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Volumn 42, Issue 9, 1998, Pages 2206-2214

Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; DEFENSIN; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0031686776     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.42.9.2206     Document Type: Article
Times cited : (689)

References (53)
  • 2
    • 0025752606 scopus 로고
    • Side chain-back-bone hydrogen bonding contributes to helix stability in peptides derived from an α-helical region of carboxypeptidase A
    • Bruch, M. D., M. M. Dhingra, and L. M. Gierasch. 1991. Side chain-back-bone hydrogen bonding contributes to helix stability in peptides derived from an α-helical region of carboxypeptidase A. Proteins Struct. Funct. Genet. 10: 130-139.
    • (1991) Proteins Struct. Funct. Genet. , vol.10 , pp. 130-139
    • Bruch, M.D.1    Dhingra, M.M.2    Gierasch, L.M.3
  • 3
    • 0029128705 scopus 로고
    • The solution structure of the active domain of CAP18 - A lipopolysaccharide binding protein from rabbit leukocytes
    • Chen, C., R. Brock, F. Luh, P.-J. Chou, J. W. Larrick, R.-F. Huang, and T.-H. Huang. 1995. The solution structure of the active domain of CAP18 - a lipopolysaccharide binding protein from rabbit leukocytes. FEBS Lett. 370: 46-52.
    • (1995) FEBS Lett. , vol.370 , pp. 46-52
    • Chen, C.1    Brock, R.2    Luh, F.3    Chou, P.-J.4    Larrick, J.W.5    Huang, R.-F.6    Huang, T.-H.7
  • 4
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous by circular dichroism
    • Chen, Y. H., J. T. Yang, and K. H. Chau. 1974. Determination of the helix and β form of proteins in aqueous by circular dichroism. Biochemistry 13: 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 5
    • 0030453086 scopus 로고    scopus 로고
    • Assembly of the phagocyte NADPH oxidase: Molecular interaction of oxidase proteins
    • DeLeo, F. R., and M. T. Quinn. 1996. Assembly of the phagocyte NADPH oxidase: molecular interaction of oxidase proteins. J. Leukocyte Biol. 60: 677-691.
    • (1996) J. Leukocyte Biol. , vol.60 , pp. 677-691
    • DeLeo, F.R.1    Quinn, M.T.2
  • 8
    • 0030956070 scopus 로고    scopus 로고
    • The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders
    • Frohm, M., B. Agerberth, G. Ahangari, M. Stahle-Backdahl, S. Liden, H. Wigzell, and G. H. Gudmundsson. 1997. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272:15258-15263.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15258-15263
    • Frohm, M.1    Agerberth, B.2    Ahangari, G.3    Stahle-Backdahl, M.4    Liden, S.5    Wigzell, H.6    Gudmundsson, G.H.7
  • 9
    • 0031009432 scopus 로고    scopus 로고
    • Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
    • Gallo, R. L., K. J. Kim, M. Bernfield, C. A. Kozak, M. Zanetti, L. Merluzzi, and R. Gennaro. 1997. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J. Biol. Chem. 272:13088-13093.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13088-13093
    • Gallo, R.L.1    Kim, K.J.2    Bernfield, M.3    Kozak, C.A.4    Zanetti, M.5    Merluzzi, L.6    Gennaro, R.7
  • 10
    • 0031046654 scopus 로고    scopus 로고
    • Antimicrobial peptides of leukocytes
    • Ganz, T., and R. I. Lehrer. 1997. Antimicrobial peptides of leukocytes. Curr. Opin. Hematol. 4:53-58.
    • (1997) Curr. Opin. Hematol. , vol.4 , pp. 53-58
    • Ganz, T.1    Lehrer, R.I.2
  • 11
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and G. Fasman. 1967. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8:4108-4115.
    • (1967) Biochemistry , vol.8 , pp. 4108-4115
    • Greenfield, N.1    Fasman, G.2
  • 12
    • 0026584772 scopus 로고
    • Molecular genetic analysis of the Escherichia coli phoP locus
    • Groisman, E. A., F. Heffron, and F. Solomon. 1992. Molecular genetic analysis of the Escherichia coli phoP locus. J. Bacteriol. 174:486-491.
    • (1992) J. Bacteriol. , vol.174 , pp. 486-491
    • Groisman, E.A.1    Heffron, F.2    Solomon, F.3
  • 13
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson, G. H., B. Agerberth, J. Odeberg, T. Bergman, B. Olsson, and R. Salcedo. 1996. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238:325-332.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 14
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid a modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo, L., K. B. Lim, J. S. Gunn, B. Bainbridge, R. P. Darveau, M. Hackett, and S. I. Miller. 1997. Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 276:250-253.
