • 7
    • 0345708307 scopus 로고    scopus 로고
    • Hypochlorous acid alters bronchial epithelial cell membrane properties and prevention by extracellular glutathione
    • Venglarik, C.J.; Giron-Calle, J.; Wigley, A.F.; Malle, E.; Watanabe, N.; Forman, H.J. Hypochlorous acid alters bronchial epithelial cell membrane properties and prevention by extracellular glutathione. J. Appl. Physiol., 2003, 95, 2444-2452.
    • (2003) J. Appl. Physiol , vol.95 , pp. 2444-2452
    • Venglarik, C.J.1    Giron-Calle, J.2    Wigley, A.F.3    Malle, E.4    Watanabe, N.5    Forman, H.J.6
  • 8
    • 41549148595 scopus 로고    scopus 로고
    • Identification of Nrf2-dependent airway epithelial adaptive response to proinflammatory oxidant-hypochlorous acid challenge by transcription profiling
    • Zhu, L.; Pi, J.; Wachi, S.; Andersen, M.E.; Wu, R.; Chen, Y. Identification of Nrf2-dependent airway epithelial adaptive response to proinflammatory oxidant-hypochlorous acid challenge by transcription profiling. Am. J. Physiol. Lung Cell Mol. Physiol., 2008, 294, L469-L477.
    • (2008) Am. J. Physiol. Lung Cell Mol. Physiol , vol.294 , pp. 469-477
    • Zhu, L.1    Pi, J.2    Wachi, S.3    Andersen, M.E.4    Wu, R.5    Chen, Y.6
  • 10
    • 73549118121 scopus 로고    scopus 로고
    • Hyperoxia-induced lung injury in gamma-glutamyl transferase deficiency is associated with alterations in nitrosative and nitrative stress
    • Klings, E.S.; Lowry, M.H.; Li, G.; Jean, J.C.; Fernandez, B.O.; Garcia-Saura, M.F.; Feelisch, M.; Joyce-Brady, M. Hyperoxia- induced lung injury in gamma-glutamyl transferase deficiency is associated with alterations in nitrosative and nitrative stress. Am. J. Pathol., 2009, 175, 2309-2318.
    • (2009) Am. J. Pathol , vol.175 , pp. 2309-2318
    • Klings, E.S.1    Lowry, M.H.2    Li, G.3    Jean, J.C.4    Fernandez, B.O.5    Garcia-Saura, M.F.6    Feelisch, M.7    Joyce-Brady, M.8
  • 11
    • 0028263767 scopus 로고
    • Glutathione-ascorbic acid antioxidant system in animals
    • Meister, A. Glutathione-ascorbic acid antioxidant system in animals. J. Biol. Chem., 1994, 269, 9397-9400.
    • (1994) J. Biol. Chem , vol.269 , pp. 9397-9400
    • Meister, A.1
  • 12
    • 0025336786 scopus 로고
    • The effect of glutathione on the vitamin E requirement for inhibition of liver microsomal lipid peroxidation
    • Leedle, R.A.; Aust, S.D. The effect of glutathione on the vitamin E requirement for inhibition of liver microsomal lipid peroxidation. Lipids, 1990, 25, 241-245.
    • (1990) Lipids , vol.25 , pp. 241-245
    • Leedle, R.A.1    Aust, S.D.2
  • 13
    • 55349118470 scopus 로고    scopus 로고
    • Metal specificity in DNA damage prevention by sulfur antioxidants
    • Battin, E.E.; Brumaghim, J.L. Metal specificity in DNA damage prevention by sulfur antioxidants. J. Inorg. Biochem., 2008, 102, 2036-2042.
    • (2008) J. Inorg. Biochem , vol.102 , pp. 2036-2042
    • Battin, E.E.1    Brumaghim, J.L.2
  • 14
    • 65049087190 scopus 로고    scopus 로고
    • Glutathione: Overview of its protective roles, measurement, and biosynthesis
    • Forman, H.J.; Zhang, H.; Rinna, A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol. Aspects Med., 2009, 30, 1-13.
    • (2009) Mol. Aspects Med , vol.30 , pp. 1-13
    • Forman, H.J.1    Zhang, H.2    Rinna, A.3
  • 15
    • 27544440248 scopus 로고    scopus 로고
    • Regulation of glutathione in inflammation and chronic lung diseases
    • Rahman, I. Regulation of glutathione in inflammation and chronic lung diseases. Mutat. Res., 2005, 579, 58-80.
    • (2005) Mutat. Res , vol.579 , pp. 58-80
    • Rahman, I.1
  • 16
    • 0027315107 scopus 로고
    • Increased levels of glutathione in bronchoalveolar lavage fluid from patients with asthma
    • Smith, L.J.; Houston, M.; Anderson, J. Increased levels of glutathione in bronchoalveolar lavage fluid from patients with asthma. Am. Rev. Respir. Dis., 1993, 147, 1461-1464.
