메뉴 건너뛰기




Volumn 302, Issue 10, 2012, Pages

Inactivation of the potent Pseudomonas aeruginosa cytotoxin pyocyanin by airway peroxidases and nitrite

Author keywords

1 hydroxyphenazine; Lactoperoxidase; Myeloperoxidase; Nitration; Oxidation; Phenazines

Indexed keywords

CYTOTOXIN; HYDROGEN PEROXIDE; LACTOPEROXIDASE; MYELOPEROXIDASE; NITRIC OXIDE; NITRITE; PEROXIDASE; PYOCYANINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SODIUM NITRITE; SUPEROXIDE;

EID: 84862061460     PISSN: 10400605     EISSN: 15221504     Source Type: Journal    
DOI: 10.1152/ajplung.00172.2011     Document Type: Article
Times cited : (17)

References (42)
  • 3
    • 0027082355 scopus 로고
    • Interaction of the Pseudomonas aeruginosa secretory products pyocyanin and pyochelin generates hydroxyl radical and causes synergistic damage to endothelial cells: Implications for pseudomonasassociated tissue injury
    • Britigan BE, Roeder TL, Rasmussen GT, Shasby DM, McCormick ML, Cox CD. Interaction of the Pseudomonas aeruginosa secretory products pyocyanin and pyochelin generates hydroxyl radical and causes synergistic damage to endothelial cells: implications for pseudomonasassociated tissue injury. J Clin Invest 90: 2187-2196, 1992.
    • (1992) J Clin Invest , vol.90 , pp. 2187-2196
    • Britigan, B.E.1    Roeder, T.L.2    Rasmussen, G.T.3    Shasby, D.M.4    McCormick, M.L.5    Cox, C.D.6
  • 7
  • 8
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • Davies MJ, Hawkins CL, Pattison DL, Rees MD. Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxid Redox Signal 10: 1199-1234, 2011.
    • (2011) Antioxid Redox Signal , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.L.3    Rees, M.D.4
  • 9
    • 0021115992 scopus 로고
    • Free radical production from the aerobic oxidation of reduced pyridine nucleotides catalyzed by phenazine derivatives
    • Davis G, Thornalley PJ. Free radical production from the aerobic oxidation of reduced pyridine nucleotides catalyzed by phenazine derivatives. Biochim Biophys Acta 724: 456-464, 1983.
    • (1983) Biochim Biophys Acta , vol.724 , pp. 456-464
    • Davis, G.1    Thornalley, P.J.2
  • 11
    • 0024511906 scopus 로고
    • Pathogenetic mechanisms in lung disease caused by Pseudomonas aeruginosa
    • Fick RB Jr, Hata JS. Pathogenetic mechanisms in lung disease caused by Pseudomonas aeruginosa. Chest 95: 206S-213S, 1989.
    • (1989) Chest , vol.95
    • Fick Jr., R.B.1    Hata, J.S.2
  • 12
    • 0030249849 scopus 로고    scopus 로고
    • Superoxide production by the mycobacterial and pseudomonad quinoid pigments phthiocol and pyocyanine in human lung cells
    • Gardner PR. Superoxide production by the mycobacterial and pseudomonad quinoid pigments phthiocol and pyocyanine in human lung cells. Arch Biochem Biophys 333: 267-274, 1996.
    • (1996) Arch Biochem Biophys , vol.333 , pp. 267-274
    • Gardner, P.R.1
  • 14
    • 0018666716 scopus 로고
    • Intracellular production of superoxide radical and hydrogen peroxide by redox active compounds
    • Hassan HM, Fridovich I. Intracellular production of superoxide radical and hydrogen peroxide by redox active compounds. Arch Biochem Biophys 196: 385-395, 1979.
    • (1979) Arch Biochem Biophys , vol.196 , pp. 385-395
    • Hassan, H.M.1    Fridovich, I.2
  • 15
    • 0018818958 scopus 로고
    • Mechanism of the antibiotic action of pyocyanine