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 15
    • 0029846572 scopus 로고    scopus 로고
    • Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Staphylococcus aureus by neutrophils
    • Hampton, M. B., A. J. Kettle, and C. C. Winterbourn. 1996. Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Staphylococcus aureus by neutrophils. Infect. Immun. 64:3512-3517.
    • (1996) Infect. Immun. , vol.64 , pp. 3512-3517
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 16
    • 0027980251 scopus 로고
    • Neutrophil defensins: Purification, characterization and antimicrobial testing
    • Harwig, S. S. L., T. Ganz, and R. I. Lehrer. 1994. Neutrophil defensins: purification, characterization and antimicrobial testing. Methods Enzymol. 236:163-172.
    • (1994) Methods Enzymol. , vol.236 , pp. 163-172
    • Harwig, S.S.L.1    Ganz, T.2    Lehrer, R.I.3
  • 17
    • 0029831079 scopus 로고    scopus 로고
    • Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations
    • Harwig, S. S. L., A. J. Waring, H. J. Yang, Y. Cho, L. Tan, and R. I. Lehrer. 1996. Intramolecular disulfide bonds enhance the antimicrobial and lytic activities of protegrins at physiological sodium chloride concentrations. Eur. J. Biochem. 240:352-357.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 352-357
    • Harwig, S.S.L.1    Waring, A.J.2    Yang, H.J.3    Cho, Y.4    Tan, L.5    Lehrer, R.I.6
  • 19
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C., Jr. 1990. Protein secondary structure and circular dichroism: a practical guide. Proteins Struct. Funct. Genet. 7:205-214.
    • (1990) Proteins Struct. Funct. Genet. , vol.7 , pp. 205-214
    • Johnson W.C., Jr.1
  • 20
    • 0029828326 scopus 로고    scopus 로고
    • Transcriptional activation of Salmonella typhimurium invasion genes by a member of the phosphorylated response-regulator superfamily
    • Johnston, C., D. A. Pegues, C. J. Hueck, A. Lee, and S. I. Miller. 1996. Transcriptional activation of Salmonella typhimurium invasion genes by a member of the phosphorylated response-regulator superfamily. Mol. Microbiol. 22:715-727.
    • (1996) Mol. Microbiol. , vol.22 , pp. 715-727
    • Johnston, C.1    Pegues, D.A.2    Hueck, C.J.3    Lee, A.4    Miller, S.I.5
  • 26
    • 0025990384 scopus 로고
    • Complementary DNA sequence of rabbit CAP-18. A unique lipopolysaccharide binding protein
    • Larrick, J. W., J. G. Morgan, I. Palings, M. Hirata, and M. H. Yen. 1991. Complementary DNA sequence of rabbit CAP-18. A unique lipopolysaccharide binding protein. Biochem. Biophys. Res. Commun. 179:170-175.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 170-175
    • Larrick, J.W.1    Morgan, J.G.2    Palings, I.3    Hirata, M.4    Yen, M.H.5
  • 27
    • 0024391711 scopus 로고
    • Interaction of human defensins with Escherichia coli: Mechanism of bactericidal activity
    • Lehrer, R. I., A. Barton, K. A. Daher, S. S. L. Harwig, T. Ganz, and M. E. Selsted. 1989. Interaction of human defensins with Escherichia coli: mechanism of bactericidal activity. J. Clin. Invest. 84:553-561.
    • (1989) J. Clin. Invest. , vol.84 , pp. 553-561
    • Lehrer, R.I.1    Barton, A.2    Daher, K.A.3    Harwig, S.S.L.4    Ganz, T.5    Selsted, M.E.6
  • 28
    • 0023920225 scopus 로고
    • Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry
    • Lehrer, R. I., A. Barton, and T. Ganz. 1988. Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry. J. Immunol. Methods 108:153-158.
    • (1988) J. Immunol. Methods , vol.108 , pp. 153-158
    • Lehrer, R.I.1    Barton, A.2    Ganz, T.3
  • 29
    • 0030012702 scopus 로고    scopus 로고
    • Antibiotic proteins of polymorphonuclear leukocytes
    • Levy, O. 1996. Antibiotic proteins of polymorphonuclear leukocytes. Eur. J. Haematol. 56:263-277.
    • (1996) Eur. J. Haematol. , vol.56 , pp. 263-277
    • Levy, O.1
  • 30
    • 0029032429 scopus 로고
    • Antibacterial proteins of granulocytes differ in interaction with endotoxin. Comparison of bactericidal/permeability-increasing protein, p15s, and defensins
    • Levy, O., C. E. Ooi, P. Elsbach, M. E. Doerfler, R. I. Lehrer, and J. Weiss. 1995. Antibacterial proteins of granulocytes differ in interaction with endotoxin. Comparison of bactericidal/permeability-increasing protein, p15s, and defensins. J. Immunol. 154:5403-5410.
