메뉴 건너뛰기




Volumn 54, Issue 17, 2015, Pages 2785-2798

Antimicrobial peptide LL-37 is both a substrate of cathepsins S and K and a selective inhibitor of cathepsin L

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BINDING ENERGY; HYDROLYSIS; PEPTIDES; POLYPEPTIDES;

EID: 84928963891     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00231     Document Type: Article
Times cited : (41)

References (58)
  • 1
    • 37149044989 scopus 로고    scopus 로고
    • The role of epithelial beta-defensins and cathelicidins in host defense of the lung
    • Hiemstra, P. S. (2007) The role of epithelial beta-defensins and cathelicidins in host defense of the lung Exp. Lung Res. 33, 537-542
    • (2007) Exp. Lung Res. , vol.33 , pp. 537-542
    • Hiemstra, P.S.1
  • 2
    • 0142058024 scopus 로고    scopus 로고
    • Endogenous production of antimicrobial peptides in innate immunity and human disease
    • Gallo, R. L. and Nizet, V. (2003) Endogenous production of antimicrobial peptides in innate immunity and human disease Curr. Allergy Asthma Rep. 3, 402-409
    • (2003) Curr. Allergy Asthma Rep. , vol.3 , pp. 402-409
    • Gallo, R.L.1    Nizet, V.2
  • 3
    • 0029870085 scopus 로고    scopus 로고
    • Cystic Fibrosis Airway Epithelia Fail to Kill Bacteria because of Abnormal Airway Surface Fluid
    • Smith, J. J., Travis, S. M., Greenberg, E. P., and Welsh, M. J. (1996) Cystic Fibrosis Airway Epithelia Fail to Kill Bacteria Because of Abnormal Airway Surface Fluid Cell 85, 229-236
    • (1996) Cell , vol.85 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 4
    • 0034914909 scopus 로고    scopus 로고
    • Salt-Independent Abnormality of Antimicrobial Activity in Cystic Fibrosis Airway Surface Fluid
    • Bals, R., Weiner, D. J., Meegalla, R. L., Accurso, F., and Wilson, J. M. (2001) Salt-Independent Abnormality of Antimicrobial Activity in Cystic Fibrosis Airway Surface Fluid Am. J. Respir. Cell Mol. Biol. 25, 21-25
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.25 , pp. 21-25
    • Bals, R.1    Weiner, D.J.2    Meegalla, R.L.3    Accurso, F.4    Wilson, J.M.5
  • 5
    • 0030949875 scopus 로고    scopus 로고
    • Human β-Defensin-1 is a Salt-Sensitive Antibiotic in Lung That is Inactivated in Cystic Fibrosis
    • Goldman, M. J., Anderson, G. M., Stolzenberg, E. D., Kari, U. P., Zasloff, M., and Wilson, J. M. (1997) Human β-Defensin-1 Is a Salt-Sensitive Antibiotic in Lung That Is Inactivated in Cystic Fibrosis Cell 88, 553-560
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 6
    • 0038312912 scopus 로고    scopus 로고
    • The Antimicrobial Activity of the Cathelicidin LL37 is Inhibited by F-actin Bundles and Restored by Gelsolin
    • Weiner, D. J., Bucki, R., and Janmey, P. A. (2003) The Antimicrobial Activity of the Cathelicidin LL37 Is Inhibited by F-actin Bundles and Restored by Gelsolin Am. J. Respir. Cell Mol. Biol. 28, 738-745
    • (2003) Am. J. Respir. Cell Mol. Biol. , vol.28 , pp. 738-745
    • Weiner, D.J.1    Bucki, R.2    Janmey, P.A.3
  • 7
    • 34147139491 scopus 로고    scopus 로고
    • Release of the antimicrobial peptide LL-37 from DNA/F-actin bundles in cystic fibrosis sputum
    • Bucki, R., Byfield, F. J., and Janmey, P. A. (2007) Release of the antimicrobial peptide LL-37 from DNA/F-actin bundles in cystic fibrosis sputum Eur. Respir. J. 29, 624-632
    • (2007) Eur. Respir. J. , vol.29 , pp. 624-632
    • Bucki, R.1    Byfield, F.J.2    Janmey, P.A.3
  • 8
    • 20444406092 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with bacterial polysaccharides from lung pathogens
