메뉴 건너뛰기




Volumn 289, Issue 46, 2014, Pages 31777-31791

New selective peptidyl di(chlorophenyl) phosphonate esters for visualizing and blocking neutrophil proteinase 3 in human diseases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BODY FLUIDS; CELL DEATH; DISEASES; ENZYME ACTIVITY;

EID: 84911374663     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.591339     Document Type: Article
Times cited : (36)

References (51)
  • 1
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures, and future prospects
    • Turk, B. (2006) Targeting proteases: successes, failures, and future prospects. Nat. Rev. Drug Discov. 5, 785-799
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 2
    • 38849143983 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3, and cathepsin G: Physicochemical properties, activity, and physiopathological functions
    • Korkmaz, B., Moreau, T., and Gauthier, F. (2008) Neutrophil elastase, proteinase 3, and cathepsin G: physicochemical properties, activity, and physiopathological functions. Biochimie 90, 227-242
    • (2008) Biochimie , vol.90 , pp. 227-242
    • Korkmaz, B.1    Moreau, T.2    Gauthier, F.3
  • 3
    • 78650096176 scopus 로고    scopus 로고
    • Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases
    • Korkmaz, B., Horwitz, M. S., Jenne, D. E., and Gauthier, F. (2010) Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases. Pharmacol. Rev. 62, 726-759
    • (2010) Pharmacol. Rev. , vol.62 , pp. 726-759
    • Korkmaz, B.1    Horwitz, M.S.2    Jenne, D.E.3    Gauthier, F.4
  • 4
    • 47849105932 scopus 로고    scopus 로고
    • Roles for proteinases in the pathogenesis of chronic obstructive pulmonary disease
    • Owen, C. A. (2008) Roles for proteinases in the pathogenesis of chronic obstructive pulmonary disease. Int. J. Chron. Obstruct. Pulmon. Dis. 3, 253-268
    • (2008) Int. J. Chron. Obstruct. Pulmon. Dis. , vol.3 , pp. 253-268
    • Owen, C.A.1
  • 6
    • 38049051222 scopus 로고    scopus 로고
    • Pathogenesis of PR3-ANCA associated vasculitis
    • Kallenberg, C. G. (2008) Pathogenesis of PR3-ANCA associated vasculitis. J. Autoimmun. 30, 29-36
    • (2008) J. Autoimmun. , vol.30 , pp. 29-36
    • Kallenberg, C.G.1
  • 7
    • 84883206431 scopus 로고    scopus 로고
    • Current understanding of the pathogenesis of granulomatosis with polyangiitis (Wegener's)
    • Csernok, E., and Gross, W. L. (2013) Current understanding of the pathogenesis of granulomatosis with polyangiitis (Wegener's). Expert Rev. Clin. Immunol. 9, 641-648
    • (2013) Expert Rev. Clin. Immunol. , vol.9 , pp. 641-648
    • Csernok, E.1    Gross, W.L.2
  • 8
    • 84865440186 scopus 로고    scopus 로고
    • Proteinase 3, the autoantigen in granulomatosis with polyangiitis, associates with calreticulin on apoptotic neutrophils, impairs macrophage phagocytosis, and promotes inflammation
    • Gabillet, J., Millet, A., Pederzoli-Ribeil, M., Tacnet-Delorme, P., Guillevin, L., Mouthon, L., Frachet, P., and Witko-Sarsat, V. (2012) Proteinase 3, the autoantigen in granulomatosis with polyangiitis, associates with calreticulin on apoptotic neutrophils, impairs macrophage phagocytosis, and promotes inflammation. J. Immunol. 189, 2574-2583
    • (2012) J. Immunol. , vol.189 , pp. 2574-2583
    • Gabillet, J.1    Millet, A.2    Pederzoli-Ribeil, M.3    Tacnet-Delorme, P.4    Guillevin, L.5    Mouthon, L.6    Frachet, P.7    Witko-Sarsat, V.8
  • 9
    • 0033214847 scopus 로고    scopus 로고
    • Presence of proteinase 3 in secretory vesicles: Evidence of a novel, highly mobilizable intracellular pool distinct from azurophil granules
    • Witko-Sarsat, V., Cramer, E. M., Hieblot, C., Guichard, J., Nusbaum, P., Lopez, S., Lesavre, P., and Halbwachs-Mecarelli, L. (1999) Presence of proteinase 3 in secretory vesicles: evidence of a novel, highly mobilizable intracellular pool distinct from azurophil granules. Blood 94, 2487-2496
    • (1999) Blood , vol.94 , pp. 2487-2496