    • (1995) J. Immunol. , vol.154 , pp. 5403-5410
    • Levy, O.1    Ooi, C.E.2    Elsbach, P.3    Doerfler, M.E.4    Lehrer, R.I.5    Weiss, J.6
  • 31
    • 0028120284 scopus 로고
    • Individual and synergistic effects of rabbit gianulocyte proteins on Escherichia coli
    • Levy, O., C. E. Ooi, J. Weiss, R. I. Lehrer, and P. Elsbach. 1994. Individual and synergistic effects of rabbit gianulocyte proteins on Escherichia coli. J. Clin. Invest. 94:672-682.
    • (1994) J. Clin. Invest. , vol.94 , pp. 672-682
    • Levy, O.1    Ooi, C.E.2    Weiss, J.3    Lehrer, R.I.4    Elsbach, P.5
  • 32
    • 0030940510 scopus 로고    scopus 로고
    • Enhanced host defense after gene transfer in the murine p47phox-deficient model of chronic granulomatous disease
    • Mardiney, M., III, S. H. Jackson, S. K. Spratt, F. Li, S. M. Holland, and H. L. Malech. 1997. Enhanced host defense after gene transfer in the murine p47phox-deficient model of chronic granulomatous disease. Blood 89:2268-2275.
    • (1997) Blood , vol.89 , pp. 2268-2275
    • Mardiney M. III1    Jackson, S.H.2    Spratt, S.K.3    Li, F.4    Holland, S.M.5    Malech, H.L.6
  • 33
    • 0022580949 scopus 로고
    • Interaction of polycationic antibiotics with Pseudomonas aeruginosa lipopolysaccharide and lipid A studied by using dansyl-polymyxin
    • Moore, R. A., N. C. Bates, and R. E. W. Hancock. 1986. Interaction of polycationic antibiotics with Pseudomonas aeruginosa lipopolysaccharide and lipid A studied by using dansyl-polymyxin. Antimicrob. Agents Chemother. 29:496-500.
    • (1986) Antimicrob. Agents Chemother. , vol.29 , pp. 496-500
    • Moore, R.A.1    Bates, N.C.2    Hancock, R.E.W.3
  • 34
    • 0003772229 scopus 로고
    • National Committee for Clinical Laboratory Standards. Wayne, Pa.
    • National Committee for Clinical Laboratory Standards. 1993. Document M7-A3. National Committee for Clinical Laboratory Standards. Wayne, Pa.
    • (1993) Document M7-A3
  • 35
    • 0031028188 scopus 로고    scopus 로고
    • Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins
    • Panyutich, A., J. Shi, P. L. Boutz, C. Zhao, and T. Ganz. 1997. Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins. Infect. Immun. 65: 978-985.
    • (1997) Infect. Immun. , vol.65 , pp. 978-985
    • Panyutich, A.1    Shi, J.2    Boutz, P.L.3    Zhao, C.4    Ganz, T.5
  • 37
    • 0024349857 scopus 로고
    • Primary structure of a new cysteine proteinase inhibitor from pig leukocytes
    • Ritonja, A., M. Kopitar, R. Jerala, and V. Turk. 1989. Primary structure of a new cysteine proteinase inhibitor from pig leukocytes. FEBS Lett. 255:211-214.
    • (1989) FEBS Lett. , vol.255 , pp. 211-214
    • Ritonja, A.1    Kopitar, M.2    Jerala, R.3    Turk, V.4
  • 38
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better the 70% accuracy
    • Rost, B., and C. Sander. 1993. Prediction of protein secondary structure at better the 70% accuracy. J. Mol. Biol. 232:584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 39
    • 0018702835 scopus 로고
    • Interaction of divalent cations and polymyxin B with lipopolysaccharide
    • Schindler, M., and M. J. Osborn. 1979. Interaction of divalent cations and polymyxin B with lipopolysaccharide. Biochemistry 18:4425-4430.
    • (1979) Biochemistry , vol.18 , pp. 4425-4430
    • Schindler, M.1    Osborn, M.J.2
  • 40
    • 0026739037 scopus 로고
    • Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins
    • Scocchi, M., B. Skerlavaj, D. Romeo, and R. Gennaro. 1992. Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins. Eur. J. Biochem. 209:589-595.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 589-595
    • Scocchi, M.1    Skerlavaj, B.2    Romeo, D.3    Gennaro, R.4
  • 41
    • 0030880531 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils
    • Sorensen, O., K. Arnljots, J. B. Cowland, D. F. Bainton, and N. Borregaard. 1997. The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood 90:2796-2803.
