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Volumn 428, Issue 3, 2010, Pages 473-482

Activation of human pro-urokinase by unrelated proteases secreted by Pseudomonas aeruginosa

Author keywords

Bacterial invasion; Human urokinase; LasB; Plasminogen activation system; Protease IV; Pseudomonas aeruginosa

Indexed keywords

ACTIVATION SYSTEMS; ANGIOSTATIN; BACTERIAL INVASION; DIFFERENT SUBSTRATES; EXTRACELLULAR; MATRIX METALLOPROTEINASE-2; METALLO-PROTEASE; PATHOGENIC BACTERIUM; PLASMINOGEN ACTIVATOR INHIBITOR-1; PROTEOLYTIC SYSTEM; PS. AERUGINOSA; PSEUDOMONAS AERUGINOSA; RECOMBINANT PROTEIN EXPRESSION; SECRETOME; SERINE PROTEASE; THERMOLYSIN;

EID: 77954918983     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20091806     Document Type: Article
Times cited : (19)

References (54)
  • 1
    • 4043122563 scopus 로고    scopus 로고
    • Bioinformatics of proteases in the MEROPS database
    • Barrett, A. J. (2004) Bioinformatics of proteases in the MEROPS database. Curr. Opin. Drug Discov. Dev. 7, 334-341
    • (2004) Curr. Opin. Drug Discov. Dev. , vol.7 , pp. 334-341
    • Barrett, A.J.1
  • 2
    • 3142737933 scopus 로고    scopus 로고
    • The omptin family of enterobacterial surface proteases/adhesins: From housekeeping in Escherichia colito systemic spread of Yersinia pestis
    • Kukkonen, M. and Korhonen, T. K. (2004) The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia colito systemic spread of Yersinia pestis. Int. J. Med. Microbiol. 294, 7-14
    • (2004) Int. J. Med. Microbiol. , vol.294 , pp. 7-14
    • Kukkonen, M.1    Korhonen, T.K.2
  • 3
    • 0028783299 scopus 로고
    • Are bacterial proteinases pathogenic factors?
    • Travis, J., Potempa, J. and Maeda, H. (1995) Are bacterial proteinases pathogenic factors? Trends Microbiol. 3, 405-407
    • (1995) Trends Microbiol. , vol.3 , pp. 405-407
    • Travis, J.1    Potempa, J.2    Maeda, H.3
  • 5
    • 4644242673 scopus 로고    scopus 로고
    • Evasive maneuvers by secreted bacterial proteins to avoid innate immune responses
    • Coombes, B. K., Valdez, Y. and Finlay, B. B. (2004) Evasive maneuvers by secreted bacterial proteins to avoid innate immune responses. Curr. Biol. 14, R856-R867
    • (2004) Curr. Biol. , vol.14
    • Coombes, B.K.1    Valdez, Y.2    Finlay, B.B.3
  • 6
    • 61449163214 scopus 로고    scopus 로고
    • Corruption of innate immunity by bacterial proteases
    • Potempa, J. and Pike, R. N. (2009) Corruption of innate immunity by bacterial proteases. J. Innate Immun. 1, 70-87
    • (2009) J. Innate Immun. , vol.1 , pp. 70-87
    • Potempa, J.1    Pike, R.N.2
  • 7
    • 12944325306 scopus 로고    scopus 로고
    • Bacterial metastasis: The host plasminogen system in bacterial invasion
    • Lahteenmaki, K., Edelman, S. and Korhonen, T. K. (2005) Bacterial metastasis: the host plasminogen system in bacterial invasion. Trends Microbiol. 13, 79-85
    • (2005) Trends Microbiol. , vol.13 , pp. 79-85
    • Lahteenmaki, K.1    Edelman, S.2    Korhonen, T.K.3
  • 8
    • 34548667697 scopus 로고    scopus 로고
    • Fibrinolysis and host response in bacterial infections
    • Bergmann, S. and Hammerschmidt, S. (2007) Fibrinolysis and host response in bacterial infections. Thromb. Haemostasis 98, 512-520
    • (2007) Thromb. Haemostasis , vol.98 , pp. 512-520