    • Witko-Sarsat, V.1    Cramer, E.M.2    Hieblot, C.3    Guichard, J.4    Nusbaum, P.5    Lopez, S.6    Lesavre, P.7    Halbwachs-Mecarelli, L.8
  • 10
    • 0028790701 scopus 로고
    • Bimodal distribution of proteinase 3 (PR3) surface expression reflects a constitutive heterogeneity in the polymorphonuclear neutrophil pool
    • Halbwachs-Mecarelli, L., Bessou, G., Lesavre, P., Lopez, S., and WitkoSarsat, V. (1995) Bimodal distribution of proteinase 3 (PR3) surface expression reflects a constitutive heterogeneity in the polymorphonuclear neutrophil pool. FEBS Lett. 374, 29-33
    • (1995) Febs Lett. , vol.374 , pp. 29-33
    • Halbwachs-Mecarelli, L.1    Bessou, G.2    Lesavre, P.3    Lopez, S.4    WitkoSarsat, V.5
  • 13
    • 67650230587 scopus 로고    scopus 로고
    • Irreversible inhibition of serine proteases: Design and in vivo activity of diaryl α-aminophosphonate derivatives
    • Sieñczyk, M., and Oleksyszyn, T- (2009) Irreversible inhibition of serine proteases: design and in vivo activity of diaryl a-aminophosphonate derivatives. Curr. Med. Chem. 16,1673-1687
    • (2009) Curr. Med. Chem. , vol.16 , pp. 1673-1687
    • Sieñczyk, M.1    Oleksyszyn, T.2
  • 14
    • 84880814429 scopus 로고    scopus 로고
    • Phosphonic esters and their application of protease control
    • Grzywa, R., and Sienczyk, M. (2013) Phosphonic esters and their application of protease control. Curr. Pharm. Des. 19, 1154-1178
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 1154-1178
    • Grzywa, R.1    Sienczyk, M.2
  • 15
    • 0028172324 scopus 로고
    • α-Aminoalkylphosphonate di(chlorophenyl) esters as inhibitors of serine proteases
    • Boduszek, B., Brown, A. D., and Powers, T. C. (1994) a-Aminoalkylphosphonate di(chlorophenyl) esters as inhibitors of serine proteases. J. Enzyme Inhib. 8,147-158
    • (1994) J. Enzyme Inhib. , vol.8 , pp. 147-158
    • Boduszek, B.1    Brown, A.D.2    Powers, T.C.3
  • 16
    • 79251537480 scopus 로고    scopus 로고
    • Peptide length and leaving-group sterics influence potency of peptide phosphonate protease inhibitors
    • Brown, C. M., Ray, M., Eroy-Reveles, A. A., Egea, P., Tajon, C., and Crailc, C. S. (2011) Peptide length and leaving-group sterics influence potency of peptide phosphonate protease inhibitors. Chem. Biol. 18, 48-57
    • (2011) Chem. Biol. , vol.18 , pp. 48-57
    • Brown, C.M.1    Ray, M.2    Eroy-Reveles, A.A.3    Egea, P.4    Tajon, C.5    Crailc, C.S.6
  • 17
    • 0028113356 scopus 로고
    • Chymase-directed serine protease inhibitor that reacts with a single 30-kDa granzyme and blocks NIC-mediated cytotoxicity
    • Woodard, S. L., Jackson, D. S., Abuelyaman, A. S., Powers, J. C., Winkler, U., and Hudig, D. (1994) Chymase-directed serine protease inhibitor that reacts with a single 30-kDa granzyme and blocks NIC-mediated cytotoxicity.J. Immunol. 153, 5016-5025
    • (1994) J. Immunol. , vol.153 , pp. 5016-5025
    • Woodard, S.L.1    Jackson, D.S.2    Abuelyaman, A.S.3    Powers, J.C.4    Winkler, U.5    Hudig, D.6
  • 20
    • 33847265882 scopus 로고    scopus 로고
    • Influence of charge distribution at the active site surface on the substrate specificity of human neutrophil protease 3 and elastase: A kinetic and molecular modeling analysis
    • Korkmaz, B., Hajjar, E., Kalupov, T., Reuter, N., Brillard-Bourdet, M., Moreau, T., Juliano, L., and Gauthier, F. (2007) Influence of charge distribution at the active site surface on the substrate specificity of human neutrophil protease 3 and elastase: a kinetic and molecular modeling analysis.J. Biol. Chem. 282, 1989-1997
    • (2007) J. Biol. Chem. , vol.282 , pp. 1989-1997
    • Korkmaz, B.1    Hajjar, E.2    Kalupov, T.3    Reuter, N.4    Brillard-Bourdet, M.5    Moreau, T.6    Juliano, L.7    Gauthier, F.8
  • 21
    • 33746645238 scopus 로고    scopus 로고
    • Inhibition of trypsin and urokinase by Cbz-amino(4-guanidinophenyl)methanephosphonate aromatic ester derivatives: The influence of the ester group on their biological activity