    • (1993) Am. Rev. Respir. Dis , vol.147 , pp. 1461-1464
    • Smith, L.J.1    Houston, M.2    Anderson, J.3
  • 17
    • 0033369168 scopus 로고    scopus 로고
    • Lung glutathione and oxidative stress: Implications in cigarette smoke-induced airway disease
    • Rahman, I.; MacNee, W. Lung glutathione and oxidative stress: implications in cigarette smoke-induced airway disease. Am. J. Physiol., 1999, 277, L1067-L1088.
    • (1999) Am. J. Physiol , vol.277 , pp. 1067-1088
    • Rahman, I.1    Macnee, W.2
  • 18
    • 0032802282 scopus 로고    scopus 로고
    • Ethanol ingestion impairs alveolar epithelial glutathione homeostasis and function, and predisposes to endotoxin-mediated acute lung injury
    • Guidot, D.; Moss, M.; Holguin, F.; Lois, M.; Brown, L. Ethanol ingestion impairs alveolar epithelial glutathione homeostasis and function, and predisposes to endotoxin-mediated acute lung injury. Chest, 1999, 116, 82S.
    • (1999) Chest , vol.82 S , pp. 116
    • Guidot, D.1    Moss, M.2    Holguin, F.3    Lois, M.4    Brown, L.5
  • 19
    • 0032519897 scopus 로고    scopus 로고
    • Chronic ethanol ingestion impairs alveolar type II cell glutathione homeostasis and function and predisposes to endotoxin-mediated acute edematous lung injury in rats
    • Holguin, F.; Moss, I.; Brown, L.A.; Guidot, D.M. Chronic ethanol ingestion impairs alveolar type II cell glutathione homeostasis and function and predisposes to endotoxin-mediated acute edematous lung injury in rats. J. Clin. Invest., 1998, 101, 761-768.
    • (1998) J. Clin. Invest , vol.101 , pp. 761-768
    • Holguin, F.1    Moss, I.2    Brown, L.A.3    Guidot, D.M.4
  • 20
    • 0036667841 scopus 로고    scopus 로고
    • Glutathione replacement preserves the functional surfactant phospholipid pool size and decreases sepsis-mediated lung dysfunction in ethanol-fed rats
    • Velasquez, A.; Bechara, R.I.; Lewis, J.F.; Malloy, J.; McCaig, L.; Brown, L.A.; Guidot, D.M. Glutathione replacement preserves the functional surfactant phospholipid pool size and decreases sepsis- mediated lung dysfunction in ethanol-fed rats. Alcohol Clin. Exp. Res., 2002, 26, 1245-1251.
    • (2002) Alcohol Clin. Exp. Res , vol.26 , pp. 1245-1251
    • Velasquez, A.1    Bechara, R.I.2    Lewis, J.F.3    Malloy, J.4    McCaig, L.5    Brown, L.A.6    Guidot, D.M.7
  • 21
    • 0024578662 scopus 로고
    • Glutathione deficiency in the epithelial lining fluid of the lower respiratory tract in idiopathic pulmonary fibrosis
    • Cantin, A.M.; Hubbard, R.C.; Crystal, R.G. Glutathione deficiency in the epithelial lining fluid of the lower respiratory tract in idiopathic pulmonary fibrosis. Am. Rev. Respir. Dis., 1989, 139, 370-372.
    • (1989) Am. Rev. Respir. Dis , vol.139 , pp. 370-372
    • Cantin, A.M.1    Hubbard, R.C.2    Crystal, R.G.3
  • 22
    • 0030747167 scopus 로고    scopus 로고
    • Alveolar fluid glutathione decreases in asymptomatic HIV-seropositive subjects over time
    • Pacht, E.R.; Diaz, P.; Clanton, T.; Hart, J.; Gadek, J.E. Alveolar fluid glutathione decreases in asymptomatic HIV-seropositive subjects over time. Chest, 1997, 112, 785-788.
    • (1997) Chest , vol.112 , pp. 785-788
    • Pacht, E.R.1    Diaz, P.2    Clanton, T.3    Hart, J.4    Gadek, J.E.5
  • 24
    • 79551607386 scopus 로고    scopus 로고
    • Hypertonic saline increases lung epithelial lining fluid glutathione and thiocyanate: Two protective CFTR-dependent thiols against oxidative injury
    • Gould, N.S.; Gauthier, S.; Kariya, C.T.; Min, E.; Huang, J.; Day, B.J. Hypertonic saline increases lung epithelial lining fluid glutathione and thiocyanate: two protective CFTR-dependent thiols against oxidative injury. Respir. Res., 2010, 11, 119.