    • Hassan HM, Fridovich I. Mechanism of the antibiotic action of pyocyanine. J Bacteriol 141: 156-163, 1980.
    • (1980) J Bacteriol , vol.141 , pp. 156-163
    • Hassan, H.M.1    Fridovich, I.2
  • 16
    • 0026322194 scopus 로고
    • Response of Pseudomonas aeruginosa to pyocyanin: Mechanisms of resistance, antioxidant defenses, and demonstration of a manganese-cofactored superoxide dismutase
    • Hassett DJ, Charniga L, Bean K, Ohman DE, Cohen MS. Response of Pseudomonas aeruginosa to pyocyanin: mechanisms of resistance, antioxidant defenses, and demonstration of a manganese-cofactored superoxide dismutase. Infect Immun 60: 328-336, 1992.
    • (1992) Infect Immun , vol.60 , pp. 328-336
    • Hassett, D.J.1    Charniga, L.2    Bean, K.3    Ohman, D.E.4    Cohen, M.S.5
  • 17
    • 0842346487 scopus 로고    scopus 로고
    • The corneal response to Pseudomonas aeruginosa infection
    • Hazlett LD. The corneal response to Pseudomonas aeruginosa infection. Prog Retin Eye Res 23: 1-30, 2004.
    • (2004) Prog Retin Eye Res , vol.23 , pp. 1-30
    • Hazlett, L.D.1
  • 18
    • 0023019283 scopus 로고
    • On the molecular mechanism of lactoperoxidase-catalyzed H2O2 metabolism and irreversible enzyme inactivation
    • Jenzer H, Jones W, Kohler H. On the molecular mechanism of lactoperoxidase-catalyzed H2O2 metabolism and irreversible enzyme inactivation. J Biol Chem 261: 15550-15556, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 15550-15556
    • Jenzer, H.1    Jones, W.2    Kohler, H.3
  • 19
    • 23044512239 scopus 로고    scopus 로고
    • Modulation of lung epithelial functions by Pseudomonas aeruginosa
    • Lau GW, Hassett DJ, Britigan BE. Modulation of lung epithelial functions by Pseudomonas aeruginosa. Trends Microbiol 13: 389-397, 2005.
    • (2005) Trends Microbiol , vol.13 , pp. 389-397
    • Lau, G.W.1    Hassett, D.J.2    Britigan, B.E.3
  • 20
    • 9644257146 scopus 로고    scopus 로고
    • The role of pyocyanin in Pseudomonas aeruginosa infection
    • Lau GW, Hassett DJ, Ran H, Kong F. The role of pyocyanin in Pseudomonas aeruginosa infection. Trends Mol Med 10: 599-606, 2004.
    • (2004) Trends Mol Med , vol.10 , pp. 599-606
    • Lau, G.W.1    Hassett, D.J.2    Ran, H.3    Kong, F.4
  • 21
    • 3042550379 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa pyocyanin is critical for lung infection in mice
    • Lau GW, Ran H, Kong F, Hassett DJ, Mavrodi D. Pseudomonas aeruginosa pyocyanin is critical for lung infection in mice. Infect Immun 72: 4275-4278, 2004.
    • (2004) Infect Immun , vol.72 , pp. 4275-4278
    • Lau, G.W.1    Ran, H.2    Kong, F.3    Hassett, D.J.4    Mavrodi, D.5
  • 22
    • 0033847562 scopus 로고    scopus 로고
    • Establishment of Pseudomonas aeruginosa infection: Lessons from a versatile opportunist
    • Lyczak JB, Cannon CL, Pier GB. Establishment of Pseudomonas aeruginosa infection: lessons from a versatile opportunist. Microbes Infect 2: 1051-1060, 2000.
    • (2000) Microbes Infect , vol.2 , pp. 1051-1060
    • Lyczak, J.B.1    Cannon, C.L.2    Pier, G.B.3
  • 23
    • 78049271821 scopus 로고    scopus 로고
    • Sodium nitrite-mediated killing of the major cystic fibrosis pathogens Pseudomonas aeruginosa, Staphylococcus aureus, and Burkholderia cepacia under anaerobic planktonic and biofilm conditions