    • Sieńczyk, M., and Oleksyszyn, J. (2006) Inhibition of trypsin and urokinase by Cbz-amino(4-guanidinophenyl)methanephosphonate aromatic ester derivatives: the influence of the ester group on their biological activity. Bioorg. Med. Chem. Lett. 16, 2886-2890
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 2886-2890
    • Sieńczyk, M.1    Oleksyszyn, J.2
  • 22
    • 0024341633 scopus 로고
    • Irreversible inhibition of serine proteases by peptidyl derivatives of α-aminoalkylphosphonate diphenyl esters
    • Oleksyszyn, J., and Powers, J. C. (1989) Irreversible inhibition of serine proteases by peptidyl derivatives of a-aminoalkylphosphonate diphenyl esters. Biochem. Biophys. Res. Commun. 161,143-149
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 143-149
    • Oleksyszyn, J.1    Powers, J.C.2
  • 23
    • 0037131259 scopus 로고    scopus 로고
    • Discriminating between the activities of human neutrophil elastase and proteinase 3 using serpin-derived fluorogenic substrates
    • Korkmaz, B., Attucci, S., Hazouard, E., F err an di ere, M., Jourdan, M. L., Brillard-Bourdet, M., Juliano, L., and Gauthier, F. (2002) Discriminating between the activities of human neutrophil elastase and proteinase 3 using serpin-derived fluorogenic substrates.J. Biol. Chem. 277, 39074-39081
    • (2002) J. Biol. Chem. , vol.277 , pp. 39074-39081
    • Korkmaz, B.1    Attucci, S.2    Hazouard, E.3    Ferrandiere, M.4    Jourdan, M.L.5    Brillard-Bourdet, M.6    Juliano, L.7    Gauthier, F.8
  • 24
    • 0020473244 scopus 로고
    • Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier
    • Tian, W. X., and Tsou, C. L. (1982) Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier. Biochemistry 21,1028-1032
    • (1982) Biochemistry , vol.21 , pp. 1028-1032
    • Tian, W.X.1    Tsou, C.L.2
  • 25
    • 44949182000 scopus 로고    scopus 로고
    • Measuring elastase, proteinase 3, and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates
    • Korkmaz, B., Attucci, S., Juliano, M. A., Kalupov, T., Jourdan, M. L., Juliano, L., and Gauthier, F. (2008) Measuring elastase, proteinase 3, and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates. Nat. Protoc. 3, 991-1000
    • (2008) Nat. Protoc. , vol.3 , pp. 991-1000
    • Korkmaz, B.1    Attucci, S.2    Juliano, M.A.3    Kalupov, T.4    Jourdan, M.L.5    Juliano, L.6    Gauthier, F.7
  • 26
    • 0029833222 scopus 로고    scopus 로고
    • The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies
    • Fujinaga, M., Chernaia, M. M., Halenbeck, R., Koths, K., and James, M. N. (1996) The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies.J. Mol. Biol. 261, 267-278
    • (1996) J. Mol. Biol. , vol.261 , pp. 267-278
    • Fujinaga, M.1    Chernaia, M.M.2    Halenbeck, R.3    Koths, K.4    James, M.N.5
  • 31
    • 67749111845 scopus 로고    scopus 로고
    • Catalytic activity and inhibition of wegener antigen proteinase 3 on the cell surface of human polymorphonuclear neutrophils
    • Korkmaz, B., Jaillet, J., Jourdan, M. L., Gauthier, A., Gauthier, F., and Attucci, S. (2009) Catalytic activity and inhibition of wegener antigen proteinase 3 on the cell surface of human polymorphonuclear neutrophils. J. Biol. Chem. 284,19896-19902
    • (2009) J. Biol. Chem. , vol.284 , pp. 19896-19902
    • Korkmaz, B.1    Jaillet, J.2    Jourdan, M.L.3    Gauthier, A.4    Gauthier, F.5    Attucci, S.6
  • 33
    • 44349095833 scopus 로고    scopus 로고
    • Computational prediction of the binding site of proteinase 3 to the plasma membrane
    • Hajjar, E., Mihajlovic, M., Witko-Sarsat, V., Laz aridis, T., and Reuter, N. (2008) Computational prediction of the binding site of proteinase 3 to the plasma membrane. Proteins. 71, 1655-1669
    • (2008) Proteins. , vol.71 , pp. 1655-1669
    • Hajjar, E.1    Mihajlovic, M.2    Witko-Sarsat, V.3    Lazaridis, T.4    Reuter, N.5
  • 34
    • 77954337983 scopus 로고    scopus 로고
    • How does proteinase 3 interact with lipid bilayers?