    • (2010) Respir. Res , vol.11 , pp. 119
    • Gould, N.S.1    Gauthier, S.2    Kariya, C.T.3    Min, E.4    Huang, J.5    Day, B.J.6
  • 26
    • 39749090507 scopus 로고    scopus 로고
    • The treatment of pulmonary diseases and respiratory-related conditions with inhaled (nebulized or aerosolized) glutathione
    • Prousky, J. The treatment of pulmonary diseases and respiratory-related conditions with inhaled (nebulized or aerosolized) glutathione. Evid. Based Complement. Alternat. Med., 2008, 5, 27-35.
    • (2008) Evid. Based Complement. Alternat. Med , vol.5 , pp. 27-35
    • Prousky, J.1
  • 27
    • 0025282179 scopus 로고
    • Augmentation of glutathione in the fluid lining the epithelium of the lower respiratory-tract by directly administering glutathione aerosol
    • Buhl, R.; Vogelmeier, C.; Critenden, M.; Hubbard, R.C.; Hoyt, R.F.; Wilson, E.M.; Cantin, A.M.; Crystal, R.G. Augmentation of glutathione in the fluid lining the epithelium of the lower respiratory-tract by directly administering glutathione aerosol. Proc. Natl. Acad. Sci. USA, 1990, 87, 4063-4067.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4063-4067
    • Buhl, R.1    Vogelmeier, C.2    Critenden, M.3    Hubbard, R.C.4    Hoyt, R.F.5    Wilson, E.M.6    Cantin, A.M.7    Crystal, R.G.8
  • 29
    • 58849092435 scopus 로고    scopus 로고
    • In utero ethanol exposure impairs defenses against experimental group B Streptococcus in the term guinea pig lung
    • Gauthier, T.W.; Young, P.A.; Gabelaia, L.; Tang, S.M.; Ping, X.D.; Harris, F.L.; Brown, L.A. In utero ethanol exposure impairs defenses against experimental group B Streptococcus in the term guinea pig lung. Alcohol Clin. Exp. Res., 2009, 33, 300-306.
    • (2009) Alcohol Clin. Exp. Res , vol.33 , pp. 300-306
    • Gauthier, T.W.1    Young, P.A.2    Gabelaia, L.3    Tang, S.M.4    Ping, X.D.5    Harris, F.L.6    Brown, L.A.7
  • 30
    • 0028361231 scopus 로고
    • Effect of N-acetyl cysteine on the concentrations of thiols in plasma, bronchoalveolar lavage fluid, and lung tissue
    • Bridgeman, M.M.; Marsden, M.; Selby, C.; Morrison, D.; MacNee, W. Effect of N-acetyl cysteine on the concentrations of thiols in plasma, bronchoalveolar lavage fluid, and lung tissue. Thorax, 1994, 49, 670-675.
    • (1994) Thorax , vol.49 , pp. 670-675
    • Bridgeman, M.M.1    Marsden, M.2    Selby, C.3    Morrison, D.4    Macnee, W.5
  • 31
    • 0023096396 scopus 로고
    • No penetration of orally administered N-acetylcysteine into bronchoalveolar lavage fluid
    • Cotgreave, I.A.; Eklund, A.; Larsson, K.; Moldeus, P.W. No penetration of orally administered N-acetylcysteine into bronchoalveolar lavage fluid. Eur. J. Respir. Dis., 1987, 70, 73-77.
    • (1987) Eur. J. Respir. Dis , vol.70 , pp. 73-77
    • Cotgreave, I.A.1    Eklund, A.2    Larsson, K.3    Moldeus, P.W.4
  • 33
    • 0022460516 scopus 로고
    • Intracellular cysteine and glutathione delivery systems
    • Meister, A.; Anderson, M.E.; Hwang, O. Intracellular cysteine and glutathione delivery systems. J. Am. Coll. Nutr., 1986, 5, 137-151.
    • (1986) J. Am. Coll. Nutr , vol.5 , pp. 137-151
    • Meister, A.1    Anderson, M.E.2    Hwang, O.3
  • 34
    • 0030977130 scopus 로고    scopus 로고
    • Mice with genetic gamma-glutamyl transpeptidase deficiency exhibit glutathionuria, severe growth failure, reduced life spans, and infertility
    • Harding, C.O.; Williams, P.; Wagner, E.; Chang, D.S.; Wild, K.; Colwell, R.E.; Wolff, J.A. Mice with genetic gamma-glutamyl transpeptidase deficiency exhibit glutathionuria, severe growth failure, reduced life spans, and infertility. J. Biol. Chem., 1997, 272, 12560-12567.
    • (1997) J. Biol. Chem , vol.272 , pp. 12560-12567
    • Harding, C.O.1    Williams, P.2    Wagner, E.3    Chang, D.S.4    Wild, K.5    Colwell, R.E.6    Wolff, J.A.7
  • 35
    • 0032963609 scopus 로고    scopus 로고
    • Gamma-Glutamyl transferase (GGT) deficiency in the GGT enu1 mouse results from a single point mutation that leads to a stop codon in the first coding exon of GGT mRNA
    • Jean, J.; Harding, C.O.; Oakes, S.M.; Yu, Q.; Held, P.K.; Joyce-Brady, M. Gamma-Glutamyl transferase (GGT) deficiency in the GGT enu1 mouse results from a single point mutation that leads to a stop codon in the first coding exon of GGT mRNA. Mutagenesis, 1999, 14, 31-36.
