메뉴 건너뛰기




Volumn 52, Issue 5, 2008, Pages 1812-1819

Enhanced resistance to bacterial infection in protegrin-1 transgenic mice

Author keywords

[No Author keywords available]

Indexed keywords

PROTEGRIN; PROTEGRIN 1;

EID: 42949110073     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.01530-07     Document Type: Article
Times cited : (19)

References (41)
  • 3
    • 1542724426 scopus 로고    scopus 로고
    • The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes
    • Bowdish, D. M., D. J. Davidson, D. P. Speert, and R. E. Hancock. 2004. The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes. J. Immunol. 172:3758-3765.
    • (2004) J. Immunol , vol.172 , pp. 3758-3765
    • Bowdish, D.M.1    Davidson, D.J.2    Speert, D.P.3    Hancock, R.E.4
  • 5
    • 0019551730 scopus 로고
    • Western blotting: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. 1981. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:195-203.
    • (1981) Anal. Biochem , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 6
    • 0035163451 scopus 로고    scopus 로고
    • Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds
    • Cole, A. M., J. Shi, A. Ceccarelli, Y. H. Kim, A. Park, and T. Ganz. 2001. Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds. Blood 97:297-304.
    • (2001) Blood , vol.97 , pp. 297-304
    • Cole, A.M.1    Shi, J.2    Ceccarelli, A.3    Kim, Y.H.4    Park, A.5    Ganz, T.6
  • 7
    • 0027140425 scopus 로고
    • Immunogens of Pasteurella
    • Confer, A. W. 1993. Immunogens of Pasteurella. Vet. Microbiol. 37:353-368.
    • (1993) Vet. Microbiol , vol.37 , pp. 353-368
    • Confer, A.W.1
  • 8
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • De, Y., Q. Chen, A. P. Schmidt, G. M. Anderson, J. M. Wang, J. Wooters, J. J. Oppenheim, and O. Chertov. 2000. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192:1069-1074.
    • (2000) J. Exp. Med , vol.192 , pp. 1069-1074
    • De, Y.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 9
    • 0033981142 scopus 로고    scopus 로고
    • Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells
    • Diamond, G., V. Kaiser, J. Rhodes, J. P. Russell, and C. L. Bevins. 2000. Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells. Infect. Immun. 68:113-119.
    • (2000) Infect. Immun , vol.68 , pp. 113-119
    • Diamond, G.1    Kaiser, V.2    Rhodes, J.3    Russell, J.P.4    Bevins, C.L.5
  • 10
    • 0141867817 scopus 로고    scopus 로고
    • Inducible expression of green fluorescent protein in porcine tracheal epithelial cells by the bovine tracheal antimicrobial peptide promoter
    • Dyce, P. W., R. J. DeVries, J. Walton, R. R. Hacker, and J. Li. 2003. Inducible expression of green fluorescent protein in porcine tracheal epithelial cells by the bovine tracheal antimicrobial peptide promoter. Biotechnol. Bioeng. 84:374-381.
    • (2003) Biotechnol. Bioeng , vol.84 , pp. 374-381
    • Dyce, P.W.1    DeVries, R.J.2    Walton, J.3    Hacker, R.R.4    Li, J.5
  • 11
    • 3042737036 scopus 로고    scopus 로고
    • In vitro activity of protegrin-1 and beta-defensin-1, alone and in combination with isoniazid, against Mycobacterium tuberculosis
    • Fattorini, L., R. Gennaro, M. Zanetti, D. Tan, L. Brunori, F. Giannoni, M. Pardini, and G. Orefici. 2004. In vitro activity of protegrin-1 and beta-defensin-1, alone and in combination with isoniazid, against Mycobacterium tuberculosis. Peptides 25:1075-1077.
    • (2004) Peptides , vol.25 , pp. 1075-1077
    • Fattorini, L.1    Gennaro, R.2    Zanetti, M.3    Tan, D.4    Brunori, L.5    Giannoni, F.6    Pardini, M.7    Orefici, G.8
  • 12
    • 0033377813 scopus 로고    scopus 로고
    • Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system
    • Gudmundsson, G. H., and B. Agerberth. 1999. Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system. J. Immunol. Methods 232:45-54.
    • (1999) J. Immunol. Methods , vol.232 , pp. 45-54
    • Gudmundsson, G.H.1    Agerberth, B.2
  • 13
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E., and H. G. Sahl. 2006. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24:1551-1557.
    • (2006) Nat. Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 14
    • 0036931504 scopus 로고    scopus 로고
    • Streptogramin resistance among Enterococcus faecium isolated from production animals in Denmark in 1997
    • Jensen, L. B., A. M. Hammerum, F. Bager, and F. M. Aarestrup. 2002. Streptogramin resistance among Enterococcus faecium isolated from production animals in Denmark in 1997. Microb. Drug Resist. 8:369-374.