    • Broemstrup, T., and Reuter, N. (2010) How does proteinase 3 interact with lipid bilayers? Phys. Chem. Chem. Phys. 12, 7487-7496
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 7487-7496
    • Broemstrup, T.1    Reuter, N.2
  • 35
    • 58149096975 scopus 로고    scopus 로고
    • A hydrophobic patch on proteinase 3, the target of autoantibodies in Wegener granulomatosis, mediates membrane binding via NB1 receptors
    • Korkmaz, B., Kuhl, A., Bayat, B., Santoso, S., and Jenne, D. E. (2008) A hydrophobic patch on proteinase 3, the target of autoantibodies in Wegener granulomatosis, mediates membrane binding via NB1 receptors. J. Biol. Chem. 283, 35976-35982
    • (2008) J. Biol. Chem. , vol.283 , pp. 35976-35982
    • Korkmaz, B.1    Kuhl, A.2    Bayat, B.3    Santoso, S.4    Jenne, D.E.5
  • 36
    • 77951745688 scopus 로고    scopus 로고
    • Structures of human proteinase 3 and neutrophil elastase: So similar yet so different
    • Hajjar, E., Broemstrup, T., Kantari, C., Witko-Sarsat, V., and Reuter, N. (2010) Structures of human proteinase 3 and neutrophil elastase: so similar yet so different. FEBS J. 277, 2238-2254
    • (2010) Febs J. , vol.277 , pp. 2238-2254
    • Hajjar, E.1    Broemstrup, T.2    Kantari, C.3    Witko-Sarsat, V.4    Reuter, N.5
  • 37
    • 36549053594 scopus 로고    scopus 로고
    • Differences in the substrate binding sites of murine and human proteinase 3 and neutrophil elastase
    • Hajjar, E., Korkmaz, B., and Reuter, N. (2007) Differences in the substrate binding sites of murine and human proteinase 3 and neutrophil elastase. FEBS Lett. 581, 5685-5690
    • (2007) Febs Lett. , vol.581 , pp. 5685-5690
    • Hajjar, E.1    Korkmaz, B.2    Reuter, N.3
  • 39
    • 0018864175 scopus 로고
    • Elastase-like enzymes in human neutrophils localized by ultrastructural cytochemistry
    • Clark, J. M., Vaughan, D. W., Aiken, B. M., and Kagan, H. M. (1980) Elastase-like enzymes in human neutrophils localized by ultrastructural cytochemistry. J. Cell Biol. 84,102-119
    • (1980) J. Cell Biol. , vol.84 , pp. 102-119
    • Clark, J.M.1    Vaughan, D.W.2    Aiken, B.M.3    Kagan, H.M.4
  • 42
    • 0025225389 scopus 로고
    • Ultrastructural localization of proteinase 3, the target antigen of anti-cytoplas-mic antibodies circulating in Wegener's granulomatosis
    • Csernok, E., Lüdemann, J., Gross, W. L., and Bainton, D. F. (1990) Ultrastructural localization of proteinase 3, the target antigen of anti-cytoplas-mic antibodies circulating in Wegener's granulomatosis. Am. J. Pathol. 137,1113-1120
    • (1990) Am. J. Pathol. , vol.137 , pp. 1113-1120
    • Csernok, E.1    Lüdemann, J.2    Gross, W.L.3    Bainton, D.F.4
  • 43
    • 0027511347 scopus 로고
    • Occurrence of autoantibodies to human leucocyte elastase in Wegener's granulomatosis and other inflammatory disorders
    • Tervaert, J. W., Mulder, L., Stegeman, C., Elema, J., Huitema, M., The, H., and Kallenberg, C. (1993) Occurrence of autoantibodies to human leucocyte elastase in Wegener's granulomatosis and other inflammatory disorders. Ann. Rheum. Dis. 52,115-120
    • (1993) Ann. Rheum. Dis. , vol.52 , pp. 115-120
    • Tervaert, J.W.1    Mulder, L.2    Stegeman, C.3    Elema, J.4    Huitema, M.5    The, H.6    Kallenberg, C.7
  • 44
    • 80055082814 scopus 로고    scopus 로고
