메뉴 건너뛰기




Volumn 81, Issue , 2015, Pages 38-46

The effects of hypochlorous acid and neutrophil proteases on the structure and function of extracellular superoxide dismutase

Author keywords

Antioxidant; Cathepsin G Free radicals; Extracellular matrix protein; Hypochlorous acid; Inflammation; Neutrophil; Superoxide dismutase

Indexed keywords

CATHEPSIN G; EXTRACELLULAR SUPEROXIDE DISMUTASE; HYPOCHLOROUS ACID; LEUKOCYTE ELASTASE; PROTEINASE; CTSG PROTEIN, HUMAN; HEPARIN; PROTEIN BINDING; SUPEROXIDE DISMUTASE;

EID: 84923366992     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.12.027     Document Type: Article
Times cited : (9)

References (53)
  • 1
    • 18044395714 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase: Structural and functional considerations of a protein shaped by two different disulfide bridge patterns
    • S.V. Petersen, and J.J. Enghild Extracellular superoxide dismutase: structural and functional considerations of a protein shaped by two different disulfide bridge patterns Biomed. Pharmacother. 59 2005 175 182
    • (2005) Biomed. Pharmacother. , vol.59 , pp. 175-182
    • Petersen, S.V.1    Enghild, J.J.2
  • 2
    • 0033591243 scopus 로고    scopus 로고
    • The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis
    • J.J. Enghild, I.B. Thogersen, T.D. Oury, Z. Valnickova, P. Hojrup, and J.D. Crapo The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis J. Biol. Chem. 274 1999 14818 14822
    • (1999) J. Biol. Chem. , vol.274 , pp. 14818-14822
    • Enghild, J.J.1    Thogersen, I.B.2    Oury, T.D.3    Valnickova, Z.4    Hojrup, P.5    Crapo, J.D.6
  • 4
    • 0023109883 scopus 로고
    • Heparin-induced release of extracellular superoxide dismutase to human blood plasma
    • K. Karlsson, and S.L. Marklund Heparin-induced release of extracellular superoxide dismutase to human blood plasma Biochem. J. 242 1987 55 59
    • (1987) Biochem. J. , vol.242 , pp. 55-59
    • Karlsson, K.1    Marklund, S.L.2
  • 9
    • 44449089083 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase inhibits inflammation by preventing oxidative fragmentation of hyaluronan
    • F. Gao, J.R. Koenitzer, J.M. Tobolewski, D. Jiang, J. Liang, P.W. Noble, and T.D. Oury Extracellular superoxide dismutase inhibits inflammation by preventing oxidative fragmentation of hyaluronan J. Biol. Chem. 283 2008 6058 6066
    • (2008) J. Biol. Chem. , vol.283 , pp. 6058-6066
    • Gao, F.1    Koenitzer, J.R.2    Tobolewski, J.M.3    Jiang, D.4    Liang, J.5    Noble, P.W.6    Oury, T.D.7
  • 11
    • 79953238532 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase protects cardiovascular syndecan-1 from oxidative shedding
    • C.R. Kliment, and T.D. Oury Extracellular superoxide dismutase protects cardiovascular syndecan-1 from oxidative shedding Free Radic. Biol. Med. 50 2011 1075 1080
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 1075-1080
    • Kliment, C.R.1    Oury, T.D.2
  • 12
    • 0029848789 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase: A regulator of nitric oxide bioavailability
    • T.D. Oury, B.J. Day, and J.D. Crapo Extracellular superoxide dismutase: a regulator of nitric oxide bioavailability Lab. Invest. 75 1996 617 636
    • (1996) Lab. Invest. , vol.75 , pp. 617-636
    • Oury, T.D.1    Day, B.J.2    Crapo, J.D.3
  • 13
    • 0141864392 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase is a major determinant of nitric oxide bioavailability: In vivo and ex vivo evidence from ecSOD-deficient mice
    • O. Jung, S.L. Marklund, H. Geiger, T. Pedrazzini, R. Busse, and R.P. Brandes Extracellular superoxide dismutase is a major determinant of nitric oxide bioavailability: in vivo and ex vivo evidence from ecSOD-deficient mice Circ. Res. 93 2003 622 629