    • (2002) Microb. Drug Resist , vol.8 , pp. 369-374
    • Jensen, L.B.1    Hammerum, A.M.2    Bager, F.3    Aarestrup, F.M.4
  • 15
    • 0025652553 scopus 로고
    • Clinical guidelines and indications for bronchoalveolar lavage (BAL): Report of the European Society of Pneumology Task Group on BALF
    • Klech, H., and C. Hutter. 1990. Clinical guidelines and indications for bronchoalveolar lavage (BAL): report of the European Society of Pneumology Task Group on BALF. Eur. Respir. J. 3:937-974.
    • (1990) Eur. Respir. J , vol.3 , pp. 937-974
    • Klech, H.1    Hutter, C.2
  • 16
    • 0023737102 scopus 로고
    • Bronchoalveolar lavage cell differential on microscope glass cover: A simple and accurate technique
    • Laviolette, M., M. Carreau, and R. Coulombe. 1988. Bronchoalveolar lavage cell differential on microscope glass cover: a simple and accurate technique. Am. Rev. Respir. Dis. 138:451-457.
    • (1988) Am. Rev. Respir. Dis , vol.138 , pp. 451-457
    • Laviolette, M.1    Carreau, M.2    Coulombe, R.3
  • 17
    • 14844351540 scopus 로고    scopus 로고
    • Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection
    • Lee, P. H., T. Ohtake, M. Zaiou, M. Murakami, J. A. Rudisill, K. H. Lin, and R. L. Gallo. 2005. Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection. Proc. Natl. Acad. Sci. USA 102:3750-3755.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3750-3755
    • Lee, P.H.1    Ohtake, T.2    Zaiou, M.3    Murakami, M.4    Rudisill, J.A.5    Lin, K.H.6    Gallo, R.L.7
  • 19
    • 0033112782 scopus 로고    scopus 로고
    • Agents of the "suis-ide diseases" of swine: Actinobacillus suis, Haemophilus parasuis, and Streptococcus suis
    • MacInnes, J. I., and R. Desrosiers. 1999. Agents of the "suis-ide diseases" of swine: Actinobacillus suis, Haemophilus parasuis, and Streptococcus suis. Can. J. Vet. Res. 63:83-89.
    • (1999) Can. J. Vet. Res , vol.63 , pp. 83-89
    • MacInnes, J.I.1    Desrosiers, R.2
  • 20
    • 4344697819 scopus 로고    scopus 로고
    • Actinobacillus suis, a potential cause of abortion in gilts and low parity sows
    • Mauch, C., and G. Bilkei. 2004. Actinobacillus suis, a potential cause of abortion in gilts and low parity sows. Vet. J. 168:186-187.
    • (2004) Vet. J , vol.168 , pp. 186-187
    • Mauch, C.1    Bilkei, G.2
  • 21
    • 0030043634 scopus 로고    scopus 로고
    • In vitro activity of the antimicrobial peptides human and rabbit defensins and porcine leukocyte protegrin against Mycobacterium tuberculosis
    • Miyakawa, Y., P. Ratnakar, A. G. Rao, M. L. Costello, O. Mathieu-Costello, R. I. Lehrer, and A. Catanzaro. 1996. In vitro activity of the antimicrobial peptides human and rabbit defensins and porcine leukocyte protegrin against Mycobacterium tuberculosis. Infect. Immun. 64:926-932.
    • (1996) Infect. Immun , vol.64 , pp. 926-932
    • Miyakawa, Y.1    Ratnakar, P.2    Rao, A.G.3    Costello, M.L.4    Mathieu-Costello, O.5    Lehrer, R.I.6    Catanzaro, A.7
  • 23
    • 34548863368 scopus 로고    scopus 로고
    • An experimental model of Actinobacillus suis infection in mice
    • Ojha, S., M. A. Hayes, P. V. Turner, and J. I. MacInnes. 2007. An experimental model of Actinobacillus suis infection in mice. Comp. Med. 57:340-348.
    • (2007) Comp. Med , vol.57 , pp. 340-348
    • Ojha, S.1    Hayes, M.A.2    Turner, P.V.3    MacInnes, J.I.4
  • 24
    • 25444511780 scopus 로고    scopus 로고
    • Identification of Actinobacillus suis genes essential for the colonization of the upper respiratory tract of swine
    • Ojha, S., M. Sirois, and J. I. MacInnes. 2005. Identification of Actinobacillus suis genes essential for the colonization of the upper respiratory tract of swine. Infect. Immun. 73:7032-7039.
    • (2005) Infect. Immun , vol.73 , pp. 7032-7039
    • Ojha, S.1    Sirois, M.2    MacInnes, J.I.3
  • 25
    • 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
  • 26
    • 0037087422 scopus 로고    scopus 로고
    • Antimicrobial peptides initiate IL-1 beta posttranslational processing: A novel role beyond innate immunity
    • Perregaux, D. G., K. Bhavsar, L. Contillo, J. Shi, and C. A. Gabel. 2002. Antimicrobial peptides initiate IL-1 beta posttranslational processing: a novel role beyond innate immunity. J. Immunol. 168:3024-3032.
    • (2002) J. Immunol , vol.168 , pp. 3024-3032