    • (1999) Mutagenesis , vol.14 , pp. 31-36
    • Jean, J.1    Harding, C.O.2    Oakes, S.M.3    Yu, Q.4    Held, P.K.5    Joyce-Brady, M.6
  • 36
    • 0028232008 scopus 로고
    • Synthesis and release of amphipathic gamma-glutamyl transferase by the pulmonary alveolar type 2 cell.Its redistribution throughout the gas exchange portion of the lung indicates a new role for surfactant
    • Joyce-Brady, M.; Takahashi, Y.; Oakes, S.M.; Rishi, A.K.; Levine, R.A.; Kinlough, C.L.; Hughey, R.P. Synthesis and release of amphipathic gamma-glutamyl transferase by the pulmonary alveolar type 2 cell. Its redistribution throughout the gas exchange portion of the lung indicates a new role for surfactant. J. Biol. Chem., 1994, 269, 14219-14226.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14219-14226
    • Joyce-Brady, M.1    Takahashi, Y.2    Oakes, S.M.3    Rishi, A.K.4    Levine, R.A.5    Kinlough, C.L.6    Hughey, R.P.7
  • 40
    • 0017315596 scopus 로고
    • Comparison of the size and physical properties of gamma-glutamyl transpeptidase purified from rat kidney following solubilization with papain or with triton X-100
    • Hughey, R.P.; Curthoys, N.P. Comparison of the size and physical properties of gamma-glutamyl transpeptidase purified from rat kidney following solubilization with papain or with triton X-100. J. Biol. Chem., 1976, 251, 7863-7870.
    • (1976) J. Biol. Chem , vol.251 , pp. 7863-7870
    • Hughey, R.P.1    Curthoys, N.P.2
  • 41
    • 0035937805 scopus 로고    scopus 로고
    • Gamma-glutamyltransferase and its isoform mediate an endoplasmic reticulum stress response
    • Joyce-Brady, M.; Jean, J.C.; Hughey, R.P. Gamma - glutamyltransferase and its isoform mediate an endoplasmic reticulum stress response. J. Biol. Chem., 2001, 276, 9468-9477.
    • (2001) J. Biol. Chem , vol.276 , pp. 9468-9477
    • Joyce-Brady, M.1    Jean, J.C.2    Hughey, R.P.3
  • 42
    • 0027250325 scopus 로고
    • Human lung expresses unique g-glutamyl transpeptidase transcripts
    • Wetmore, L.A.; Gerard, C.; Drazen, J.M. Human lung expresses unique g-glutamyl transpeptidase transcripts. Proc. Natl. Acad. Sci. USA, 1993, 90, 7461-7465.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7461-7465
    • Wetmore, L.A.1    Gerard, C.2    Drazen, J.M.3
  • 43
    • 29144536222 scopus 로고    scopus 로고
    • Prooxidant reactions promoted by soluble and cell-bound gamma-glutamyltransferase activity
    • Dominici, S.; Paolicchi, A.; Corti, A.; Maellaro, E.; Pompella, A. Prooxidant reactions promoted by soluble and cell-bound gamma- glutamyltransferase activity. Methods Enzymol., 2005, 401, 484-501.
    • (2005) Methods Enzymol , vol.401
    • Dominici, S.1    Paolicchi, A.2    Corti, A.3    Maellaro, E.4    Pompella, A.5
  • 44
    • 0018640906 scopus 로고
    • Characterization and physiological function of rat renal gamma-glutamyltranspeptidase
    • Curthoys, N.P.; Hughey, R.P. Characterization and physiological function of rat renal gamma-glutamyltranspeptidase. Enzyme, 1979, 24, 383-403.
    • (1979) Enzyme , vol.24 , pp. 383-403
    • Curthoys, N.P.1    Hughey, R.P.2
  • 45
    • 0027263185 scopus 로고
    • Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase
    • Hanigan, M.; Ricketts, W.A. Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase. Biochemistry, 1993, 32, 6302-6306.
    • (1993) Biochemistry , vol.32 , pp. 6302-6306
    • Hanigan, M.1    Ricketts, W.A.2
  • 46
    • 0021591010 scopus 로고
    • New aspects of glutathione biochemistry and transport: Selective alteration of glutathione metabolism
    • Meister, A. New aspects of glutathione biochemistry and transport: selective alteration of glutathione metabolism. Fed. Proc., 1984, 43, 3031-3042.
