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Volumn 288, Issue 25, 2013, Pages 18421-18428

Selective metabolism of hypothiocyanous acid by mammalian thioredoxin reductase promotes lung innate immunity and antioxidant defense

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT DEFENSE; INNATE IMMUNITY; MAMMALIAN CELLS; THIOREDOXIN REDUCTASE;

EID: 84880052989     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.468090     Document Type: Article
Times cited : (63)

References (47)
  • 1
    • 84868456659 scopus 로고    scopus 로고
    • Thiocyanate: A potentially useful therapeutic agent with host defense and antioxidant properties
    • Chandler, J. D., and Day, B. J. (2012) Thiocyanate: A potentially useful therapeutic agent with host defense and antioxidant properties. Biochem. Pharmacol. 84, 1381-1387
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 1381-1387
    • Chandler, J.D.1    Day, B.J.2
  • 2
    • 33750054080 scopus 로고    scopus 로고
    • Lactoperoxidase-catalyzed oxidation of thiocyanate by hydrogen peroxide: A reinvestigation of hypothiocyanite by nuclear magnetic resonance and optical spectroscopy
    • DOI 10.1021/bi061015y
    • Nagy, P., Alguindigue, S. S., and Ashby, M. T. (2006) Lactoperoxidasecatalyzed oxidation of thiocyanate by hydrogen peroxide: A reinvestigation of hypothiocyanite by nuclear magnetic resonance and optical spectroscopy. Biochemistry 45, 12610-12616 (Pubitemid 44583702)
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12610-12616
    • Nagy, P.1    Alguindigue, S.S.2    Ashby, M.T.3
  • 3
    • 0030660227 scopus 로고    scopus 로고
    • Thiocyanate and chloride as competing substrates for myeloperoxidase
    • van Dalen, C. J., Whitehouse, M. W., Winterbourn, C. C., and Kettle, A. J. (1997) Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem. J. 327, 487-492 (Pubitemid 27477827)
    • (1997) Biochemical Journal , vol.327 , Issue.2 , pp. 487-492
    • Van Dalen, C.J.1    Whitehouse, M.W.2    Winterbourn, C.C.3    Kettle, A.J.4
  • 5
    • 72749119238 scopus 로고    scopus 로고
    • Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione
    • Nagy, P., Jameson, G. N. L., and Winterbourn, C. C. (2009) Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione. Chem. Res. Toxicol. 22, 1833-1840
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1833-1840
    • Nagy, P.1    Jameson, G.N.L.2    Winterbourn, C.C.3
  • 6
    • 0017239932 scopus 로고
    • Nonspecific bactericidal activity of the lactoperoxidase-thiocyanate- hydrogen peroxide system of milk against Escherichia coli and some Gram-negative pathogens
    • Reiter, B., Marshall, V. M. E., BjörckL, and Rosén, C.-G. (1976) Nonspecific bactericidal activity of the lactoperoxidase-thiocyanate- hydrogen peroxide system of milk against Escherichia coli and some Gram-negative pathogens. Infect. Immun. 13, 800-807
    • (1976) Infect. Immun. , vol.13 , pp. 800-807
    • Reiter, B.1    Marshall, V.M.E.2    Björck, L.3    Rosén, C.-G.4
  • 7
    • 0021968134 scopus 로고
    • Antibacterial effect of lactoperoxidase and myeloperoxidase against Bacillus cereus
    • Tenovuo, J., Mäkinen, K. K., and Sievers, G. (1985) Antibacterial effect of lactoperoxidase and myeloperoxidase against Bacillus cereus. Antimicrob. Agents Chemother. 27, 96-101 (Pubitemid 15198162)
    • (1985) Antimicrobial Agents and Chemotherapy , vol.27 , Issue.1 , pp. 96-101
    • Tenovuo, J.1    Makinen, K.K.2    Sievers, G.3
  • 8
    • 0028815793 scopus 로고
    • Thiocyanate, a plausible physiological electron donor of gastric peroxidase
    • Das, D., De, P. K., and Banerjee, R. K. (1995) Thiocyanate, a plausible physiological electron donor of gastric peroxidase. Biochem. J. 305, 59-64