    • Perregaux, D.G.1    Bhavsar, K.2    Contillo, L.3    Shi, J.4    Gabel, C.A.5
  • 27
    • 0031034573 scopus 로고    scopus 로고
    • Protegrin structure and activity against Neisseria gonorrhoeae
    • Qu, X. D., S. S. Harwig, W. M. Shafer, and R. I. Lehrer. 1997. Protegrin structure and activity against Neisseria gonorrhoeae. Infect. Immun. 65:636-639.
    • (1997) Infect. Immun , vol.65 , pp. 636-639
    • Qu, X.D.1    Harwig, S.S.2    Shafer, W.M.3    Lehrer, R.I.4
  • 29
    • 0026755667 scopus 로고
    • Detection of extracellular neutrophil elastase in hamster lungs after intratracheal instillation of E. coli lipopolysaccharide using a fluorogenic, elastase-specific, synthetic substrate
    • Rudolphus, A., J. Stolk, C. van Twisk, C. J. van Noorden, J. H. Dijkman, and J. A. Kramps. 1992. Detection of extracellular neutrophil elastase in hamster lungs after intratracheal instillation of E. coli lipopolysaccharide using a fluorogenic, elastase-specific, synthetic substrate. Am. J. Pathol. 141:153-160.
    • (1992) Am. J. Pathol , vol.141 , pp. 153-160
    • Rudolphus, A.1    Stolk, J.2    van Twisk, C.3    van Noorden, C.J.4    Dijkman, J.H.5    Kramps, J.A.6
  • 30
    • 0037417311 scopus 로고    scopus 로고
    • Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin
    • Salzman, N. H., D. Ghosh, K. M. Huttner, Y. Paterson, and C. L. Bevins. 2003. Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature 422:522-526.
    • (2003) Nature , vol.422 , pp. 522-526
    • Salzman, N.H.1    Ghosh, D.2    Huttner, K.M.3    Paterson, Y.4    Bevins, C.L.5
  • 31
    • 0031870993 scopus 로고    scopus 로고
    • The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids
    • Shi, J., and T. Ganz. 1998. The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids. Infect. Immun. 66:3611-3617.
    • (1998) Infect. Immun , vol.66 , pp. 3611-3617
    • Shi, J.1    Ganz, T.2
  • 35
    • 33646586648 scopus 로고    scopus 로고
    • Human cathelicidin LL-37 is a chemoattractant for eosinophils and neutrophils that acts via formyl-peptide receptors
    • Tjabringa, G. S., D. K. Ninaber, J. W. Drijfhout, K. F. Rabe, and P. S. Hiemstra. 2006. Human cathelicidin LL-37 is a chemoattractant for eosinophils and neutrophils that acts via formyl-peptide receptors. Int. Arch. Allergy Immunol. 140:103-112.
    • (2006) Int. Arch. Allergy Immunol , vol.140 , pp. 103-112
    • Tjabringa, G.S.1    Ninaber, D.K.2    Drijfhout, J.W.3    Rabe, K.F.4    Hiemstra, P.S.5
  • 36
    • 0037133259 scopus 로고    scopus 로고
    • Constitutive expression of a single antimicrobial peptide can restore wild-type resistance to infection in immunodeficient Drosophila mutants
    • Tzou, P., J. M. Reichhart, and B. Lemaitre. 2002. Constitutive expression of a single antimicrobial peptide can restore wild-type resistance to infection in immunodeficient Drosophila mutants. Proc. Natl. Acad. Sci. USA 99:2152-2157.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2152-2157
    • Tzou, P.1    Reichhart, J.M.2    Lemaitre, B.3
  • 37
    • 16844380318 scopus 로고    scopus 로고
    • Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells
    • van Wetering, S., G. S. Tjabringa, and P. S. Hiemstra. 2005. Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells. J. Leukoc. Biol. 77:444-450.
    • (2005) J. Leukoc. Biol , vol.77 , pp. 444-450
    • van Wetering, S.1    Tjabringa, G.S.2    Hiemstra, P.S.3
  • 39
    • 0035032985 scopus 로고    scopus 로고
    • Synergistic interactions between mammalian antimicrobial defense peptides
    • Yan, H., and R. E. Hancock. 2001. Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob. Agents Chemother. 45:1558-1560.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 1558-1560
    • Yan, H.1    Hancock, R.E.2
  • 40
    • 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
  • 41
    • 2942576132 scopus 로고    scopus 로고
    • Influence of tissue origins and external microenvironment on porcine foetal fibroblast growth, proliferative life span and genome stability
    • Zhu, H., B. Tamot, M. Quinton, J. Walton, R. R. Hacker, and J. Li. 2004. Influence of tissue origins and external microenvironment on porcine foetal fibroblast growth, proliferative life span and genome stability. Cell Prolif. 37:255-266.
    • (2004) Cell Prolif , vol.37 , pp. 255-266
    • Zhu, H.1    Tamot, B.2    Quinton, M.3    Walton, J.4    Hacker, R.R.5    Li, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.