    • Bergmann, S.1    Hammerschmidt, S.2
  • 9
    • 34250736946 scopus 로고    scopus 로고
    • Fibrin and fibrinolysis in infection and host defense
    • Degen, J. L., Bugge, T. H. and Goguen, J. D. (2007) Fibrin and fibrinolysis in infection and host defense. J. Thromb. Haemostasis 5, 24-31
    • (2007) J. Thromb. Haemostasis , vol.5 , pp. 24-31
    • Degen, J.L.1    Bugge, T.H.2    Goguen, J.D.3
  • 10
    • 16844384895 scopus 로고    scopus 로고
    • Structure and function of the plasminogen/plasmin system
    • Castellino, F. J. and Ploplis, V. A. (2005) Structure and function of the plasminogen/plasmin system. Thromb. Haemostasis 93, 647-654
    • (2005) Thromb. Haemostasis , vol.93 , pp. 647-654
    • Castellino, F.J.1    Ploplis, V.A.2
  • 11
    • 0034969433 scopus 로고    scopus 로고
    • Elements of the fibrinolytic system
    • Lijnen, H. R. (2001) Elements of the fibrinolytic system. Ann. N.Y. Acad. Sci. 936, 226-236
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 226-236
    • Lijnen, H.R.1
  • 12
    • 0642308407 scopus 로고    scopus 로고
    • Plasminogen activation at the cell surface
    • Ellis, V. (2003) Plasminogen activation at the cell surface. Curr. Top. Dev. Biol. 54, 263-312
    • (2003) Curr. Top. Dev. Biol. , vol.54 , pp. 263-312
    • Ellis, V.1
  • 14
    • 26944437783 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa
    • 6th edn (Mandell, G. L., Bennett, J. E. and Dolin, R., eds), Churchill Livingstone, London
    • Pier, G. B. and Ramphal, R. (2005) Pseudomonas aeruginosa. In Mandell, Douglas and Bennett's Principles and Practice of Infectious Diseases, 6th edn (Mandell, G. L., Bennett, J. E. and Dolin, R., eds), pp. 2587-2615, Churchill Livingstone, London
    • (2005) Mandell, Douglas and Bennett's Principles and Practice of Infectious Diseases , pp. 2587-2615
    • Pier, G.B.1    Ramphal, R.2
  • 15
  • 16
    • 10044291650 scopus 로고    scopus 로고
    • Role of bacterial proteases in pseudomonal and serratial keratitis
    • Matsumoto, K. (2004) Role of bacterial proteases in pseudomonal and serratial keratitis. Biol. Chem. 385, 1007-1016
    • (2004) Biol. Chem. , vol.385 , pp. 1007-1016
    • Matsumoto, K.1
  • 17
    • 45249083027 scopus 로고    scopus 로고
    • A novel secreted protease from Pseudomonas aeruginosa activates NF-κB through protease-activated receptors
    • Kida, Y., Higashimoto, Y., Inoue, H., Shimizu, T. and Kuwano, K. (2008) A novel secreted protease from Pseudomonas aeruginosa activates NF-κB through protease-activated receptors. Cell. Microbiol. 10, 1491-1504
    • (2008) Cell. Microbiol. , vol.10 , pp. 1491-1504
    • Kida, Y.1    Higashimoto, Y.2    Inoue, H.3    Shimizu, T.4    Kuwano, K.5
  • 20
    • 0025906404 scopus 로고
    • Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-Å resolution
    • Thayer, M. M., Flaherty, K. M. and McKay, D. B. (1991) Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-Å resolution. J. Biol. Chem. 266, 2864-2871
    • (1991) J. Biol. Chem. , vol.266 , pp. 2864-2871
    • Thayer, M.M.1    Flaherty, K.M.2    McKay, D.B.3
  • 21
    • 0032530707 scopus 로고    scopus 로고
    • Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 Å resolution
    • Banbula, A., Potempa, J., Travis, J., Fernandez-Catalan, C., Mann, K., Huber, R., Bode, W. and Medrano, F. (1998) Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 Å resolution. Structure 6, 1185-1193 (Pubitemid 28434120)