    • Herasimenka, Y., Benincasa, M., Mattiuzzo, M., Cescutti, P., Gennaro, R., and Rizzo, R. (2005) Interaction of antimicrobial peptides with bacterial polysaccharides from lung pathogens Peptides 26, 1127-1132
    • (2005) Peptides , vol.26 , pp. 1127-1132
    • Herasimenka, Y.1    Benincasa, M.2    Mattiuzzo, M.3    Cescutti, P.4    Gennaro, R.5    Rizzo, R.6
  • 9
    • 70349650567 scopus 로고    scopus 로고
    • Activity of antimicrobial peptides in the presence of polysaccharides produced by pulmonary pathogens
    • Benincasa, M., Mattiuzzo, M., Herasimenka, Y., Cescutti, P., Rizzo, R., and Gennaro, R. (2009) Activity of antimicrobial peptides in the presence of polysaccharides produced by pulmonary pathogens J. Pept. Sci. 15, 595-600
    • (2009) J. Pept. Sci. , vol.15 , pp. 595-600
    • Benincasa, M.1    Mattiuzzo, M.2    Herasimenka, Y.3    Cescutti, P.4    Rizzo, R.5    Gennaro, R.6
  • 10
    • 47249162101 scopus 로고    scopus 로고
    • Salivary mucins inhibit antibacterial activity of the cathelicidin-derived LL-37 peptide but not the cationic steroid CSA-13
    • Bucki, R., Namiot, D. B., Namiot, Z., Savage, P. B., and Janmey, P. A. (2008) Salivary mucins inhibit antibacterial activity of the cathelicidin-derived LL-37 peptide but not the cationic steroid CSA-13 J. Antimicrob. Chemother. 62, 329-335
    • (2008) J. Antimicrob. Chemother. , vol.62 , pp. 329-335
    • Bucki, R.1    Namiot, D.B.2    Namiot, Z.3    Savage, P.B.4    Janmey, P.A.5
  • 11
    • 1642405248 scopus 로고    scopus 로고
    • β-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis
    • Chen, C. I.-U., Schaller-Bals, S., Paul, K. P., Wahn, U., and Bals, R. (2004) β-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis J. Cystic Fibrosis 3, 45-50
    • (2004) J. Cystic Fibrosis , vol.3 , pp. 45-50
    • Chen, C.I.-U.1    Schaller-Bals, S.2    Paul, K.P.3    Wahn, U.4    Bals, R.5
  • 12
    • 27144462218 scopus 로고    scopus 로고
    • Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation
    • Xiao, W., Hsu, Y.-P., Ishizaka, A., Kirikae, T., and Moss, R. B. (2005) Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation Chest 128, 2316-2326
    • (2005) Chest , vol.128 , pp. 2316-2326
    • Xiao, W.1    Hsu, Y.-P.2    Ishizaka, A.3    Kirikae, T.4    Moss, R.B.5
  • 13
    • 0037960231 scopus 로고    scopus 로고
    • Antimicrobial and Protease Inhibitory Functions of the Human Cathelicidin (hCAP18/LL-37) Prosequence
    • Zaiou, M., Nizet, V., and Gallo, R. L. (2003) Antimicrobial and Protease Inhibitory Functions of the Human Cathelicidin (hCAP18/LL-37) Prosequence J. Investig. Dermatol. 120, 810-816
    • (2003) J. Investig. Dermatol. , vol.120 , pp. 810-816
    • Zaiou, M.1    Nizet, V.2    Gallo, R.L.3
  • 14
    • 77951092674 scopus 로고    scopus 로고
    • Kallikrein expression and cathelicidin processing are independently controlled in keratinocytes by calcium, vitamin D(3), and retinoic acid
    • Morizane, S., Yamasaki, K., Kabigting, F. D., and Gallo, R. L. (2010) Kallikrein expression and cathelicidin processing are independently controlled in keratinocytes by calcium, vitamin D(3), and retinoic acid J. Invest. Dermatol. 130, 1297-1306
    • (2010) J. Invest. Dermatol. , vol.130 , pp. 1297-1306
    • Morizane, S.1    Yamasaki, K.2    Kabigting, F.D.3    Gallo, R.L.4
  • 15
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sørensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., and Borregaard, N. (2001) Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3 Blood 97, 3951-3959