    • (1984) Fed. Proc , vol.43 , pp. 3031-3042
    • Meister, A.1
  • 50
    • 0038368911 scopus 로고    scopus 로고
    • L-2-oxothiazolidine-4-carboxylate supplementation in murine gamma-GT deficiency
    • Held, P.; Harding, C.O. L-2-oxothiazolidine-4-carboxylate supplementation in murine gamma-GT deficiency. Free Radic. Biol. Med., 2003, 34, 1482-1487.
    • (2003) Free Radic. Biol. Med , vol.34 , pp. 1482-1487
    • Held, P.1    Harding, C.O.2
  • 51
    • 0141483289 scopus 로고    scopus 로고
    • Kinetic studies of rat kidney gamma-glutamyltranspeptidase deacylation reveal a general base-catalyzed mechanism
    • Castonguay, R.; Lherbet, C.; Keillor, J.W. Kinetic studies of rat kidney gamma-glutamyltranspeptidase deacylation reveal a general base-catalyzed mechanism. Biochemistry, 2003, 42, 11504-11513.
    • (2003) Biochemistry , vol.42 , pp. 11504-11513
    • Castonguay, R.1    Lherbet, C.2    Keillor, J.W.3
  • 52
    • 30144443591 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase substrate specificity Mechanism catalytic
    • Keillor, J. W.; Castonguay, R.; Lherbet, C. Gamma-glutamyl transpeptidase substrate specificity and catalytic mechanism. Methods Enzymol., 2005, 401, 449-467.
    • (2005) Methods Enzymol , vol.401 , pp. 449-467
    • Keillor, J.W.1    Castonguay, R.2    Lherbet, C.3
  • 53
    • 0022272471 scopus 로고
    • Gamma-Glutamyl transpeptidase: Kinetics and mechanism
    • Allison, R.D. gamma-Glutamyl transpeptidase: kinetics and mechanism. Methods Enzymol., 1985, 113, 419-437.
    • (1985) Methods Enzymol , vol.113 , pp. 419-437
    • Allison, R.D.1
  • 54
    • 2942735409 scopus 로고    scopus 로고
    • Pre-steady-state kinetic studies of rat kidney gamma-glutamyl transpeptidase confirm its ping-pong mechanism
    • Keillor, J.W.; Menard A; Castonguay, R.; Lherbet, C.; Rivard, C. Pre-steady-state kinetic studies of rat kidney gamma-glutamyl transpeptidase confirm its ping-pong mechanism. J. Phys. Org. Chem., 2004, 17, 529-536.
    • (2004) J. Phys. Org. Chem , vol.17 , pp. 529-536
    • Keillor, J.W.1    Menard, A.2    Castonguay, R.3    Lherbet, C.4    Rivard, C.5
  • 55
    • 0034604269 scopus 로고    scopus 로고
    • Identification of catalytic nucleophile of Escherichia coli gamma-glutamyltranspeptidase by gamma-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile
    • Inoue, M.; Hiratake, J.; Suzuki, H.; Kumagai, H.; Sakata, K. Identification of catalytic nucleophile of Escherichia coli gamma- glutamyltranspeptidase by gamma-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile. Biochemistry, 2000, 39, 7764-7771.
    • (2000) Biochemistry , vol.39 , pp. 7764-7771
    • Inoue, M.1    Hiratake, J.2    Suzuki, H.3    Kumagai, H.4    Sakata, K.5
  • 56
    • 35648962831 scopus 로고    scopus 로고
    • Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase
    • Castonguay, R.; Halim, D.; Morin, M.; Furtos, A.; Lherbet, C.; Bonneil, E.; Thibault, P.; Keillor, J. W. Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase. Biochemistry, 2007, 46, 12253-12262.
    • (2007) Biochemistry , vol.46 , pp. 12253-12262
    • Castonguay, R.1    Halim, D.2    Morin, M.3    Furtos, A.4    Lherbet, C.5    Bonneil, E.6    Thibault, P.7    Keillor, J.W.8
  • 57
    • 0042033156 scopus 로고
    • Serine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase
    • Tate, S.; Meister, A. Serine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase. Proc. Natl. Acad. Sci. USA, 1978, 75, 4806-4809.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4806-4809
    • Tate, S.1    Meister, A.2
  • 58
    • 0035862175 scopus 로고    scopus 로고
    • Development and evaluation of a boronate inhibitor of gamma-glutamyl transpeptidase
    • London, R.E.; Gabel, S.A. Development and evaluation of a boronate inhibitor of gamma-glutamyl transpeptidase. Arch. Biochem. Biophys., 2001, 385, 250-258.
    • (2001) Arch. Biochem. Biophys , vol.385 , pp. 250-258
    • London, R.E.1    Gabel, S.A.2
  • 59
    • 0035873796 scopus 로고    scopus 로고
    • Slow-binding inhibition of gamma-glutamyl transpeptidase by gamma-boroGlu
    • Stein, R.L.; DeCicco, C.; Nelson, D.; Thomas, B. Slow-binding inhibition of gamma-glutamyl transpeptidase by gamma-boroGlu. Biochemistry, 2001, 40, 5804-5811.