    • (2003) Circ. Res. , vol.93 , pp. 622-629
    • Jung, O.1    Marklund, S.L.2    Geiger, H.3    Pedrazzini, T.4    Busse, R.5    Brandes, R.P.6
  • 14
    • 84878797878 scopus 로고    scopus 로고
    • Hydrogen peroxide induces modifications of human extracellular superoxide dismutase that results in enzyme inhibition
    • R.H. Gottfredsen, U.G. Larsen, J.J. Enghild, and S.V. Petersen Hydrogen peroxide induces modifications of human extracellular superoxide dismutase that results in enzyme inhibition Redox Biol 1 2013 24 31
    • (2013) Redox Biol , vol.1 , pp. 24-31
    • Gottfredsen, R.H.1    Larsen, U.G.2    Enghild, J.J.3    Petersen, S.V.4
  • 15
    • 79958238542 scopus 로고    scopus 로고
    • Hydrogen peroxide as a signaling molecule
    • E. Veal, and A. Day Hydrogen peroxide as a signaling molecule Antioxid. Redox Signaling 15 2011 147 151
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 147-151
    • Veal, E.1    Day, A.2
  • 18
    • 0031863285 scopus 로고    scopus 로고
    • Expression of extracellular SOD and iNOS in macrophages and smooth muscle cells in human and rabbit atherosclerotic lesions: Colocalization with epitopes characteristic of oxidized LDL and peroxynitrite-modified proteins
    • J.S. Luoma, P. Stralin, S.L. Marklund, T.P. Hiltunen, T. Sarkioja, and S. Yla-Herttuala Expression of extracellular SOD and iNOS in macrophages and smooth muscle cells in human and rabbit atherosclerotic lesions: colocalization with epitopes characteristic of oxidized LDL and peroxynitrite-modified proteins Arterioscler. Thromb. Vasc. Biol. 18 1998 157 167
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 157-167
    • Luoma, J.S.1    Stralin, P.2    Marklund, S.L.3    Hiltunen, T.P.4    Sarkioja, T.5    Yla-Herttuala, S.6
  • 19
    • 84895516620 scopus 로고    scopus 로고
    • The cellular distribution of extracellular superoxide dismutase in macrophages is altered by cellular activation but unaffected by the naturally occurring R213G substitution
    • R.H. Gottfredsen, D.A. Goldstrohm, J.M. Hartney, U.G. Larsen, R.P. Bowler, and S.V. Petersen The cellular distribution of extracellular superoxide dismutase in macrophages is altered by cellular activation but unaffected by the naturally occurring R213G substitution Free Radic. Biol. Med. 69 2014 348 356
    • (2014) Free Radic. Biol. Med. , vol.69 , pp. 348-356
    • Gottfredsen, R.H.1    Goldstrohm, D.A.2    Hartney, J.M.3    Larsen, U.G.4    Bowler, R.P.5    Petersen, S.V.6
  • 21
    • 84859388811 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase inhibits innate immune responses and clearance of an intracellular bacterial infection
    • T.J. Break, S. Jun, M. Indramohan, K.D. Carr, A.N. Sieve, L. Dory, and R.E. Berg Extracellular superoxide dismutase inhibits innate immune responses and clearance of an intracellular bacterial infection J. Immunol. 188 2012 3342 3350
    • (2012) J. Immunol. , vol.188 , pp. 3342-3350
    • Break, T.J.1    Jun, S.2    Indramohan, M.3    Carr, K.D.4    Sieve, A.N.5    Dory, L.6    Berg, R.E.7
  • 22
    • 80255133209 scopus 로고    scopus 로고
    • Regulation of skin inflammation and angiogenesis by EC-SOD via HIF-1α and NF-κB pathways
    • Y. Kim, B.H. Kim, H. Lee, B. Jeon, Y.S. Lee, M.J. Kwon, and T.Y. Kim Regulation of skin inflammation and angiogenesis by EC-SOD via HIF-1α and NF-κB pathways Free Radic. Biol. Med. 51 2011 1985 1995
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1985-1995
    • Kim, Y.1    Kim, B.H.2    Lee, H.3    Jeon, B.4    Lee, Y.S.5    Kwon, M.J.6    Kim, T.Y.7
  • 23
    • 84855378145 scopus 로고    scopus 로고