    • (1995) Biochem. J. , vol.305 , pp. 59-64
    • Das, D.1    De, P.K.2    Banerjee, R.K.3
  • 9
    • 0028900396 scopus 로고
    • Inhibition of herpes simplex virus type 1, respiratory syncytial virus and echovirus type 11 by peroxidase-generated hypothiocyanite
    • Mikola, H., Waris, M., and Tenovuo, J. (1995) Inhibition of herpes simplex virus type 1, respiratory syncytial virus and echovirus type 11 by peroxidase-generated hypothiocyanite. Antiviral Res. 26, 161-171
    • (1995) Antiviral Res. , vol.26 , pp. 161-171
    • Mikola, H.1    Waris, M.2    Tenovuo, J.3
  • 10
    • 0026937212 scopus 로고
    • Inhibition of Candida albicans by the peroxidase/ SCN/H2O2 system
    • Lenander-Lumikari, M. (1992) Inhibition of Candida albicans by the peroxidase/ SCN/H2O2 system. Oral. Microbiol. Immunol. 7, 315-320
    • (1992) Oral. Microbiol. Immunol. , vol.7 , pp. 315-320
    • Lenander-Lumikari, M.1
  • 11
    • 73949105483 scopus 로고    scopus 로고
    • The antioxidant role of thiocyanate in the pathogenesis of cystic fibrosis and other inflammation-related diseases
    • Xu, Y., Szép, S., and Lu, Z. (2009) The antioxidant role of thiocyanate in the pathogenesis of cystic fibrosis and other inflammation-related diseases. Proc. Natl. Acad. Sci. U.S.A. 106, 20515-20519
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20515-20519
    • Xu, Y.1    Szép, S.2    Lu, Z.3
  • 12
    • 0020174541 scopus 로고
    • Peroxidase antimicrobial system of human saliva: Hypothiocyanite levels in resting and stimulated saliva
    • Tenovuo, J., Pruitt, K. M., and Thomas, E. L. (1982) Peroxidase antimicrobial system of human saliva: Hypothiocyanite levels in resting and stimulated saliva. J. Dent. Res. 61, 982-985
    • (1982) J. Dent. Res. , vol.61 , pp. 982-985
    • Tenovuo, J.1    Pruitt, K.M.2    Thomas, E.L.3
  • 13
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • DOI 10.1189/jlb.1204697
    • Klebanoff, S. J. (2005) Myeloperoxidase: Friend and foe. J. Leukoc. Biol. 77, 598-625 (Pubitemid 40628741)
    • (2005) Journal of Leukocyte Biology , vol.77 , Issue.5 , pp. 598-625
    • Klebanoff, S.J.1
  • 14
    • 81555212303 scopus 로고    scopus 로고
    • Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases
    • Souza, C. E. A., Maitra, D., Saed, G. M., Diamond, M. P., Moura, A. A., Pennathur, S., and Abu-Soud, H. M. (2011) Hypochlorous acid-induced heme degradation from lactoperoxidase as a novel mechanism of free iron release and tissue injury in inflammatory diseases. PLoS ONE 6, e27641
    • (2011) PLoS ONE , vol.6
    • Souza, C.E.A.1    Maitra, D.2    Saed, G.M.3    Diamond, M.P.4    Moura, A.A.5    Pennathur, S.6    Abu-Soud, H.M.7
  • 15
    • 84862186506 scopus 로고    scopus 로고
    • Oxidation of 2-Cys peroxiredoxins in human endothelial cells by hydrogen peroxide, hypochlorous acid, and chloramines
    • Stacey, M. M., Vissers, M. C. M., and Winterbourn, C. C. (2012) Oxidation of 2-Cys peroxiredoxins in human endothelial cells by hydrogen peroxide, hypochlorous acid, and chloramines. Antioxid. Redox Signal. 17, 411-421
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 411-421
    • Stacey, M.M.1    Vissers, M.C.M.2    Winterbourn, C.C.3
  • 16
    • 77749337726 scopus 로고    scopus 로고
    • Small molecular, macromolecular, and cellular chloramines react with thiocyanate to give the human defense factor hypothiocyanite
    • Xulu, B. A., and Ashby, M. T. (2010) Small molecular, macromolecular, and cellular chloramines react with thiocyanate to give the human defense factor hypothiocyanite. Biochemistry 49, 2068-2074
    • (2010) Biochemistry , vol.49 , pp. 2068-2074
    • Xulu, B.A.1    Ashby, M.T.2
  • 17