    • (2001) Biochemistry , vol.40 , pp. 5804-5811
    • Stein, R.L.1    Decicco, C.2    Nelson, D.3    Thomas, B.4
  • 60
    • 0018417145 scopus 로고
    • Isolation of anthglutin, an inhibitor of gamma-glutamyl transpeptidase from Penicillum oxalicum
    • Minato, S. Isolation of anthglutin, an inhibitor of gamma-glutamyl transpeptidase from Penicillum oxalicum. Arch. Biochem. Biophys., 1979, 192, 235-240.
    • (1979) Arch. Biochem. Biophys , vol.192 , pp. 235-240
    • Minato, S.1
  • 61
    • 0012971643 scopus 로고
    • Translocation of intracellular glutathione to membrane-bound gamma-glutamyl transpeptidase as a discrete step in the gamma-glutamyl cycle: Glutathionuria after inhibition of transpeptidase
    • Griffith, O.W.; Meister, A. Translocation of intracellular glutathione to membrane-bound gamma-glutamyl transpeptidase as a discrete step in the gamma-glutamyl cycle: glutathionuria after inhibition of transpeptidase. Proc. Natl. Acad. Sci. USA, 1979, 76, 268-272.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 268-272
    • Griffith, O.W.1    Meister, A.2
  • 62
    • 0028168829 scopus 로고
    • Interaction of gamma-glutamyl transpeptidase with acivicin
    • Stole, E.; Smith, T.K.; Manning, J.M.; Meister, A. Interaction of gamma-glutamyl transpeptidase with acivicin. J. Biol. Chem., 1994, 269, 21435-21439.
    • (1994) J. Biol. Chem , vol.269 , pp. 21435-21439
    • Stole, E.1    Smith, T.K.2    Manning, J.M.3    Meister, A.4
  • 63
    • 0025240043 scopus 로고
    • Identification of a highly reactive threonine residue at the active site of gamma-glutamyl transpeptidase
    • Stole, E.; Seddon, A.P.; Wellner, D.; Meister, A. Identification of a highly reactive threonine residue at the active site of gamma- glutamyl transpeptidase. Proc. Natl. Acad. Sci. USA, 1990, 87, 1706-1709.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1706-1709
    • Stole, E.1    Seddon, A.P.2    Wellner, D.3    Meister, A.4
  • 64
    • 0028951183 scopus 로고
    • Different sites of acivicin binding and inactivation of gamma-glutamyl transpeptidases
    • USA
    • Smith, T.K.; Ikeda, Y.; Fujii, J.; Taniguchi, N.; Meister, A. Different sites of acivicin binding and inactivation of gamma- glutamyl transpeptidases. Proc. Natl. Acad. Sci. USA, 1995, 92, 2360-2364.
    • (1995) Proc. Natl. Acad. Sci , vol.92 , pp. 2360-2364
    • Smith, T.K.1    Ikeda, Y.2    Fujii, J.3    Taniguchi, N.4    Meister, A.5
  • 65
    • 0642350495 scopus 로고
    • Affinity labeling of gamma-glutamyl transpeptidase and location of the gamma-glutamyl binding site on the light subunit
    • Tate, S.S.; Meister, A. Affinity labeling of gamma-glutamyl transpeptidase and location of the gamma-glutamyl binding site on the light subunit. Proc. Natl. Acad. Sci. USA, 1977, 74, 931-935.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 931-935
    • Tate, S.S.1    Meister, A.2
  • 66
    • 0017642809 scopus 로고
    • Human kidney gamma-glutamyl transpeptidase.Catalytic properties,subunit structure,and localization of the gamma-glutamyl binding site on the light subunit
    • Tate, S.S.; Ross, M.E. Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. J. Biol. Chem., 1977, 252, 6042-6045.
    • (1977) J. Biol. Chem , vol.252 , pp. 6042-6045
    • Tate, S.S.1    Ross, M.E.2
  • 67
    • 0017614157 scopus 로고
    • Affinity labeling of rat-kidney gamma-glutamyl transpeptidase
    • Inoue, M.; Horiuchi, S.; Morino, Y. Affinity labeling of rat-kidney gamma-glutamyl transpeptidase. Eur. J. Biochem., 1977, 73, 335-342.
    • (1977) Eur. J. Biochem , vol.73 , pp. 335-342
    • Inoue, M.1    Horiuchi, S.2    Morino, Y.3
  • 68
    • 3042808682 scopus 로고    scopus 로고
    • Inhibition of gamma-glutamyl transpeptidase activity decreases intracellular cysteine levels in cervical carcinoma
    • Ruoso, P.; Hedley, D.W. Inhibition of gamma-glutamyl transpeptidase activity decreases intracellular cysteine levels in cervical carcinoma. Cancer Chemother. Pharmacol., 2004, 54, 49-56.