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sørensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 18
    • 79959644039 scopus 로고    scopus 로고
    • Transmembrane Pores Formed by Human Antimicrobial Peptide LL-37
    • Lee, C.-C., Sun, Y., Qian, S., and Huang, H. W. (2011) Transmembrane Pores Formed by Human Antimicrobial Peptide LL-37 Biophys. J. 100, 1688-1696
    • (2011) Biophys. J. , vol.100 , pp. 1688-1696
    • Lee, C.-C.1    Sun, Y.2    Qian, S.3    Huang, H.W.4
  • 19
    • 0036785559 scopus 로고    scopus 로고
    • The Human Antimicrobial Peptide LL-37 is a Multifunctional Modulator of Innate Immune Responses
    • Scott, M. G., Davidson, D. J., Gold, M. R., Bowdish, D., and Hancock, R. E. W. (2002) The Human Antimicrobial Peptide LL-37 Is a Multifunctional Modulator of Innate Immune Responses J. Immunol. 169, 3883-3891
    • (2002) J. Immunol. , vol.169 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3    Bowdish, D.4    Hancock, R.E.W.5
  • 23
    • 4644263748 scopus 로고    scopus 로고
    • Loss of microbicidal activity and increased formation of biofilm due to decreased lactoferrin activity in patients with cystic fibrosis
    • Rogan, M. P., Taggart, C. C., Greene, C. M., Murphy, P. G., ONeill, S. J., and McElvaney, N. G. (2004) Loss of microbicidal activity and increased formation of biofilm due to decreased lactoferrin activity in patients with cystic fibrosis J. Infect. Dis. 190, 1245-1253
    • (2004) J. Infect. Dis. , vol.190 , pp. 1245-1253
    • Rogan, M.P.1    Taggart, C.C.2    Greene, C.M.3    Murphy, P.G.4    Oneill, S.J.5    McElvaney, N.G.6
  • 25
    • 43049128497 scopus 로고    scopus 로고
    • Lung cysteine cathepsins: Intruders or unorthodox contributors to the kallikrein-kinin system?
    • Veillard, F., Lecaille, F., and Lalmanach, G. (2008) Lung cysteine cathepsins: intruders or unorthodox contributors to the kallikrein-kinin system? Int. J. Biochem. Cell Biol. 40, 1079-1094
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1079-1094
    • Veillard, F.1    Lecaille, F.2    Lalmanach, G.3
  • 26
    • 84903543514 scopus 로고    scopus 로고
    • Cysteine cathepsins and extracellular matrix degradation
    • Fonović, M. and Turk, B. (2014) Cysteine cathepsins and extracellular matrix degradation Biochim. Biophys. Acta 1840, 2560-2570
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 2560-2570
    • Fonović, M.1    Turk, B.2
  • 27
    • 84922311530 scopus 로고    scopus 로고
    • Cysteine cathepsins and cystatins: From ancillary tasks to prominent status in lung diseases
    • Lalmanach, G., Saidi, A., Marchand-Adam, S., Lecaille, F., and Kasabova, M. (2015) Cysteine cathepsins and cystatins: from ancillary tasks to prominent status in lung diseases Biol. Chem. 396, 111-130
    • (2015) Biol. Chem. , vol.396 , pp. 111-130
    • Lalmanach, G.1    Saidi, A.2    Marchand-Adam, S.3    Lecaille, F.4    Kasabova, M.5
  • 29
    • 0026731362 scopus 로고
    • Inhibition of rat tissue kallikrein gene family members by rat kallikrein-binding protein and alpha 1-proteinase inhibitor
    • Serveau, C., Moreau, T., Zhou, G. X., ElMoujahed, A., Chao, J., and Gauthier, F. (1992) Inhibition of rat tissue kallikrein gene family members by rat kallikrein-binding protein and alpha 1-proteinase inhibitor FEBS Lett. 309, 405-408
    • (1992) FEBS Lett. , vol.309 , pp. 405-408
    • Serveau, C.1    Moreau, T.2    Zhou, G.X.3    Elmoujahed, A.4    Chao, J.5    Gauthier, F.6
  • 31