    • Major TA, Panmanee W, Mortensen JE, Gray LD, Hoglen N, Hassett DJ. Sodium nitrite-mediated killing of the major cystic fibrosis pathogens Pseudomonas aeruginosa, Staphylococcus aureus, and Burkholderia cepacia under anaerobic planktonic and biofilm conditions. Antimicrob Agents Chemother 54: 4671-4677, 2010.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 4671-4677
    • Major, T.A.1    Panmanee, W.2    Mortensen, J.E.3    Gray, L.D.4    Hoglen, N.5    Hassett, D.J.6
  • 24
    • 0035685204 scopus 로고    scopus 로고
    • Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1
    • Mavrodi DV, Bonsall RF, Delaney SM, Soule MJ, Phillips G, Thomashow LS. Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1. J Bacteriol 183: 6454-6465, 2001.
    • (2001) J Bacteriol , vol.183 , pp. 6454-6465
    • Mavrodi, D.V.1    Bonsall, R.F.2    Delaney, S.M.3    Soule, M.J.4    Phillips, G.5    Thomashow, L.S.6
  • 25
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxidants in microbial pathophysiology
    • Miller RA, Britigan BE. Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10: 1-18, 1997.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 26
    • 1542314758 scopus 로고    scopus 로고
    • Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide
    • Monzani E, Roncone R, Galliano M, Koppenol WH, Casella L. Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide. Eur J Biochem 271: 895-906, 2004.
    • (2004) Eur J Biochem , vol.271 , pp. 895-906
    • Monzani, E.1    Roncone, R.2    Galliano, M.3    Koppenol, W.H.4    Casella, L.5
  • 28
    • 0015416039 scopus 로고
    • Enthalpy of decomposition of hydrogen peroxide by catalase at 25 degrees C (with molar extinction coefficients of H2O2 solutions in the UV)
    • Nelson DP, Kiesow LA. Enthalpy of decomposition of hydrogen peroxide by catalase at 25 degrees C (with molar extinction coefficients of H2O2 solutions in the UV). Anal Biochem 49: 474-478, 1972.
    • (1972) Anal Biochem , vol.49 , pp. 474-478
    • Nelson, D.P.1    Kiesow, L.A.2
  • 31
    • 0033372542 scopus 로고    scopus 로고
    • Nitrite- and peroxidedependent oxidation pathways of dopamine: 6- nitrodopamine and 6-hydroxydopamine formation as potential contributory mechanisms of oxidative stress- and nitric oxide-induced neurotoxicity in neuronal degeneration
    • Palumbo A, Napolitano A, Barone P, d'Ischia M. Nitrite- and peroxidedependent oxidation pathways of dopamine: 6- nitrodopamine and 6-hydroxydopamine formation as potential contributory mechanisms of oxidative stress- and nitric oxide-induced neurotoxicity in neuronal degeneration. Chem Res Toxicol 12: 1213-1222, 1999.
    • (1999) Chem Res Toxicol , vol.12 , pp. 1213-1222
    • Palumbo, A.1    Napolitano, A.2    Barone, P.3    D'ischia, M.4
  • 32
    • 0022426881 scopus 로고
    • Reactions of nitrogen dioxide in aqueous model systems: Oxidation of tyrosine units in peptides and proteins
    • Prütz WA, Mönig H, Butler J, Land EJ. Reactions of nitrogen dioxide in aqueous model systems: Oxidation of tyrosine units in peptides and proteins. Arch Biochem Biophys 243: 125-134, 1985.
    • (1985) Arch Biochem Biophys , vol.243 , pp. 125-134
    • Prütz, W.A.1    Mönig, H.2    Butler, J.3    Land, E.J.4
  • 33
    • 58149290251 scopus 로고    scopus 로고
    • The Pseudomonas toxin pyocyanin inhibits the dual oxidase-based antimicrobial system as it imposes oxidative stress on airway epithelial cells
