메뉴 건너뛰기




Volumn 1, Issue 2, 2009, Pages 118-122

Degradation of human α- And β-defensins by culture supernatants of porphyromonas gingivalis strain 381

Author keywords

Defensins; Gingipains; Porphyromonas gingivalis; Proteases

Indexed keywords

ALPHA DEFENSIN; BACTERIAL ENZYME; BETA DEFENSIN; PROTEINASE; BIOLOGICAL FACTOR; PEPTIDE HYDROLASE;

EID: 70350461325     PISSN: 1662811X     EISSN: 16628128     Source Type: Journal    
DOI: 10.1159/000181015     Document Type: Article
Times cited : (55)

References (35)
  • 1
    • 0030280463 scopus 로고    scopus 로고
    • Periodontal diseases: Pathogenesis
    • Offenbacher S: Periodontal diseases: pathogenesis. Ann Periodontol 1996; 1:821-878.
    • (1996) Ann Periodontol , vol.1 , pp. 821-878
    • Offenbacher, S.1
  • 5
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: Pathogenic mechanisms of Por-phyromonas gingivalis
    • Lamont RJ, Jenkinson HF: Life below the gum line: pathogenic mechanisms of Por-phyromonas gingivalis . Microbiol Mol Biol Rev 1998; 62:1244-1263.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 6
    • 0033202353 scopus 로고    scopus 로고
    • Porphyromonas gingivalis virulence factors and invasion of cells of the cardiovascular system
    • Progulske-Fox A, Kozarov E, Dorn B, Dunn W Jr., Burks J, Wu Y: Porphyromonas gingivalis virulence factors and invasion of cells of the cardiovascular system. J Periodontal Res 1999;34:393-399.
    • (1999) J Periodontal Res , vol.34 , pp. 393-399
    • Progulske-Fox, A.1    Kozarov, E.2    Dorn, B.3    Dunn Jr., W.4    Burks, J.5    Wu, Y.6
  • 7
    • 0030338378 scopus 로고    scopus 로고
    • Porphyromonas gingivalis proteinases in periodontitis, a review
    • Potempa J, Travis J: Porphyromonas gingivalis proteinases in periodontitis, a review. Acta Biochim Pol 1996; 43:455-465.
    • (1996) Acta Biochim Pol , vol.43 , pp. 455-465
    • Potempa, J.1    Travis, J.2
  • 8
    • 0033515503 scopus 로고    scopus 로고
    • Prolyl tripeptidyl peptidase from Porphyromonas gingivalis : A novel enzyme with possible pathological implications for the development of periodontitis
    • Banbula A, Mak P, Bugno M, Silberring J, Dubin A, Nelson D, Travis J, Potempa J: Prolyl tripeptidyl peptidase from Porphyromonas gingivalis : a novel enzyme with possible pathological implications for the development of periodontitis. J Biol Chem 1999; 274: 9246-9252.
    • (1999) J Biol Chem , vol.274 , pp. 9246-9252
    • Banbula, A.1    Mak, P.2    Bugno, M.3    Silberring, J.4    Dubin, A.5    Nelson, D.6    Travis, J.7    Potempa, J.8
  • 9
    • 0033982189 scopus 로고    scopus 로고
    • Emerging family of proline-specific peptidases of Porphyromonas gingivalis : Purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV
    • Banbula A, Bugno M, Goldstein J, Yen J, Nelson D, Travis J, Potempa J: Emerging family of proline-specific peptidases of Porphyromonas gingivalis : purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV. Infect Immun 2000;68:1176-1182.
    • (2000) Infect Immun , vol.68 , pp. 1176-1182
    • Banbula, A.1    Bugno, M.2    Goldstein, J.3    Yen, J.4    Nelson, D.5    Travis, J.6    Potempa, J.7
  • 10
    • 0030631850 scopus 로고    scopus 로고
    • Porphyromonas gingivalis proteinases as virulence factors in the development of periodontitis
    • Travis J, Pike R, Imamura T, Potempa J: Porphyromonas gingivalis proteinases as virulence factors in the development of periodontitis. J Periodontal Res 1997;32:120-125.
    • (1997) J Periodontal Res , vol.32 , pp. 120-125
    • Travis, J.1    Pike, R.2    Imamura, T.3    Potempa, J.4
  • 11
    • 0037261991 scopus 로고    scopus 로고
    • The role of gingipains in the pathogenesis of periodontal disease
    • Imamura T: The role of gingipains in the pathogenesis of periodontal disease. J Periodontol 2003; 74:111-118.
    • (2003) J Periodontol , vol.74 , pp. 111-118
    • Imamura, T.1
  • 13
    • 15544387126 scopus 로고    scopus 로고
    • Functional implication of the hydrolysis of platelet endothelial cell adhesion molecule 1 (CD31) by gingipains of Porphyromonas gingivalis for the pathology of periodontal disease
    • Yun PL, Decarlo AA, Chapple CC, Hunter N: Functional implication of the hydrolysis of platelet endothelial cell adhesion molecule 1 (CD31) by gingipains of Porphyromonas gingivalis for the pathology of periodontal disease. Infect Immun 2005; 73:1386-1398.
    • (2005) Infect Immun , vol.73 , pp. 1386-1398
    • Yun, P.L.1    Decarlo, A.A.2    Chapple, C.C.3    Hunter, N.4
  • 14
    • 0034801467 scopus 로고    scopus 로고