    • 23244457789 scopus 로고    scopus 로고
    • Inhibition of a cathepsin L-like cysteine protease by a chimeric propeptide-derived inhibitor
    • Godat, E., Chowdhury, S., Lecaille, F., Belghazi, M., Purisima, E. O., and Lalmanach, G. (2005) Inhibition of a cathepsin L-like cysteine protease by a chimeric propeptide-derived inhibitor Biochemistry 44, 10486-10493
    • (2005) Biochemistry , vol.44 , pp. 10486-10493
    • Godat, E.1    Chowdhury, S.2    Lecaille, F.3    Belghazi, M.4    Purisima, E.O.5    Lalmanach, G.6
  • 35
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 36
    • 3242877815 scopus 로고    scopus 로고
    • ClusPro: A fully automated algorithm for protein-protein docking
    • Comeau, S. R., Gatchell, D. W., Vajda, S., and Camacho, C. J. (2004) ClusPro: a fully automated algorithm for protein-protein docking Nucleic Acids Res. 32, W96-99
    • (2004) Nucleic Acids Res. , vol.32 , pp. 96-99
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 39
    • 68949117860 scopus 로고    scopus 로고
    • LL-37 Complexation with Glycosaminoglycans in Cystic Fibrosis Lungs Inhibits Antimicrobial Activity, Which Can Be Restored by Hypertonic Saline
    • Bergsson, G., Reeves, E. P., McNally, P., Chotirmall, S. H., Greene, C. M., Greally, P., Murphy, P., ONeill, S. J., and McElvaney, N. G. (2009) LL-37 Complexation with Glycosaminoglycans in Cystic Fibrosis Lungs Inhibits Antimicrobial Activity, Which Can Be Restored by Hypertonic Saline J. Immunol. 183, 543-551
    • (2009) J. Immunol. , vol.183 , pp. 543-551
    • Bergsson, G.1    Reeves, E.P.2    McNally, P.3    Chotirmall, S.H.4    Greene, C.M.5    Greally, P.6    Murphy, P.7    Oneill, S.J.8    McElvaney, N.G.9
  • 40
    • 59749089160 scopus 로고    scopus 로고
    • Evaluation of Strategies for Improving Proteolytic Resistance of Antimicrobial Peptides by Using Variants of EFK17, an Internal Segment of LL-37
    • Strömstedt, A. A., Pasupuleti, M., Schmidtchen, A., and Malmsten, M. (2009) Evaluation of Strategies for Improving Proteolytic Resistance of Antimicrobial Peptides by Using Variants of EFK17, an Internal Segment of LL-37 Antimicrob. Agents Chemother. 53, 593-602
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 593-602
    • Strömstedt, A.A.1    Pasupuleti, M.2    Schmidtchen, A.3    Malmsten, M.4
  • 41
    • 84871027267 scopus 로고    scopus 로고
    • A comprehensive summary of LL-37, the factotum human cathelicidin peptide
    • Vandamme, D., Landuyt, B., Luyten, W., and Schoofs, L. (2012) A comprehensive summary of LL-37, the factotum human cathelicidin peptide Cell. Immunol. 280, 22-35
    • (2012) Cell. Immunol. , vol.280 , pp. 22-35
    • Vandamme, D.1    Landuyt, B.2    Luyten, W.3    Schoofs, L.4
  • 44
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson, J., Gudmundsson, G. H., Rottenberg, M. E., Berndt, K. D., and Agerberth, B. (1998) Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37 J. Biol. Chem. 273, 3718-3724
    • (1998) J. Biol. Chem. , vol.273 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 45
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities
    • Choe, Y., Leonetti, F., Greenbaum, D. C., Lecaille, F., Bogyo, M., Brömme, D., Ellman, J. A., and Craik, C. S. (2006) Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities J. Biol. Chem. 281, 12824-12832
    • (2006) J. Biol. Chem. , vol.281 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3    Lecaille, F.4    Bogyo, M.5    Brömme, D.6    Ellman, J.A.7    Craik, C.S.8
  • 46