    • Superoxide dismutase 3 suppresses hyaluronic acid fragments mediated skin inflammation by inhibition of toll-like receptor 4 signaling pathway: Superoxide dismutase 3 inhibits reactive oxygen species-induced trafficking of toll-like receptor 4 to lipid rafts
    • M.J. Kwon, J. Han, B.H. Kim, Y.S. Lee, and T.Y. Kim Superoxide dismutase 3 suppresses hyaluronic acid fragments mediated skin inflammation by inhibition of toll-like receptor 4 signaling pathway: superoxide dismutase 3 inhibits reactive oxygen species-induced trafficking of toll-like receptor 4 to lipid rafts Antioxid. Redox Signaling 16 2012 297 313
    • (2012) Antioxid. Redox Signaling , vol.16 , pp. 297-313
    • Kwon, M.J.1    Han, J.2    Kim, B.H.3    Lee, Y.S.4    Kim, T.Y.5
  • 24
    • 67149103675 scopus 로고    scopus 로고
    • SOD3 reduces inflammatory cell migration by regulating adhesion molecule and cytokine expression
    • J.P. Laurila, L.E. Laatikainen, M.D. Castellone, and M.O. Laukkanen SOD3 reduces inflammatory cell migration by regulating adhesion molecule and cytokine expression PLoS One 4 2009 e5786
    • (2009) PLoS One , vol.4 , pp. e5786
    • Laurila, J.P.1    Laatikainen, L.E.2    Castellone, M.D.3    Laukkanen, M.O.4
  • 27
    • 0035890010 scopus 로고    scopus 로고
    • Altered expression of extracellular superoxide dismutase in mouse lung after bleomycin treatment
    • C.L. Fattman, C.T. Chu, S.M. Kulich, J.J. Enghild, and T.D. Oury Altered expression of extracellular superoxide dismutase in mouse lung after bleomycin treatment Free Radic. Biol. Med. 31 2001 1198 1207
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1198-1207
    • Fattman, C.L.1    Chu, C.T.2    Kulich, S.M.3    Enghild, J.J.4    Oury, T.D.5
  • 29
    • 7044220466 scopus 로고    scopus 로고
    • Redistribution of pulmonary EC-SOD after exposure to asbestos
    • R.J. Tan, C.L. Fattman, S.C. Watkins, and T.D. Oury Redistribution of pulmonary EC-SOD after exposure to asbestos J. Appl. Physiol. 97 2004 2006 2013
    • (2004) J. Appl. Physiol. , vol.97 , pp. 2006-2013
    • Tan, R.J.1    Fattman, C.L.2    Watkins, S.C.3    Oury, T.D.4
  • 31
    • 0030014041 scopus 로고    scopus 로고
    • Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: A simplified, high-yield purification of extracellular superoxide dismutase
    • T.D. Oury, J.D. Crapo, Z. Valnickova, and J.J. Enghild Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase Biochem. J. 317 1996 51 57
    • (1996) Biochem. J. , vol.317 , pp. 51-57
    • Oury, T.D.1    Crapo, J.D.2    Valnickova, Z.3    Enghild, J.J.4
  • 32
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymic function for erythrocuprein (hemocuprein)
    • J.M. McCord, and I. Fridovich Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein) J. Biol. Chem. 244 1969 6049 6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 33
    • 0019792891 scopus 로고
    • Analysis of protein and peptide mixtures: Evaluation of three sodium dodecyl sulfate-polyacrylamide gel electrophoresis buffer systems
    • A.F. Bury Analysis of protein and peptide mixtures: evaluation of three sodium dodecyl sulfate-polyacrylamide gel electrophoresis buffer systems J. Chromatogr. 213 1981 491 500
    • (1981) J. Chromatogr. , vol.213 , pp. 491-500
    • Bury, A.F.1
  • 34
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • P. Matsudaira Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes J. Biol. Chem. 262 1987 10035 10038
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 35
    • 12844261649 scopus 로고    scopus 로고
    • The high concentration of Arg213→Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities
    • S.V. Petersen, D.A. Olsen, J.M. Kenney, T.D. Oury, Z. Valnickova, I.B. Thogersen, J.D. Crapo, and J.J. Enghild The high concentration of Arg213→Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities Biochem. J. 385 2005 427 432
    • (2005) Biochem. J. , vol.385 , pp. 427-432
    • Petersen, S.V.1    Olsen, D.A.2    Kenney, J.M.3    Oury, T.D.4    Valnickova, Z.5    Thogersen, I.B.6    Crapo, J.D.7    Enghild, J.J.8
  • 36
    • 0031441834 scopus 로고    scopus 로고
    • Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach
    • S. Najjam, R.V. Gibbs, M.Y. Gordon, and C.C. Rider Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach Cytokine 9 1997 1013 1022
    • (1997) Cytokine , vol.9 , pp. 1013-1022
    • Najjam, S.1    Gibbs, R.V.2    Gordon, M.Y.3    Rider, C.C.4
  • 37
    • 0006157248 scopus 로고
    • Human copper-containing superoxide dismutase of high molecular weight
    • S.L. Marklund Human copper-containing superoxide dismutase of high molecular weight Proc. Natl. Acad. Sci. USA 79 1982 7634 7638
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 7634-7638
    • Marklund, S.L.1
  • 38
    • 0026764737 scopus 로고
    • The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro
    • T. Adachi, H. Ohta, K. Hayashi, K. Hirano, and S.L. Marklund The site of nonenzymic glycation of human extracellular-superoxide dismutase in vitro Free Radic. Biol. Med. 13 1992 205 210
    • (1992) Free Radic. Biol. Med. , vol.13 , pp. 205-210
    • Adachi, T.1    Ohta, H.2    Hayashi, K.3    Hirano, K.4    Marklund, S.L.5
  • 39
    • 0037022804 scopus 로고    scopus 로고
    • Structural requirements for high-affinity heparin binding: Alanine scanning analysis of charged residues in the C-terminal domain of human extracellular superoxide dismutase
    • P. Stenlund, M.J. Lindberg, and L.A. Tibell Structural requirements for high-affinity heparin binding: alanine scanning analysis of charged residues in the C-terminal domain of human extracellular superoxide dismutase Biochemistry 41 2002 3168 3175
    • (2002) Biochemistry , vol.41 , pp. 3168-3175
    • Stenlund, P.1    Lindberg, M.J.2    Tibell, L.A.3
  • 40
    • 0038825874 scopus 로고    scopus 로고
    • Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation
    • Z. Guan, N.A. Yates, and R. Bakhtiar Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation J. Am. Soc. Mass Spectrom 14 2003 605 613
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , pp. 605-613
    • Guan, Z.1    Yates, N.A.2    Bakhtiar, R.3
  • 41
    • 0025775214 scopus 로고
    • Glycosylation of extracellular superoxide dismutase studied by high-performance liquid chromatography and mass spectrometry
    • M. Stromqvist, J. Holgersson, and B. Samuelsson Glycosylation of extracellular superoxide dismutase studied by high-performance liquid chromatography and mass spectrometry J. Chromatogr. 548 1991 293 301
    • (1991) J. Chromatogr. , vol.548 , pp. 293-301
    • Stromqvist, M.1    Holgersson, J.2    Samuelsson, B.3
  • 42
    • 0029992837 scopus 로고    scopus 로고
    • The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid
    • L.M. Carlsson, S.L. Marklund, and T. Edlund The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid Proc. Natl. Acad. Sci. USA 93 1996 5219 5222
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5219-5222
    • Carlsson, L.M.1    Marklund, S.L.2    Edlund, T.3
  • 43
    • 2542509037 scopus 로고    scopus 로고
    • Determination of the structural role of the N-terminal domain of human extracellular superoxide dismutase by use of protein fusions
    • L.A. Tibell, E. Skarfstad, and B.H. Jonsson Determination of the structural role of the N-terminal domain of human extracellular superoxide dismutase by use of protein fusions Biochim. Biophys. Acta 1292 1996 47 52