    • (2004) Cancer Chemother. Pharmacol , vol.54 , pp. 49-56
    • Ruoso, P.1    Hedley, D.W.2
  • 69
    • 14844286405 scopus 로고    scopus 로고
    • Acceleration of glutathione efflux and inhibition of gamma-glutamyltranspeptidase sensitize metastatic B16 melanoma cells to endothelium-induced cytotoxicity
    • Benlloch, M.; Ortega, A.; Ferrer, P.; Segarra, R.; Obrador, E.; Asensi, M.; Carretero, J.; Estrela, J.M. Acceleration of glutathione efflux and inhibition of gamma-glutamyltranspeptidase sensitize metastatic B16 melanoma cells to endothelium-induced cytotoxicity. J. Biol. Chem., 2005, 280, 6950-6959.
    • (2005) J. Biol. Chem , vol.280 , pp. 6950-6959
    • Benlloch, M.1    Ortega, A.2    Ferrer, P.3    Segarra, R.4    Obrador, E.5    Asensi, M.6    Carretero, J.7    Estrela, J.M.8
  • 71
    • 33846245015 scopus 로고    scopus 로고
    • The effect of modulation of gamma-glutamyl transpeptidase and nitric oxide synthase activity on GSH homeostasis in HepG2 cells
    • Kwiecien, I.; Rokita, H.; Lorenc-Koci, E.; Sokolowska, M.; Wlodek, L. The effect of modulation of gamma-glutamyl transpeptidase and nitric oxide synthase activity on GSH homeostasis in HepG2 cells. Fundam. Clin. Pharmacol., 2007, 21, 95-103.
    • (2007) Fundam. Clin. Pharmacol , vol.21 , pp. 95-103
    • Kwiecien, I.1    Rokita, H.2    Lorenc-Koci, E.3    Sokolowska, M.4    Wlodek, L.5
  • 74
    • 35948951072 scopus 로고    scopus 로고
    • Akt-mediated activation of HIF-1 in pulmonary vascular endothelial cells by S-nitrosoglutathione
    • Carver, D.J.; Gaston, B.; Deronde, K.; Palmer, L.A. Akt-mediated activation of HIF-1 in pulmonary vascular endothelial cells by S- nitrosoglutathione. Am. J. Respir. Cell Mol. Biol., 2007, 37, 255-263.
    • (2007) Am. J. Respir. Cell Mol. Biol , vol.37
    • Carver, D.J.1    Gaston, B.2    Deronde, K.3    Palmer, L.A.4
  • 75
    • 34250798528 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
    • Grzam, A.; Martin, M.N.; Hell, R.; Meyer, A.J. Gamma-glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis. FEBS Lett., 2007, 581, 3131-3138.
    • (2007) FEBS Lett , vol.581 , pp. 3131-3138
    • Grzam, A.1    Martin, M.N.2    Hell, R.3    Meyer, A.J.4
  • 76
    • 44849096813 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: Novel mechanistic implication for inhibition by glutamine antagonists
    • Wada, K.; Hiratake, J.; Irie, M.; Okada, T.; Yamada, C.; Kumagai, H.; Suzuki, H.; Fukuyama, K. Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists. J. Mol. Biol., 2008, 380, 361-372.
    • (2008) J. Mol. Biol , vol.380 , pp. 361-372
    • Wada, K.1    Hiratake, J.2    Irie, M.3    Okada, T.4    Yamada, C.5    Kumagai, H.6    Suzuki, H.7    Fukuyama, K.8
  • 77
    • 64849086541 scopus 로고    scopus 로고
    • Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis
    • Williams, K.; Cullati, S.; Sand, A.; Biterova, E.I.; Barycki, J.J. Crystal structure of acivicin-inhibited gamma- glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis. Biochemistry, 2009, 48, 2459-2467.
    • (2009) Biochemistry , vol.48 , pp. 2459-2467
    • Williams, K.1    Cullati, S.2    Sand, A.3    Biterova, E.I.4    Barycki, J.J.5
  • 79
    • 0031982179 scopus 로고    scopus 로고
    • The mechanism of glutamine-dependent amidotransferases
    • Massiere, F.; Badet-Denisot, M.A. The mechanism of glutamine- dependent amidotransferases. Cell Mol. Life Sci., 1998, 54, 205-222.
    • (1998) Cell Mol. Life Sci , vol.54
    • Massiere, F.1    Badet-Denisot, M.A.2
  • 80
    • 0025232412 scopus 로고
    • Metabolism and action of amino acid analog anti-cancer agents
    • Ahluwalia, G.S.; Grem, J.L.; Hao, Z.; Cooney, D.A. Metabolism and action of amino acid analog anti-cancer agents. Pharmacol. Ther., 1990, 46, 243-271.