    • (1998) Structure , vol.6 , Issue.9 , pp. 1185-1193
    • Banbula, A.1    Potempa, J.2    Travis, J.3    Fernandez-Catalan, C.4    Mann, K.5    Huber, R.6    Bode, W.7    Medrano, F.J.8
  • 22
    • 0347479352 scopus 로고    scopus 로고
    • Binding of plasminogen to Pseudomonas aeruginosa results in formation of surface-associated plasmin and enhanced bacterial invasiveness
    • da Silva, C. M., de Abreu Vidipo, L., Nishi, R. and Cristina Plotkowski, M. (2004) Binding of plasminogen to Pseudomonas aeruginosa results in formation of surface-associated plasmin and enhanced bacterial invasiveness. Microb. Pathog. 36, 59-66
    • (2004) Microb. Pathog. , vol.36 , pp. 59-66
    • Da Silva, C.M.1    De Abreu Vidipo, L.2    Nishi, R.3    Cristina Plotkowski, M.4
  • 23
    • 0032479154 scopus 로고    scopus 로고
    • Protease IV, a unique extracellular protease and virulence factor from Pseudomonas aeruginosa
    • Engel, L. S., Hill, J. M., Caballero, A. R., Green, L. C. and O'Callaghan, R. J. (1998) Protease IV, a unique extracellular protease and virulence factor from Pseudomonas aeruginosa. J. Biol. Chem. 273, 16792-16797
    • (1998) J. Biol. Chem. , vol.273 , pp. 16792-16797
    • Engel, L.S.1    Hill, J.M.2    Caballero, A.R.3    Green, L.C.4    O'Callaghan, R.J.5
  • 24
    • 0037107569 scopus 로고    scopus 로고
    • An ELISA avoiding interference by heterophilic antibodies in the measurement of components of the plasminogen activation system in blood
    • Grebenchtchikov, N., Sweep, C. G., Geurts-Moespot, A., Piffanelli, A., Foekens, J. A. and Benraad, T. J. (2002) An ELISA avoiding interference by heterophilic antibodies in the measurement of components of the plasminogen activation system in blood. J. Immunol. Methods 268, 219-231
    • (2002) J. Immunol. Methods , vol.268 , pp. 219-231
    • Grebenchtchikov, N.1    Sweep, C.G.2    Geurts-Moespot, A.3    Piffanelli, A.4    Foekens, J.A.5    Benraad, T.J.6
  • 25
    • 0030945032 scopus 로고    scopus 로고
    • Epitope-mapped monoclonal antibodies as tools for functional and morphological analyses of the human urokinase receptor in tumor tissue
    • Luther, T., Magdolen, V., Albrecht, S., Kasper, M., Riemer, C., Kessler, H., Graeff, H., Muller, M. and Schmitt, M. (1997) Epitope-mapped monoclonal antibodies as tools for functional and morphological analyses of the human urokinase receptor in tumor tissue. Am. J. Pathol. 150, 1231-1244
    • (1997) Am. J. Pathol. , vol.150 , pp. 1231-1244
    • Luther, T.1    Magdolen, V.2    Albrecht, S.3    Kasper, M.4    Riemer, C.5    Kessler, H.6    Graeff, H.7    Muller, M.8    Schmitt, M.9
  • 27
    • 0029612321 scopus 로고
    • The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa
    • McIver, K. S., Kessler, E., Olson, J. C. and Ohman, D. E. (1995) The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. Mol. Microbiol. 18, 877-889
    • (1995) Mol. Microbiol. , vol.18 , pp. 877-889
    • McIver, K.S.1    Kessler, E.2    Olson, J.C.3    Ohman, D.E.4
  • 29
    • 0015546107 scopus 로고
    • Determination of the operational molarity of solutions of bovine α-chymotrypsin, trypsin, thrombin and Factor Xa by spectrofluorimetric titration
