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Volumn 289, Issue 47, 2014, Pages 32481-32487

Peptidyl arginine deiminase from porphyromonas gingivalis abolishes anaphylatoxin C5a activity

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; BACTERIA; BIOCHEMISTRY; CALCIUM; CELL CULTURE; DISEASES; EVOLUTIONARY ALGORITHMS; MASS SPECTROMETRY;

EID: 84911906315     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C114.617142     Document Type: Article
Times cited : (79)

References (28)
  • 1
    • 0027621554 scopus 로고
    • Prevalence, extent, severity and progression of periodontal disease
    • Brown, L.J., and Löe, H. (1993) Prevalence, extent, severity and progression of periodontal disease. Periodontology 2000 2, 57-71
    • (1993) Periodontology 2000 , vol.2 , pp. 57-71
    • Brown, L.J.1    Löe, H.2
  • 2
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: Pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont, R. J., and Jenkinson, H. F. (1998) Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev. 62, 1244-1263
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 4
    • 0033004481 scopus 로고    scopus 로고
    • Purification, characterization, and sequence analysis of a potential virulence factor from Porphyromonas gingivalis, peptidylarginine deiminase
    • McGraw, W. T., Potempa, J., Farley, D., and Travis, J. (1999) Purification, characterization, and sequence analysis of a potential virulence factor from Porphyromonas gingivalis, peptidylarginine deiminase. Infect. Immun. 67, 3248-3256
    • (1999) Infect. Immun. , vol.67 , pp. 3248-3256
    • McGraw, W.T.1    Potempa, J.2    Farley, D.3    Travis, J.4
  • 5
    • 53449087927 scopus 로고    scopus 로고
    • Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: A naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation
    • Loos, T., Mortier, A., Gouwy, M., Ronsse, I., Put, W., Lenaerts, J. P., Van Damme, J., and Proost, P. (2008) Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation. Blood 112, 2648-2656
    • (2008) Blood , vol.112 , pp. 2648-2656
    • Loos, T.1    Mortier, A.2    Gouwy, M.3    Ronsse, I.4    Put, W.5    Lenaerts, J.P.6    Van Damme, J.7    Proost, P.8
  • 7
    • 77955733490 scopus 로고    scopus 로고
    • Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and a-enolase: Implications for autoimmunity in rheumatoid arthritis
    • Wegner, N., Wait, R., Sroka, A., Eick, S., Nguyen, K. A., Lundberg, K., Kinloch, A., Culshaw, S., Potempa, J., and Venables, P. J. (2010) Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and a-enolase: implications for autoimmunity in rheumatoid arthritis. Arthritis Rheum. 62, 2662-2672
    • (2010) Arthritis Rheum. , vol.62 , pp. 2662-2672
    • Wegner, N.1    Wait, R.2    Sroka, A.3    Eick, S.4    Nguyen, K.A.5    Lundberg, K.6    Kinloch, A.7    Culshaw, S.8    Potempa, J.9    Venables, P.J.10
  • 9
    • 35348821843 scopus 로고    scopus 로고
    • Function, structure and therapeutic potential of complement C5a receptors
    • Monk, P. N., Scola, A. M., Madala, P., and Fairlie, D. P. (2007) Function, structure and therapeutic potential of complement C5a receptors. Br. J. Pharmacol. 152, 429-448
    • (2007) Br. J. Pharmacol. , vol.152 , pp. 429-448
    • Monk, P.N.1    Scola, A.M.2    Madala, P.3    Fairlie, D.P.4
  • 10
    • 84883181202 scopus 로고    scopus 로고
    • Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingiva-lis
    • Zhou, X. Y., Gao, J. L., Hunter, N., Potempa, J., and Nguyen, K. A. (2013) Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingiva-lis. Mol. Microbiol. 89, 903-917
    • (2013) Mol. Microbiol. , vol.89 , pp. 903-917
    • Zhou, X.Y.1    Gao, J.L.2    Hunter, N.3    Potempa, J.4    Nguyen, K.A.5
  • 11
    • 27944438816 scopus 로고    scopus 로고
    • A continuous spectrophotometric assay method for peptidylarginine deiminase type 4 activity
    • Liao, Y. F., Hsieh, H. C., Liu, G. Y., and Hung, H. C. (2005) A continuous spectrophotometric assay method for peptidylarginine deiminase type 4 activity. Anal. Biochem. 347, 176-181