    • Molecular analysis of the membrane insertion domain of proteinase 3, the Wegener's autoantigen, in RBL cells: Implication for its pathogenic activity
    • Kantari, C., Millet, A., Gabili et, J., Hajjar, E., Broemstrup, T., Pluta, P., Reuter, N., and Witko-Sarsat, V. (2011) Molecular analysis of the membrane insertion domain of proteinase 3, the Wegener's autoantigen, in RBL cells: implication for its pathogenic activity. J. Leukoc. Biol. 90, 941-950
    • (2011) J. Leukoc. Biol. , vol.90 , pp. 941-950
    • Kantari, C.1    Millet, A.2    Gabiliet, J.3    Hajjar, E.4    Broemstrup, T.5    Pluta, P.6    Reuter, N.7    Witko-Sarsat, V.8
  • 45
    • 84890128446 scopus 로고    scopus 로고
    • Relevance of the mouse model as a therapeutic approach for neutrophil proteinase 3-associated human diseases
    • Korkmaz, B., Jenne, D. E., and Gauthier, F. (2013) Relevance of the mouse model as a therapeutic approach for neutrophil proteinase 3-associated human diseases. Int. Immunopharmacol. 17,1198-1205
    • (2013) Int. Immunopharmacol. , vol.17 , pp. 1198-1205
    • Korkmaz, B.1    Jenne, D.E.2    Gauthier, F.3
  • 46
    • 84884185457 scopus 로고    scopus 로고
    • A monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism
    • Hinkofer, L. C., Seidel, S. A., Korkmaz, B., Silva, F., Hummel, A. M., Braun, D., Jenne, D.E., and Specks, U. (2013) A monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism. J. Biol. Chem. 288, 26635-26648
    • (2013) J. Biol. Chem. , vol.288 , pp. 26635-26648
    • Hinkofer, L.C.1    Seidel, S.A.2    Korkmaz, B.3    Silva, F.4    Hummel, A.M.5    Braun, D.6    Jenne, D.E.7    Specks, U.8
  • 48
    • 23844554460 scopus 로고    scopus 로고
    • Inhibition of neutrophil elastase by αl-protease inhibitor at the surface of human polymorphonuclear neutrophils
    • Korkmaz, B., Attucci, S., Jourdan, M. L., Juliano, L., and Gauthier, F. (2005) Inhibition of neutrophil elastase by αl-protease inhibitor at the surface of human polymorphonuclear neutrophils.J. Immunol. 175, 3329-3338
    • (2005) J. Immunol. , vol.175 , pp. 3329-3338
    • Korkmaz, B.1    Attucci, S.2    Jourdan, M.L.3    Juliano, L.4    Gauthier, F.5
  • 49
    • 0022801412 scopus 로고
    • X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the Turkey ovomucoid inhibitor
    • Bode, W., Wei, A. Z., Huber, R., Meyer, E., Travis, J., and Neumann, S. (1986) X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor. EMBOJ. 5, 2453-2458
    • (1986) Emboj , vol.5 , pp. 2453-2458
    • Bode, W.1    Wei, A.Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 50
    • 33745941917 scopus 로고    scopus 로고
    • EPI-hNE4, a proteolysisresistant inhibitor of human neutrophil elastase and potential anti-inflammatory drug for treating cystic fibrosis
    • Attucci, S., Gauthier, A., Korkmaz, B., Delépine, P., Martino, M. F., Saudubray, F., Diot, P., and Gauthier, F. (2006) EPI-hNE4, a proteolysisresistant inhibitor of human neutrophil elastase and potential anti-inflammatory drug for treating cystic fibrosis. J. Pharmacol. Exp. Ther. 318, 803-809
    • (2006) J. Pharmacol. Exp. Ther. , vol.318 , pp. 803-809
    • Attucci, S.1    Gauthier, A.2    Korkmaz, B.3    Delépine, P.4    Martino, M.F.5    Saudubray, F.6    Diot, P.7    Gauthier, F.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.