    • 33947718470 scopus 로고    scopus 로고
    • The S2 subsites of cathepsins K and L and their contribution to collagen degradation
    • Lecaille, F., Chowdhury, S., Purisima, E., Brömme, D., and Lalmanach, G. (2007) The S2 subsites of cathepsins K and L and their contribution to collagen degradation Protein Sci. 16, 662-670
    • (2007) Protein Sci. , vol.16 , pp. 662-670
    • Lecaille, F.1    Chowdhury, S.2    Purisima, E.3    Brömme, D.4    Lalmanach, G.5
  • 48
    • 40849084973 scopus 로고    scopus 로고
    • Activation of cathepsin L by the cathelin-like domain of protegrin-3
    • Zhu, S., Wei, L., Yamasaki, K., and Gallo, R. L. (2008) Activation of cathepsin L by the cathelin-like domain of protegrin-3 Mol. Immunol. 45, 2531-2536
    • (2008) Mol. Immunol. , vol.45 , pp. 2531-2536
    • Zhu, S.1    Wei, L.2    Yamasaki, K.3    Gallo, R.L.4
  • 49
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe, R., Grochulski, P., Sivaraman, J., Ménard, R., Mort, J. S., and Cygler, M. (1996) Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment EMBO J. 15, 5492-5503
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Ménard, R.4    Mort, J.S.5    Cygler, M.6
  • 51
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • Schmidtchen, A., Frick, I.-M., Andersson, E., Tapper, H., and Björck, L. (2002) Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37 Mol. Microbiol. 46, 157-168
    • (2002) Mol. Microbiol. , vol.46 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.-M.2    Andersson, E.3    Tapper, H.4    Björck, L.5
  • 54
    • 4544254599 scopus 로고    scopus 로고
    • Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides
    • Belas, R., Manos, J., and Suvanasuthi, R. (2004) Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides Infect. Immun. 72, 5159-5167
    • (2004) Infect. Immun. , vol.72 , pp. 5159-5167
    • Belas, R.1    Manos, J.2    Suvanasuthi, R.3
  • 56
    • 84883546762 scopus 로고    scopus 로고
    • LL-37 in periodontal health and disease and its susceptibility to degradation by proteinases present in gingival crevicular fluid
    • McCrudden, M. T. C., Orr, D. F., Yu, Y., Coulter, W. A., Manning, G., Irwin, C. R., and Lundy, F. T. (2013) LL-37 in periodontal health and disease and its susceptibility to degradation by proteinases present in gingival crevicular fluid J. Clin. Periodontol. 40, 933-941
    • (2013) J. Clin. Periodontol. , vol.40 , pp. 933-941
    • McCrudden, M.T.C.1    Orr, D.F.2    Yu, Y.3    Coulter, W.A.4    Manning, G.5    Irwin, C.R.6    Lundy, F.T.7
  • 57
    • 20444387986 scopus 로고    scopus 로고
    • The human cathelicidin LL-37: A multifunctional peptide involved in infection and inflammation in the lung
    • Tjabringa, S. G., Rabe, K. F., and Hiemstra, P. S. (2005) The human cathelicidin LL-37: a multifunctional peptide involved in infection and inflammation in the lung Pulm. Pharmacol. Ther. 18, 321-327
    • (2005) Pulm. Pharmacol. Ther. , vol.18 , pp. 321-327
    • Tjabringa, S.G.1    Rabe, K.F.2    Hiemstra, P.S.3
  • 58
    • 84861188087 scopus 로고    scopus 로고
    • Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37
    • Nan, Y. H., Bang, J.-K., Jacob, B., Park, I.-S., and Shin, S. Y. (2012) Prokaryotic selectivity and LPS-neutralizing activity of short antimicrobial peptides designed from the human antimicrobial peptide LL-37 Peptides 35, 239-247
    • (2012) Peptides , vol.35 , pp. 239-247
    • Nan, Y.H.1    Bang, J.-K.2    Jacob, B.3    Park, I.-S.4    Shin, S.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.