    • 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., and Day, B. J. (2010) Hypertonic saline increases lung epithelial lining fluid glutathione and thiocyanate: Two protective CFTR-dependent thiols against oxidative injury. Respir. Res. 11, 119-128
    • (2010) Respir. Res. , vol.11 , pp. 119-128
    • Gould, N.S.1    Gauthier, S.2    Kariya, C.T.3    Min, E.4    Huang, J.5    Day, B.J.6
  • 18
    • 81855198483 scopus 로고    scopus 로고
    • Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: Determination of absolute rate constants and implications for biological damage
    • Skaff, O., Pattison, D. I., Morgan, P. E., Bachana, R., Jain, V. K., Priyadarsini, K. I., and Davies, M. J. (2012) Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: Determination of absolute rate constants and implications for biological damage. Biochem. J. 441, 305-316
    • (2012) Biochem. J. , vol.441 , pp. 305-316
    • Skaff, O.1    Pattison, D.I.2    Morgan, P.E.3    Bachana, R.4    Jain, V.K.5    Priyadarsini, K.I.6    Davies, M.J.7
  • 19
    • 59449105695 scopus 로고    scopus 로고
    • Selenoproteins
    • Lu, J., and Holmgren, A. (2009) Selenoproteins. J. Biol. Chem. 284, 723-727
    • (2009) J. Biol. Chem. , vol.284 , pp. 723-727
    • Lu, J.1    Holmgren, A.2
  • 20
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér, E. S. J., and Holmgren, A. (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267, 6102-6109
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arnér, E.S.J.1    Holmgren, A.2
  • 21
    • 0036629836 scopus 로고    scopus 로고
    • The diversity and evolution of thioredoxin reductase: New perspectives
    • DOI 10.1016/S1471-4922(02)02293-6, PII S1471492202022936
    • Hirt, R. P., Müller, S., Embley, T. M., and Coombs, G. H. (2002) The diversity and evolution of thioredoxin reductase: New perspectives. Trends Parasitol. 18, 302-308 (Pubitemid 35257855)
    • (2002) Trends in Parasitology , vol.18 , Issue.7 , pp. 302-308
    • Hirt, R.P.1    Muller, S.2    Martin Embley, T.3    Coombs, G.H.4
  • 22
    • 79959345933 scopus 로고    scopus 로고
    • Differing views of the role of selenium in thioredoxin reductase
    • Hondal, R. J., and Ruggles, E. L. (2011) Differing views of the role of selenium in thioredoxin reductase. Amino Acids 41, 73-89
    • (2011) Amino Acids , vol.41 , pp. 73-89
    • Hondal, R.J.1    Ruggles, E.L.2
  • 24
    • 53649086809 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae infection and environmental tobacco smoke inhibit lung glutathione adaptive responses and increase oxidative stress
    • Kariya, C., Chu, H. W., Huang, J., Leitner, H., Martin, R. J., and Day, B. J. (2008) Mycoplasma pneumoniae infection and environmental tobacco smoke inhibit lung glutathione adaptive responses and increase oxidative stress. Infect. Immun. 76, 4455-4462
    • (2008) Infect. Immun. , vol.76 , pp. 4455-4462
    • Kariya, C.1    Chu, H.W.2    Huang, J.3    Leitner, H.4    Martin, R.J.5    Day, B.J.6
  • 25
    • 0037439453 scopus 로고    scopus 로고
    • Molar absorption coefficients for the reduced ellman reagent: Reassessment
    • DOI 10.1016/S0003-2697(02)00506-7, PII S0003269702005067
    • Eyer, P., Worek, F., Kiderlen, D., Sinko, G., Stuglin, A., Simeon-Rudolf, V., and Reiner, E. (2003) Molar absorption coefficients for the reduced Ellman reagent: Reassessment. Anal. Biochem. 312, 224-227 (Pubitemid 36151135)
    • (2003) Analytical Biochemistry , vol.312 , Issue.2 , pp. 224-227
    • Eyer, P.1    Worek, F.2    Kiderlen, D.3    Sinko, G.4    Stuglin, A.5    Simeon-Rudolf, V.6    Reiner, E.7
  • 26
    • 0017283326 scopus 로고
    • Molar absorptivities of β-NADH and β-NADPH
    • Ziegenhorn, J., Senn, M., and Bücher, T. (1976) Molar absorptivities of β-NADH and β-NADPH. Clin. Chem. 22, 151-160