    • Jameson, G. W., Roberts, D. V., Adams, R. W., Kyle, W. S. and Elmore, D. T. (1973) Determination of the operational molarity of solutions of bovine α-chymotrypsin, trypsin, thrombin and Factor Xa by spectrofluorimetric titration. Biochem. J. 131, 107-117
    • (1973) Biochem. J. , vol.131 , pp. 107-117
    • Jameson, G.W.1    Roberts, D.V.2    Adams, R.W.3    Kyle, W.S.4    Elmore, D.T.5
  • 30
    • 0027475969 scopus 로고
    • The kinetics of plasminogen activation by thrombin-cleaved pro-urokinase and promotion of its activity by fibrin fragment E-2 and by tissue plasminogen activator
    • Liu, J. N. and Gurewich, V. (1993) The kinetics of plasminogen activation by thrombin-cleaved pro-urokinase and promotion of its activity by fibrin fragment E-2 and by tissue plasminogen activator. Blood 81, 980-987
    • (1993) Blood , vol.81 , pp. 980-987
    • Liu, J.N.1    Gurewich, V.2
  • 31
    • 0028943263 scopus 로고
    • A spectrophotometric assay for the determination of the catalytic efficiency of plasminogen activators using a slowly hydrolyzed plasmin substrate
    • Castro, M. J., Kingston, I. B. and Anderson, S. (1995) A spectrophotometric assay for the determination of the catalytic efficiency of plasminogen activators using a slowly hydrolyzed plasmin substrate. Anal. Biochem. 226, 225-231
    • (1995) Anal. Biochem. , vol.226 , pp. 225-231
    • Castro, M.J.1    Kingston, I.B.2    Anderson, S.3
  • 32
    • 34547622484 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa LasB metalloproteinase regulates the human urokinase-type plasminogen activator receptor through domain-specific endoproteolysis
    • Leduc, D., Beaufort, N., de Bentzmann, S., Rousselle, J. C., Namane, A., Chignard, M. and Pidard, D. (2007) The Pseudomonas aeruginosa LasB metalloproteinase regulates the human urokinase-type plasminogen activator receptor through domain-specific endoproteolysis. Infect. Immun. 75, 3848-3858
    • (2007) Infect. Immun. , vol.75 , pp. 3848-3858
    • Leduc, D.1    Beaufort, N.2    De Bentzmann, S.3    Rousselle, J.C.4    Namane, A.5    Chignard, M.6    Pidard, D.7
  • 33
    • 0028934314 scopus 로고
    • Production of elastase, exotoxin A, and alkaline protease in sputa during pulmonary exacerbation of cystic fibrosis in patients chronically infected by Pseudomonas aeruginosa
    • Jaffar-Bandjee, M. C., Lazdunski, A., Bally, M., Carrere, J., Chazalette, J. P. and Galabert, C. (1995) Production of elastase, exotoxin A, and alkaline protease in sputa during pulmonary exacerbation of cystic fibrosis in patients chronically infected by Pseudomonas aeruginosa. J. Clin. Microbiol. 33, 924-929
    • (1995) J. Clin. Microbiol. , vol.33 , pp. 924-929
    • Jaffar-Bandjee, M.C.1    Lazdunski, A.2    Bally, M.3    Carrere, J.4    Chazalette, J.P.5    Galabert, C.6
  • 35
  • 36
    • 0022980217 scopus 로고
    • Isolation and characterization of a lysine-specific protease from Pseudomonas aeruginosa
    • Elliott, Jr, B. W. and Cohen, C. (1986) Isolation and characterization of a lysine-specific protease from Pseudomonas aeruginosa. J. Biol. Chem. 261, 11259-11265
    • (1986) J. Biol. Chem. , vol.261 , pp. 11259-11265
    • Elliott Jr., B.W.1    Cohen, C.2
  • 37
    • 0942287242 scopus 로고    scopus 로고