    • Rada B, Lekstron K, Damain S, Dupuy C, Leto TL. The Pseudomonas toxin pyocyanin inhibits the dual oxidase-based antimicrobial system as it imposes oxidative stress on airway epithelial cells. J Immunol 181: 4884-4893, 2008.
    • (2008) J Immunol , vol.181 , pp. 4884-4893
    • Rada, B.1    Lekstron, K.2    Damain, S.3    Dupuy, C.4    Leto, T.L.5
  • 34
    • 0344198520 scopus 로고    scopus 로고
    • Human targets of Pseudomonas aeruginosa pyocyanin
    • Ran H, Hassett DJ, Lau GW. Human targets of Pseudomonas aeruginosa pyocyanin. Proc Natl Acad Sci USA 100: 14315-14320, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14315-14320
    • Ran, H.1    Hassett, D.J.2    Lau, G.W.3
  • 35
    • 0032974902 scopus 로고    scopus 로고
    • 2): An EPR and spin trapping study
    • Reszka KJ, Matuszak Z, Chignell CF, Dillon J. Oxidation of biological electron donors and antioxidants by a reactive lactoperoxidase metabolite from nitrite (NO2): An EPR and spin trapping study. Free Radic Biol Med 26: 669-678, 1999.
    • (1999) Free Radic Biol Med , vol.26 , pp. 669-678
    • Reszka, K.J.1    Matuszak, Z.2    Chignell, C.F.3    Dillon, J.4
  • 36
    • 2342527169 scopus 로고    scopus 로고
    • Oxidation of pyocyanin, a cytotoxic product from Pseudomonas aeruginosa, by microperoxidase 11 and hydrogen peroxide
    • Reszka KJ, O'Malley Y, McCormick ML, Denning GM, Britigan BE. Oxidation of pyocyanin, a cytotoxic product from Pseudomonas aeruginosa, by microperoxidase 11 and hydrogen peroxide. Free Radic Biol Med 36: 1448-1459, 2004.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1448-1459
    • Reszka, K.J.1    O'Malley, Y.2    McCormick, M.L.3    Denning, G.M.4    Britigan, B.E.5
  • 38
    • 0025921582 scopus 로고
    • Sensitivity of bacteria to NaNO2 and to L-arginine-dependent system in murine macrophages
    • Saito S, Onozuka K, Shinomiya H, Nakano M. Sensitivity of bacteria to NaNO2 and to L-arginine-dependent system in murine macrophages. Microbiol Immunol 35: 325-329, 1991.
    • (1991) Microbiol Immunol , vol.35 , pp. 325-329
    • Saito, S.1    Onozuka, K.2    Shinomiya, H.3    Nakano, M.4
  • 40
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidasecatalyzed oxidation of nitrite- A potential additional, mechanism of nitric oxide-dependent toxicity
    • Van der Vliet A, Eiserich JP, Halliwell B, Cross CE. Formation of reactive nitrogen species during peroxidasecatalyzed oxidation of nitrite- A potential additional, mechanism of nitric oxide-dependent toxicity. J Biol Chem 272: 7617-7625, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 7617-7625
    • van der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 41
    • 0023777725 scopus 로고
    • Measurement of Pseudomonas aeruginosa phenazine pigments in sputum and assessment of their contribution to sputum sol toxicity for respiratory epithelium
    • Wilson R, Sykes DA, Watson D, Rutman A, Taylor GW, Cole PJ. Measurement of Pseudomonas aeruginosa phenazine pigments in sputum and assessment of their contribution to sputum sol toxicity for respiratory epithelium. Infect Immun 56: 2515-2517, 1988.
    • (1988) Infect Immun , vol.56 , pp. 2515-2517
    • Wilson, R.1    Sykes, D.A.2    Watson, D.3    Rutman, A.4    Taylor, G.W.5    Cole, P.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.