    • (1976) Clin. Chem. , vol.22 , pp. 151-160
    • Ziegenhorn, J.1    Senn, M.2    Bücher, T.3
  • 31
    • 33847014053 scopus 로고    scopus 로고
    • Inhibition of thioredoxin reductase by auranofin induces apoptosis in cisplatin-resistant human ovarian cancer cells
    • DOI 10.1016/j.freeradbiomed.2006.12.021, PII S0891584906008148
    • Marzano, C., Gandin, V., Folda, A., Scutari, G., Bindoli, A., and Rigobello, M. P. (2007) Inhibition of thioredoxin reductase by auranofin induces apoptosis in cisplatin-resistant human ovarian cancer cells. Free Radic. Biol. Med. 42, 872-881 (Pubitemid 46274171)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.6 , pp. 872-881
    • Marzano, C.1    Gandin, V.2    Folda, A.3    Scutari, G.4    Bindoli, A.5    Rigobello, M.P.6
  • 34
    • 33845403071 scopus 로고    scopus 로고
    • Thiocyanate-dependent induction of endothelial cell adhesion molecule expression by phagocyte peroxidases
    • Wang, J.-G., Mahmud, S. A., Nguyen, J., and Slungaard, A. (2006) Thiocyanate-dependent induction of endothelial cell adhesion molecule expression by phagocyte peroxidases. J. Immunol. 177, 8714-8722
    • (2006) J. Immunol. , vol.177 , pp. 8714-8722
    • Wang, J.-G.1    Mahmud, S.A.2    Nguyen, J.3    Slungaard, A.4
  • 36
    • 30544453005 scopus 로고    scopus 로고
    • Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride
    • DOI 10.1016/j.abb.2005.07.005, PII S0003986105002882
    • Senthilmohan, R., and Kettle, A. J. (2006) Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride. Arch. Biochem. Biophys. 445, 235-244 (Pubitemid 43082216)
    • (2006) Archives of Biochemistry and Biophysics , vol.445 , Issue.2 , pp. 235-244
    • Senthilmohan, R.1    Kettle, A.J.2
  • 37
    • 0037155914 scopus 로고    scopus 로고
    • Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus
    • DOI 10.1074/jbc.M106134200
    • Chapman, A. L. P., Hampton, M. B., Senthilmohan, R., Winterbourn, C. C., and Kettle, A. J. (2002) Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus. J. Biol. Chem. 277, 9757-9762 (Pubitemid 34968078)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 9757-9762
    • Chapman, A.L.P.1    Hampton, M.B.2    Senthilmohan, R.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 38
    • 0013935126 scopus 로고
    • The inhibition of streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide
    • Oram, J. D., and Reiter, B. (1966) The inhibition of streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide. Biochem. J. 100, 373-381
    • (1966) Biochem. J. , vol.100 , pp. 373-381
    • Oram, J.D.1    Reiter, B.2
  • 39
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • Holmgren, A. (2000) Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid. Redox. Signal. 2, 811-820 (Pubitemid 32062330)
    • (2000) Antioxidants and Redox Signaling , vol.2 , Issue.4 , pp. 811-820
    • Holmgren, A.1
  • 42
    • 0029989505 scopus 로고    scopus 로고
    • Purification of NADH: Hypothiocyanite oxidoreductase in Streptococcus sanguis
    • DOI 10.1006/bmme.1996.0019
    • Courtois, P. H., and Pourtois, M. (1996) Purification of NADH: Hypothiocyanite oxidoreductase in Streptococcus sanguis. Biochem. Mol. Med. 57, 134-138 (Pubitemid 26142734)
    • (1996) Biochemical and Molecular Medicine , vol.57 , Issue.2 , pp. 134-138
    • Courtois, Ph.1    Pourtois, M.2
  • 43
    • 0033520499 scopus 로고    scopus 로고
    • Eosinophil peroxidase nitrates protein tyrosyl residues
    • Wu, W., Chen, Y., and Hazen, S. L. (1999) Eosinophil peroxidase nitrates protein tyrosyl residues. J. Biol. Chem. 274, 25933-25944
    • (1999) J. Biol. Chem. , vol.274 , pp. 25933-25944
    • Wu, W.1    Chen, Y.2    Hazen, S.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.