    • Pseudomonaskeratitis: Protease IV gene conservation, distribution, and production relative to virulence and other Pseudomonasproteases
    • Caballero, A., Thibodeaux, B., Marquart, M., Traidej, M. and O'Callaghan, R. (2004) Pseudomonaskeratitis: protease IV gene conservation, distribution, and production relative to virulence and other Pseudomonasproteases. Invest. Ophthalmol. Visual Sci. 45, 522-530
    • (2004) Invest. Ophthalmol. Visual Sci. , vol.45 , pp. 522-530
    • Caballero, A.1    Thibodeaux, B.2    Marquart, M.3    Traidej, M.4    O'Callaghan, R.5
  • 40
    • 0037462766 scopus 로고    scopus 로고
    • Identification of the active site residues of Pseudomonas aeruginosa protease IV: Importance of enzyme activity in autoprocessing and activation
    • Traidej, M., Marquart, M. E., Caballero, A. R., Thibodeaux, B. A. and O'Callaghan, R. J. (2003) Identification of the active site residues of Pseudomonas aeruginosa protease IV: importance of enzyme activity in autoprocessing and activation. J. Biol. Chem. 278, 2549-2553
    • (2003) J. Biol. Chem. , vol.278 , pp. 2549-2553
    • Traidej, M.1    Marquart, M.E.2    Caballero, A.R.3    Thibodeaux, B.A.4    O'Callaghan, R.J.5
  • 42
    • 22144469749 scopus 로고    scopus 로고
    • The conversion of active to latent plasminogen activator inhibitor-1 is an energetically silent event
    • Boudier, C., Gils, A., Declerck, P. J. and Bieth, J. G. (2005) The conversion of active to latent plasminogen activator inhibitor-1 is an energetically silent event. Biophys. J. 88, 2848-2854
    • (2005) Biophys. J. , vol.88 , pp. 2848-2854
    • Boudier, C.1    Gils, A.2    Declerck, P.J.3    Bieth, J.G.4
  • 43
    • 18244426126 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa virulence factors delay airway epithelial wound repair by altering the actin cytoskeleton and inducing overactivation of epithelial matrix metalloproteinase-2
    • de Bentzmann, S., Polette, M., Zahm, J. M., Hinnrasky, J., Kileztky, C., Bajolet, O., Klossek, J. M., Filloux, A., Lazdunski, A. and Puchelle, E. (2000) Pseudomonas aeruginosa virulence factors delay airway epithelial wound repair by altering the actin cytoskeleton and inducing overactivation of epithelial matrix metalloproteinase-2. Lab. Invest. 80, 209-219
    • (2000) Lab. Invest. , vol.80 , pp. 209-219
    • De Bentzmann, S.1    Polette, M.2    Zahm, J.M.3    Hinnrasky, J.4    Kileztky, C.5    Bajolet, O.6    Klossek, J.M.7    Filloux, A.8    Lazdunski, A.9    Puchelle, E.10
  • 45
    • 0035816636 scopus 로고    scopus 로고
    • The profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis cleaves and inactivates plasminogen activator inhibitor type 1
    • Urano, T., Ihara, H., Umemura, K., Suzuki, Y., Oike, M., Akita, S., Tsukamoto, Y., Suzuki, I. and Takada, A. (2001) The profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis cleaves and inactivates plasminogen activator inhibitor type 1. J. Biol. Chem. 276, 24690-24696
    • (2001) J. Biol. Chem. , vol.276 , pp. 24690-24696
    • Urano, T.1    Ihara, H.2    Umemura, K.3    Suzuki, Y.4    Oike, M.5    Akita, S.6    Tsukamoto, Y.7    Suzuki, I.8    Takada, A.9
  • 46
    • 37749038976 scopus 로고    scopus 로고
    • Immune evasion of the human pathogen Pseudomonas aeruginosa: Elongation factor Tuf is a factor H and plasminogen binding protein