    • (1997) Blood , vol.90 , pp. 2796-2803
    • Sorensen, O.1    Arnljots, K.2    Cowland, J.B.3    Bainton, D.F.4    Borregaard, N.5
  • 42
    • 0030805339 scopus 로고    scopus 로고
    • An ELISA for hCAP-18, the cathelicidin present in human neutrophils and plasma
    • Sorensøn, O., J. B. Cowland, J. Askaa, and N. Borregaard. 1997. An ELISA for hCAP-18, the cathelicidin present in human neutrophils and plasma. J. Immunol. Methods 206:53-59.
    • (1997) J. Immunol. Methods , vol.206 , pp. 53-59
    • Sorensøn, O.1    Cowland, J.B.2    Askaa, J.3    Borregaard, N.4
  • 43
    • 0028000143 scopus 로고
    • Infection with Pseudomonas cepacia in chronic granulomatous disease: Role of non-oxidative killing by neutrophils in host defense
    • Speert, D. P., M. Bond, R. C. Woodman, and J. T. Curnutte. 1994. Infection with Pseudomonas cepacia in chronic granulomatous disease: role of non-oxidative killing by neutrophils in host defense. J. Infect. Dis. 170:1524-1531.
    • (1994) J. Infect. Dis. , vol.170 , pp. 1524-1531
    • Speert, D.P.1    Bond, M.2    Woodman, R.C.3    Curnutte, J.T.4
  • 44
    • 0030623934 scopus 로고    scopus 로고
    • Designer assays for antimicrobial peptides
    • Steinberg, D., and R. I. Lehrer. 1997. Designer assays for antimicrobial peptides. Methods Mol. Biol. 78:169-186.
    • (1997) Methods Mol. Biol. , vol.78 , pp. 169-186
    • Steinberg, D.1    Lehrer, R.I.2
  • 46
    • 0017372652 scopus 로고
    • Selective binding of polymyxin B to negatively charged lipid monolayers
    • Teuber, M., and I. R. Miller. 1977. Selective binding of polymyxin B to negatively charged lipid monolayers. Biochim. Biophys. Acta 467:280-289.
    • (1977) Biochim. Biophys. Acta , vol.467 , pp. 280-289
    • Teuber, M.1    Miller, I.R.2
  • 47
    • 0028294292 scopus 로고
    • Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit leukocytes
    • Tossi, A., M. Scocchi, B. Skerlavaj, and R. Gennaro. 1994. Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit leukocytes. FEBS Lett. 339:108-112.
    • (1994) FEBS Lett. , vol.339 , pp. 108-112
    • Tossi, A.1    Scocchi, M.2    Skerlavaj, B.3    Gennaro, R.4
  • 49
    • 0000195486 scopus 로고    scopus 로고
    • Structure and activity of protegrin-1 in model lipid membranes
    • Waring, A. J., S. S. L. Harwig, and R. I. Lehrer. 1996. Structure and activity of protegrin-1 in model lipid membranes. Protein Peptide Lett. 3:177-184.
    • (1996) Protein Peptide Lett. , vol.3 , pp. 177-184
    • Waring, A.J.1    Harwig, S.S.L.2    Lehrer, R.I.3
  • 50
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White, S. H., W. C. Wimley, and M. E. Selsted. 1995. Structure, function, and membrane integration of defensins. Curr. Opin. Struct. Biol. 5:521-527.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 51
    • 0002439879 scopus 로고
    • Circular dichroism of peptides
    • S. Udenfriend, J. Meienhofer, and V. J. Hruby (ed.), Academic Press, Inc., New York, N.Y.
    • Woody, R. W. 1985. Circular dichroism of peptides, p. 15-114. In S. Udenfriend, J. Meienhofer, and V. J. Hruby (ed.), The peptides: synthesis and biology, vol. 7. Academic Press, Inc., New York, N.Y.
    • (1985) The Peptides: Synthesis and Biology , vol.7 , pp. 15-114
    • Woody, R.W.1
  • 52
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-termmal antimicrobial domain
    • Zanetti, M., R. Gennaro, and D. Romeo. 1995. Cathelicidins: a novel protein family with a common proregion and a variable C-termmal antimicrobial domain. FEBS Lett. 374:1-5.
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 53
    • 0029015666 scopus 로고
    • The structure of porcine protegrin genes
    • Zhao, C., T. Ganz, and R. I. Lehrer. 1995. The structure of porcine protegrin genes. FEBS Lett. 368:197-202.
    • (1995) FEBS Lett. , vol.368 , pp. 197-202
    • Zhao, C.1    Ganz, T.2    Lehrer, R.I.3


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