    • Degradation of host heme proteins by lysine- and arginine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis
    • Sroka A, Sztukowska M, Potempa J, Travis J, Genco CA: Degradation of host heme proteins by lysine- and arginine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis . J Bacteriol 2001;183:5609-5616.
    • (2001) J Bacteriol , vol.183 , pp. 5609-5616
    • Sroka, A.1    Sztukowska, M.2    Potempa, J.3    Travis, J.4    Genco, C.A.5
  • 15
    • 0032899780 scopus 로고    scopus 로고
    • Modulation of antibacterial peptide activity by products of Porphyromonas gingivalis and Prevotella spp
    • Devine DA, Marsh PD, Percival RS, Ranga-rajan M, Curtis MA: Modulation of antibacterial peptide activity by products of Porphyromonas gingivalis and Prevotella spp. Microbiology 1999; 145: 965-971.
    • (1999) Microbiology , vol.145 , pp. 965-971
    • Devine, D.A.1    Marsh, P.D.2    Percival, R.S.3    Ranga-rajan, M.4    Curtis, M.A.5
  • 19
    • 34147222846 scopus 로고    scopus 로고
    • Quantification of human beta-defensin-2 and -3 in body fluids: Application for studies of innate immunity
    • Ghosh SK, Gerken TA, Schneider KM, Feng Z, McCormick TS, Weinberg A: Quantification of human beta-defensin-2 and -3 in body fluids: application for studies of innate immunity. Clin Chem 2007;53:757-765.
    • (2007) Clin Chem , vol.53 , pp. 757-765
    • Ghosh, S.K.1    Gerken, T.A.2    Schneider, K.M.3    Feng, Z.4    McCormick, T.S.5    Weinberg, A.6
  • 23
    • 2542480000 scopus 로고    scopus 로고
    • Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
    • Yang D, Biragyn A, Hoover DM, Lubkowski J, Oppenheim JJ: Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu Rev Immunol 2004;22: 181-215.
    • (2004) Annu Rev Immunol , vol.22 , pp. 181-215
    • Yang, D.1    Biragyn, A.2    Hoover, D.M.3    Lubkowski, J.4    Oppenheim, J.J.5
  • 24
    • 1542513868 scopus 로고    scopus 로고
    • Human ß-defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms
    • Joly S, Maze C, McCray PB Jr, Guthmiller JM: Human ß-defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms. J Clin Microbiol 2004; 42: 1024-1029.
    • (2004) J Clin Microbiol , vol.42 , pp. 1024-1029
    • Joly, S.1    Maze, C.2    McCray Jr, P.B.3    Guthmiller, J.M.4
  • 25
    • 0034473528 scopus 로고    scopus 로고
    • The role of bacterial and host proteinases in periodontal disease
    • Travis J, Banbula A, Potempa J: The role of bacterial and host proteinases in periodontal disease. Adv Exp Med Biol 2000; 477: 455-465.
    • (2000) Adv Exp Med Biol , vol.477 , pp. 455-465
    • Travis, J.1    Banbula, A.2    Potempa, J.3
  • 27
    • 34548230420 scopus 로고    scopus 로고
    • Susceptibility of various oral bacteria to antimicrobial peptides and to phagocytosis by neutrophils
    • Ji S, Hyun J, Park E, Lee BL, Kim KK, Choi Y: Susceptibility of various oral bacteria to antimicrobial peptides and to phagocytosis by neutrophils. J Periodontal Res 2007;42: 410-419.
    • (2007) J Periodontal Res , vol.42 , pp. 410-419
    • Ji, S.1    Hyun, J.2    Park, E.3    Lee, B.L.4    Kim, K.K.5    Choi, Y.6
  • 30
    • 4544254599 scopus 로고    scopus 로고
    • Proteus mi-rabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides
    • Belas R, Manos J, Suvanasuthi R: Proteus mi-rabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides. Infect Immun 2004; 72: 5159-5167.
    • (2004) Infect Immun , vol.72 , pp. 5159-5167
    • Belas, R.1    Manos, J.2    Suvanasuthi, R.3
  • 32
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • Ganz T: Defensins: antimicrobial peptides of innate immunity. Nat Rev Immunol 2003;3: 710-720.
    • (2003) Nat Rev Immunol , vol.3 , pp. 710-720
    • Ganz, T.1
  • 33
    • 4444246692 scopus 로고    scopus 로고
    • Primate defensins
    • Lehrer RI: Primate defensins. Nat Rev Microbiol 2004;2:727-738.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 727-738
    • Lehrer, R.I.1
  • 34
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA: Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 2005;3:238-250.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 35
    • 0034960109 scopus 로고    scopus 로고
    • The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity
    • Yang D, Chertov O, Oppenheim JJ: The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity. Cell Mol Life Sci 2001;58:978-989.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 978-989
    • Yang, D.1    Chertov, O.2    Oppenheim, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.