    • (2005) Anal. Biochem. , vol.347 , pp. 176-181
    • Liao, Y.F.1    Hsieh, H.C.2    Liu, G.Y.3    Hung, H.C.4
  • 13
    • 0028942506 scopus 로고
    • The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain
    • Potempa, J., Pike, R., and Travis, J. (1995) The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain. Infect. Immun. 63, 1176-1182
    • (1995) Infect. Immun. , vol.63 , pp. 1176-1182
    • Potempa, J.1    Pike, R.2    Travis, J.3
  • 14
    • 0030893029 scopus 로고    scopus 로고
    • Undifferentiated U937 cells trans-fected with chemoattractant receptors: A model system to investigate che-motactic mechanisms and receptor structure/function relationships
    • Kew, R. R., Peng, T., DiMartino, S. J., Madhavan, D., Weinman, S. J., Cheng, D., and Prossnitz, E. R. (1997) Undifferentiated U937 cells trans-fected with chemoattractant receptors: a model system to investigate che-motactic mechanisms and receptor structure/function relationships. J. Leukocyte Biol. 61, 329-337
    • (1997) J. Leukocyte Biol. , vol.61 , pp. 329-337
    • Kew, R.R.1    Peng, T.2    Dimartino, S.J.3    Madhavan, D.4    Weinman, S.J.5    Cheng, D.6    Prossnitz, E.R.7
  • 15
    • 84857463226 scopus 로고    scopus 로고
    • A metalloproteinase karilysin present in the majority of Tannerella forsythia isolates inhibits all pathways of the complement system
    • Jusko, M., Potempa, J., Karim, A. Y., Ksiazek, M., Riesbeck, K., Garred, P., Eick, S., and Blom, A. M. (2012) A metalloproteinase karilysin present in the majority of Tannerella forsythia isolates inhibits all pathways of the complement system. J. Immunol. 188, 2338-2349
    • (2012) J. Immunol. , vol.188 , pp. 2338-2349
    • Jusko, M.1    Potempa, J.2    Karim, A.Y.3    Ksiazek, M.4    Riesbeck, K.5    Garred, P.6    Eick, S.7    Blom, A.M.8
  • 16
    • 0026725842 scopus 로고
    • Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis
    • Wingrove, J. A., DiScipio, R. G., Chen, Z., Potempa, J., Travis, J., and Hugli, T. E. (1992) Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis. J. Biol. Chem. 267, 18902-18907
    • (1992) J. Biol. Chem. , vol.267 , pp. 18902-18907
    • Wingrove, J.A.1    Discipio, R.G.2    Chen, Z.3    Potempa, J.4    Travis, J.5    Hugli, T.E.6
  • 17
    • 84892484811 scopus 로고    scopus 로고
    • Effect of Porphyromonas gingivalis outer membrane vesicles on gingipain-mediated detachment of cultured oral epithelial cells and immune responses
    • Nakao, R., Takashiba, S., Kosono, S., Yoshida, M., Watanabe, H., Ohnishi, M., and Senpuku, H. (2014) Effect of Porphyromonas gingivalis outer membrane vesicles on gingipain-mediated detachment of cultured oral epithelial cells and immune responses. Microbes Infect. 16, 6-16
    • (2014) Microbes Infect. , vol.16 , pp. 6-16
    • Nakao, R.1    Takashiba, S.2    Kosono, S.3    Yoshida, M.4    Watanabe, H.5    Ohnishi, M.6    Senpuku, H.7
  • 18
    • 84899842537 scopus 로고    scopus 로고
    • Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carryacargo enriched with virulence factors
    • Veith, P. D., Chen, Y. Y., Gorasia, D. G., Chen, D., Glew, M. D., O'Brien-Simpson, N. M., Cecil, J. D., Holden, J. A., and Reynolds, E. C. (2014) Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carryacargo enriched with virulence factors. J. Proteome Res. 13, 2420-2432
    • (2014) J. Proteome Res. , vol.13 , pp. 2420-2432
    • Veith, P.D.1    Chen, Y.Y.2    Gorasia, D.G.3    Chen, D.4    Glew, M.D.5    O'Brien-Simpson, N.M.6    Cecil, J.D.7    Holden, J.A.8    Reynolds, E.C.9
  • 19
    • 84869470660 scopus 로고    scopus 로고
    • Protease-dependent mechanisms of complement evasion by bacterial pathogens
    • Potempa, M., and Potempa, J. (2012) Protease-dependent mechanisms of complement evasion by bacterial pathogens. Biol. Chem. 393, 873-888
    • (2012) Biol. Chem. , vol.393 , pp. 873-888
    • Potempa, M.1    Potempa, J.2
  • 20
    • 0026443899 scopus 로고