    • (1990) Pharmacol. Ther , vol.46 , pp. 243-271
    • Ahluwalia, G.S.1    Grem, J.L.2    Hao, Z.3    Cooney, D.A.4
  • 82
    • 0018939925 scopus 로고
    • Mechanism of inactivation of glutamine amidotransferases by the antitumor drug L-(alpha S, 5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (AT-125)
    • Tso, J.Y.; Bower, S.G.; Zalkin, H. Mechanism of inactivation of glutamine amidotransferases by the antitumor drug L-(alpha S, 5S)- alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (AT- 125). J. Biol. Chem., 1980, 255, 6734-6738.
    • (1980) J. Biol. Chem , vol.255 , pp. 6734-6738
    • Tso, J.Y.1    Bower, S.G.2    Zalkin, H.3
  • 83
    • 0035969949 scopus 로고    scopus 로고
    • Mechanism for acivicin inactivation of triad glutamine amidotransferases
    • Chittur, S.V.; Klem, T.J.; Shafer, C.M.; Davisson, V.J. Mechanism for acivicin inactivation of triad glutamine amidotransferases. Biochemistry, 2001, 40, 876-887.
    • (2001) Biochemistry , vol.40 , pp. 876-887
    • Chittur, S.V.1    Klem, T.J.2    Shafer, C.M.3    Davisson, V.J.4
  • 84
    • 0037040295 scopus 로고    scopus 로고
    • Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin
    • Miles, B.W.; Thoden, J.B.; Holden, H.M.; Raushel, F.M. Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin. J. Biol. Chem., 2002, 277, 4368-4373.
    • (2002) J. Biol. Chem , vol.277 , pp. 4368-4373
    • Miles, B.W.1    Thoden, J.B.2    Holden, H.M.3    Raushel, F.M.4
  • 85
    • 33746047636 scopus 로고    scopus 로고
    • Gamma-(monophenyl)phosphono glutamate analogues as mechanism-based inhibitors of gamma-glutamyl transpeptidase
    • Han, L.; Hiratake, J.; Tachi, N.; Suzuki, H.; Kumagai, H.; Sakata, K. Gamma-(monophenyl)phosphono glutamate analogues as mechanism-based inhibitors of gamma-glutamyl transpeptidase. Bioorg. Med. Chem., 2006, 14, 6043-6054.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 6043-6054
    • Han, L.1    Hiratake, J.2    Tachi, N.3    Suzuki, H.4    Kumagai, H.5    Sakata, K.6
  • 86
    • 33846845012 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase
    • Han, L.; Hiratake, J.; Kamiyama, A.; Sakata, K. Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase. Biochemistry, 2007, 46, 1432-1447.
    • (2007) Biochemistry , vol.46 , pp. 1432-1447
    • Han, L.1    Hiratake, J.2    Kamiyama, A.3    Sakata, K.4
  • 87
    • 2942585593 scopus 로고    scopus 로고
    • Synthesis of S-alkyl L-homocysteine analogues of glutathione and their kinetic studies with gamma-glutamyl transpeptidase
    • Lherbet, C.; Gravel, C.; Keillor, J.W. Synthesis of S-alkyl L- homocysteine analogues of glutathione and their kinetic studies with gamma-glutamyl transpeptidase. Bioorg. Med. Chem. Lett., 2004, 14, 3451-3455.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 3451-3455
    • Lherbet, C.1    Gravel, C.2    Keillor, J.W.3
  • 88
    • 1642443170 scopus 로고    scopus 로고
    • Probing the stereochemistry of the active site of gamma-glutamyl transpeptidase using sulfur derivatives of l-glutamic acid
    • Lherbet, C.; Keillor, J.W. Probing the stereochemistry of the active site of gamma-glutamyl transpeptidase using sulfur derivatives of l- glutamic acid. Org. Biomol. Chem., 2004, 2, 238-245.
    • (2004) Org. Biomol. Chem , vol.2 , pp. 238-245
    • Lherbet, C.1    Keillor, J.W.2
  • 89
    • 66149155033 scopus 로고    scopus 로고
    • A novel, species-specific class of uncompetitive inhibitors of gamma-glutamyl transpeptidase
    • King, J.B.; West, M.B.; Cook, P.F.; Hanigan, M.H. A novel, species-specific class of uncompetitive inhibitors of gamma- glutamyl transpeptidase. J. Biol. Chem., 2009, 284, 9059-9065.
    • (2009) J. Biol. Chem , vol.284 , pp. 9059-9065
    • King, J.B.1    West, M.B.2    Cook, P.F.3    Hanigan, M.H.4
  • 90
    • 0030802906 scopus 로고    scopus 로고
    • Pulmonary oxidative stress response in young children with cystic fibrosis
    • Hull, J.; Vervaart, P.; Grimwood, K.; Phelan, P. Pulmonary oxidative stress response in young children with cystic fibrosis. Thorax, 1997, 52, 557-560.
    • (1997) Thorax , vol.52 , pp. 557-560
    • Hull, J.1    Vervaart, P.2    Grimwood, K.3    Phelan, P.4


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