    • (1996) Biochim. Biophys. Acta , vol.1292 , pp. 47-52
    • Tibell, L.A.1    Skarfstad, E.2    Jonsson, B.H.3
  • 44
    • 0030722746 scopus 로고    scopus 로고
    • Subunit interaction in extracellular superoxide dismutase: Effects of mutations in the N-terminal domain
    • P. Stenlund, D. Andersson, and L.A. Tibell Subunit interaction in extracellular superoxide dismutase: effects of mutations in the N-terminal domain Protein Sci. 6 1997 2350 2358
    • (1997) Protein Sci. , vol.6 , pp. 2350-2358
    • Stenlund, P.1    Andersson, D.2    Tibell, L.A.3
  • 45
    • 84873736060 scopus 로고    scopus 로고
    • Loss of extracellular superoxide dismutase induces severe IL-23-mediated skin inflammation in mice
    • Y.S. Lee, I.S. Cheon, B.H. Kim, M.J. Kwon, H.W. Lee, and T.Y. Kim Loss of extracellular superoxide dismutase induces severe IL-23-mediated skin inflammation in mice J. Invest. Dermatol. 133 2013 732 741
    • (2013) J. Invest. Dermatol. , vol.133 , pp. 732-741
    • Lee, Y.S.1    Cheon, I.S.2    Kim, B.H.3    Kwon, M.J.4    Lee, H.W.5    Kim, T.Y.6
  • 47
    • 0036828212 scopus 로고    scopus 로고
    • Oxidation of Cu, Zn-superoxide dismutase by the myeloperoxidase/hydrogen peroxide/chloride system: Functional and structural effects
    • F. Auchere, and C. Capeillere-Blandin Oxidation of Cu, Zn-superoxide dismutase by the myeloperoxidase/hydrogen peroxide/chloride system: functional and structural effects Free Radic. Res. 36 2002 1185 1198
    • (2002) Free Radic. Res. , vol.36 , pp. 1185-1198
    • Auchere, F.1    Capeillere-Blandin, C.2
  • 48
    • 0023554040 scopus 로고
    • Action of hypochlorous acid on the antioxidant protective enzymes superoxide dismutase, catalase and glutathione peroxidase
    • O.I. Aruoma, and B. Halliwell Action of hypochlorous acid on the antioxidant protective enzymes superoxide dismutase, catalase and glutathione peroxidase Biochem. J. 248 1987 973 976
    • (1987) Biochem. J. , vol.248 , pp. 973-976
    • Aruoma, O.I.1    Halliwell, B.2
  • 49
    • 0344410068 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of amino acids, peptides and proteins
    • C.L. Hawkins, D.I. Pattison, and M.J. Davies Hypochlorite-induced oxidation of amino acids, peptides and proteins Amino Acids 25 2003 259 274
    • (2003) Amino Acids , vol.25 , pp. 259-274
    • Hawkins, C.L.1    Pattison, D.I.2    Davies, M.J.3
  • 50
    • 33745559712 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Specific regulators of inflammation
    • C.T. Pham Neutrophil serine proteases: specific regulators of inflammation Nat. Rev. Immunol. 6 2006 541 550
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 541-550
    • Pham, C.T.1
  • 51
    • 78149485386 scopus 로고    scopus 로고
    • How immune peptidases change specificity: Cathepsin G gained tryptic function but lost efficiency during primate evolution
    • W.W. Raymond, N.N. Trivedi, A. Makarova, M. Ray, C.S. Craik, and G.H. Caughey How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution J. Immunol. 185 2010 5360 5368
    • (2010) J. Immunol. , vol.185 , pp. 5360-5368
    • Raymond, W.W.1    Trivedi, N.N.2    Makarova, A.3    Ray, M.4    Craik, C.S.5    Caughey, G.H.6
  • 52
    • 0028865394 scopus 로고
    • Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • C.A. Owen, M.A. Campbell, P.L. Sannes, S.S. Boukedes, and E.J. Campbell Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases J. Cell Biol. 131 1995 775 789
    • (1995) J. Cell Biol. , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.4    Campbell, E.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.