    • Streptococcal C5a peptidase is a highly specific endopeptidase
    • Cleary, P. P., Prahbu, U., Dale, J. B., Wexler, D. E., and Handley, J. (1992) Streptococcal C5a peptidase is a highly specific endopeptidase. Infect. Immun. 60, 5219-5223
    • (1992) Infect. Immun. , vol.60 , pp. 5219-5223
    • Cleary, P.P.1    Prahbu, U.2    Dale, J.B.3    Wexler, D.E.4    Handley, J.5
  • 21
    • 34249799593 scopus 로고    scopus 로고
    • Biphasic effect ofgingipains fromPorphyromonas gingivalis on the human complement system
    • Popadiak, K., Potempa, J., Riesbeck, K., and Blom, A. M. (2007) Biphasic effect ofgingipains fromPorphyromonas gingivalis on the human complement system. J. Immunol. 178, 7242-7250
    • (2007) J. Immunol. , vol.178 , pp. 7242-7250
    • Popadiak, K.1    Potempa, J.2    Riesbeck, K.3    Blom, A.M.4
  • 22
    • 54049101495 scopus 로고    scopus 로고
    • Binding of complement inhibitor C4b-binding protein contributes to serum resistance of Porphyromonas gingivalis
    • Potempa, M., Potempa, J., Okroj, M., Popadiak, K., Eick, S., Nguyen, K. A., Riesbeck, K., and Blom, A. M. (2008) Binding of complement inhibitor C4b-binding protein contributes to serum resistance of Porphyromonas gingivalis. J. Immunol. 181, 5537-5544
    • (2008) J. Immunol. , vol.181 , pp. 5537-5544
    • Potempa, M.1    Potempa, J.2    Okroj, M.3    Popadiak, K.4    Eick, S.5    Nguyen, K.A.6    Riesbeck, K.7    Blom, A.M.8
  • 24
    • 84869761067 scopus 로고    scopus 로고
    • Local complement-targeted intervention in periodontitis: Proof-of-concept using a C5a receptor (CD88) antagonist
    • Abe, T., Hosur, K. B., Hajishengallis, E., Reis, E. S., Ricklin, D., Lambris, J. D., and Hajishengallis, G. (2012) Local complement-targeted intervention in periodontitis: proof-of-concept using a C5a receptor (CD88) antagonist. J. Immunol. 189, 5442-5448
    • (2012) J. Immunol. , vol.189 , pp. 5442-5448
    • Abe, T.1    Hosur, K.B.2    Hajishengallis, E.3    Reis, E.S.4    Ricklin, D.5    Lambris, J.D.6    Hajishengallis, G.7
  • 25
    • 0030004180 scopus 로고    scopus 로고
    • Pro-teolytic inactivation of the leukocyte C5a receptor by proteinases derived from Porphyromonas gingivalis
    • Jagels, M. A., Travis, J., Potempa, J., Pike, R., and Hugli, T. E. (1996) Pro-teolytic inactivation of the leukocyte C5a receptor by proteinases derived from Porphyromonas gingivalis. Infect. Immun. 64, 1984-1991
    • (1996) Infect. Immun. , vol.64 , pp. 1984-1991
    • Jagels, M.A.1    Travis, J.2    Potempa, J.3    Pike, R.4    Hugli, T.E.5
  • 26
    • 84868545657 scopus 로고    scopus 로고
    • C5a receptor-dependent cell activation by physiological concentrations of desarginated C5a: Insights from a novel label-free cellular assay
    • Reis, E. S., Chen, H., Sfyroera, G., Monk, P. N., Köhl, J., Ricklin, D., and Lambris, J.D. (2012) C5a receptor-dependent cell activation by physiological concentrations of desarginated C5a: insights from a novel label-free cellular assay. J. Immunol. 189, 4797-4805
    • (2012) J. Immunol. , vol.189 , pp. 4797-4805
    • Reis, E.S.1    Chen, H.2    Sfyroera, G.3    Monk, P.N.4    Köhl, J.5    Ricklin, D.6    Lambris, J.D.7
  • 27
    • 0031910222 scopus 로고    scopus 로고
    • Carboxypeptidase M as a marker of macrophage maturation
    • Krause, S. W., Rehli, M., and Andreesen, R. (1998) Carboxypeptidase M as a marker of macrophage maturation. Immunol. Rev. 161, 119-127
    • (1998) Immunol. Rev. , vol.161 , pp. 119-127
    • Krause, S.W.1    Rehli, M.2    Andreesen, R.3
  • 28
    • 84857922958 scopus 로고    scopus 로고
    • The influence of ACPA status and characteristics on the course of RA
    • Willemze, A., Trouw, L. A., Toes, R. E., and Huizinga, T. W. (2012) The influence of ACPA status and characteristics on the course of RA. Nat. Rev. Rheumatol. 8, 144-152
    • (2012) Nat. Rev. Rheumatol. , vol.8 , pp. 144-152
    • Willemze, A.1    Trouw, L.A.2    Toes, R.E.3    Huizinga, T.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.