    • Kunert, A., Losse, J., Gruszin, C., Huhn, M., Kaendler, K., Mikkat, S., Volke, D., Hoffmann, R., Jokiranta, T. S., Seeberger, H. et al. (2007) Immune evasion of the human pathogen Pseudomonas aeruginosa: elongation factor Tuf is a factor H and plasminogen binding protein. J. Immunol. 179, 2979-2988
    • (2007) J. Immunol. , vol.179 , pp. 2979-2988
    • Kunert, A.1    Losse, J.2    Gruszin, C.3    Huhn, M.4    Kaendler, K.5    Mikkat, S.6    Volke, D.7    Hoffmann, R.8    Jokiranta, T.S.9    Seeberger, H.10
  • 47
    • 0025004988 scopus 로고
    • Receptors for human plasminogen on Gram-negative bacteria
    • Ullberg, M., Kronvall, G., Karlsson, I. and Wiman, B. (1990) Receptors for human plasminogen on Gram-negative bacteria. Infect. Immun. 58, 21-25
    • (1990) Infect. Immun. , vol.58 , pp. 21-25
    • Ullberg, M.1    Kronvall, G.2    Karlsson, I.3    Wiman, B.4
  • 49
    • 0028148746 scopus 로고
    • Human urokinase, a serine proteinase, potentiates the in vitro growth of micro-organisms which commonly infect burn patients
    • Hart, D. A. and Woods, D. E. (1994) Human urokinase, a serine proteinase, potentiates the in vitro growth of micro-organisms which commonly infect burn patients. J. Med. Microbiol. 41, 264-271
    • (1994) J. Med. Microbiol. , vol.41 , pp. 264-271
    • Hart, D.A.1    Woods, D.E.2
  • 50
    • 0033041832 scopus 로고    scopus 로고
    • Effect of urokinase on the extracellular virulence properties of Pseudomonas aeruginosa and Burkholderia cepacia
    • Heys, S. J., Orton, S. L. and Allison, D. G. (1999) Effect of urokinase on the extracellular virulence properties of Pseudomonas aeruginosa and Burkholderia cepacia. J. Basic Microbiol. 39, 17-24
    • (1999) J. Basic Microbiol. , vol.39 , pp. 17-24
    • Heys, S.J.1    Orton, S.L.2    Allison, D.G.3
  • 51
    • 0023223148 scopus 로고
    • The receptor-binding sequence of urokinase: A biological function for the growth-factor module of proteases
    • Appella, E., Robinson, E. A., Ullrich, S. J., Stoppelli, M. P., Corti, A., Cassani, G. and Blasi, F. (1987) The receptor-binding sequence of urokinase: a biological function for the growth-factor module of proteases. J. Biol. Chem. 262, 4437-4440
    • (1987) J. Biol. Chem. , vol.262 , pp. 4437-4440
    • Appella, E.1    Robinson, E.A.2    Ullrich, S.J.3    Stoppelli, M.P.4    Corti, A.5    Cassani, G.6    Blasi, F.7
  • 53
    • 0017107996 scopus 로고
    • Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin
    • Bode, W. and Huber, R. (1976) Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin. FEBS Lett. 68, 231-236
    • (1976) FEBS Lett. , vol.68 , pp. 231-236
    • Bode, W.1    Huber, R.2
  • 54
    • 3142526250 scopus 로고    scopus 로고
    • 1.2 Å crystal structure of the serine carboxyl proteinase pro-kumamolisin: Structure of an intact pro-subtilase
    • DOI 10.1016/j.str.2004.04.013, PII S0969212604001601
    • Comellas-Bigler, M., Maskos, K., Huber, R., Oyama, H., Oda, K. and Bode, W. (2004) 1.2 Å crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase. Structure 12, 1313-1323 (Pubitemid 38900773)
    • (2004) Structure , vol.12 , Issue.7 , pp. 1313-1323
    • Comellas-Bigler, M.1    Maskos, K.2    Huber, R.3    Oyama, H.4    Oda, K.5    Bode, W.6


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