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Arginine Catabolism and Its Role in Pathogenecity by Periodontopathogenic Bacteria

Research Project

Project/Area Number 12470461
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field 矯正・小児・社会系歯学
Research InstitutionThe University of Tokushima

Principal Investigator

NAKAMURA Ryo  The University of Tokushima, School of Dentistry, Professor, 歯学部, 教授 (30034169)

Co-Investigator(Kenkyū-buntansha) TANABE Shin-ichi  The University of Tokushima, School of Dentistry, Research Associate, 歯学部, 助手 (40284301)
MASUDA Kaname  The University of Tokushima, School of Dentistry, Research Associate, 歯学部, 助手 (30243710)
HINOD daisuke  The University of Tokushima, School of Dentistry, Associate Professor, 歯学部, 助教授 (70189801)
SHIMADA Junko  The University of Tokushima, School of Dentistry, Assistant, 歯学部, 教務員 (10170945)
TAMATANI Kanako  The University of Tokushima, School of Dentistry, Research Associate, 歯学部, 助手 (40243711)
赤木 毅  徳島大学, 歯学部, 助手 (50314878)
Project Period (FY) 2000 – 2002
Project Status Completed (Fiscal Year 2002)
Budget Amount *help
¥12,300,000 (Direct Cost: ¥12,300,000)
Fiscal Year 2002: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 2001: ¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 2000: ¥7,400,000 (Direct Cost: ¥7,400,000)
KeywordsGrowth of Porphyromonas gingivalis / Arginine carboxypeptidase / Arginine deiminase / Energy production / Periodontopathogenicity / 遺伝子解析 / ATP産生 / トリプシン様酵素 / アルギニンデイミナーゼ
Research Abstract

Porphyromonas gingivalis predominantly consumes arginine in the culture medium, suggesting that this amino acid could be the energy source. In relation to the arginine comsuption, cell extracts of P.gingivalis clearly demonstrated enzyme activities for the arginine deiminase pathway and adenosine triphosphate production. The pathogenic properties of this bacterium have been studied extensively in relation to the proteolytic enzyme, especially a trypsin-like enzyme, which splits the bond at the carboxyl side of arginine containing peptide. To obtain free arginine from protein and /or peptide, we performed to elucidate presence and role the arginine carboxypeptidase which cleaves peptide bond at the amino side of arginine. Arginine carboxypeptidase was found in the culture medium and cells. The enzyme was isolated and purified from cytoplasm of P.gingivalis cells. SDS-PAGE of the enzyme revealed the presence of three major bands of 42, 33, and 32kDa, of which 30 amino acid sequences at NH_2-terminal were identical. The ORF, suspected from the nucleotide sequences corresponding to the N-terminal amino acids on the date bases containing unfinished P.gingivalis W83 genome, showed to include signature, suggesting a zinc carboxypeptidase. By Western blotting and immunomicroscopy, the enzyme was found to distribute widely in the cytoplasm and on the surface of the outer membrane of P.gingivalis cells. These results show that this enzyme may function to release arginine in collaboration with a trypsin-like enzyme, to obtain arginine from periodontal tissues in the deep anaerobic pockets during the growth of P.gingivalis. Consequently, these processes might result in the pathogenecity of this bacterium.

Report

(4 results)
  • 2002 Annual Research Report   Final Research Report Summary
  • 2001 Annual Research Report
  • 2000 Annual Research Report
  • Research Products

    (19 results)

All Other

All Publications (19 results)

  • [Publications] Masuda, K., et al.: "Consumption of peptide-derived arginine by periodontopathogenic bacterium, Porphyromonas gingivalis"Anaerobe. 7. 209-217 (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Hinode, D., et al.: "Antigenic properties of the GroEL-like protein of Campyrobacter rectus"Oral Microbiol.Immunol.. 17. 16-21 (2002)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Sugiyama, A., et al.: "Activation of human gingival epithelial cell-surface components of black-pigmented bacteria"J.Med.Microbiol.. 51. 27-33 (2002)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Kaname Masuda et al.: "Purification and Chacterization of Arginine Carboxypeptidase Produced by Porphyromonas gingivalis"Infection and Immunity. 70. 1807-1815 (2002)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Tanabe S., et al.: "Helicobacter pyloli and Campyrobacter rectus share a common antigen"Oral Microbiol.Immunol.. 18(in press). (2003)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Masuda, K. et al.: "Consumption of peptide-derived arginine by a periodontopathogenic bacterium, Porphyromonas gingivalis."Anaerobe. 7. 209-217 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Hinode, D. et al.: "Antigenic properties of the GroEL-like protein of Campyrobacter rectus."Oral Microbiol. Immunol.. 17. 16-21 (2002)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Sugiyama, A., et al.: "Activation of human gingival epithelial cells by cell-surface components of black pigmented bacteria : augmentation od production of interleukin-8, granulocytecolony-stimulating factor and granulocytemacrophage colony-stimulating factor and expression of intercellular adhesion molecule1."J. Med. Microbiol.. 51. 27-33 (2002)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Masuda, K., et al.: "Purification and characterization of arginine carboxypeptidase produced by Porphyromonas gingivalis."Infect. Immuni.. 70. 1807-1815 (2002)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Tanabe, S., et al.: "Helicobacter pylori and Campylobater rectus share a common antigen"Oral Microbiol. Immnol.. 18 (in press). (2003)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Hinode Daisuke et al.: "Antigenic properties of the GroEL-like protein of Campyrobacter rectus"Oral Microbiol. Immunol. 17. 16-21 (2002)

    • Related Report
      2002 Annual Research Report
  • [Publications] Sugiyama Akiko et al.: "Activation of human gingival epithelian cells by cell-surface components of Black pigmented bacteria"J. Med. Microbiol.. 51. 27-33 (2002)

    • Related Report
      2002 Annual Research Report
  • [Publications] Kaname Masuda et al.: "Purification and Chacterization of Arginine Carboxypeptidase Produced by Porphyromonas gingivalis"Infection and Immunity. 70. 1807-1815 (2002)

    • Related Report
      2002 Annual Research Report
  • [Publications] Tanabe Shin-ichi et al.: "Hericobacter pylori and Campyrobacter rectus share a common antigen"Oral Microbiol. Immunol. 18(in press). (2003)

    • Related Report
      2002 Annual Research Report
  • [Publications] Kaname Masuda et al.: "Consumption of peptide-derived arginine by periodontopathogenic bacterium, Porphyromonas gingivallis"Anaerobe. 7. 209-217 (2001)

    • Related Report
      2001 Annual Research Report
  • [Publications] K.Masuda,and 6 others: "Subcellular Localization of Arginine Carboxypeptidase in Porphyromonas gingivalis"J.Dent.Res.. 80(in press). (2001)

    • Related Report
      2000 Annual Research Report
  • [Publications] 横山正明 他6名: "Campylobacter rectus表層抗原物質の性状"口腔衛生学会雑誌. 50. 594-595 (2000)

    • Related Report
      2000 Annual Research Report
  • [Publications] 中村亮 他1名(分担執筆): "歯周病-新しい治療を求めて-、歯周病原細菌の熱ショック蛋白質"医療先端技術研究所. 536 (2000)

    • Related Report
      2000 Annual Research Report
  • [Publications] 中村亮 他4名(分担執筆): "歯科医学と健康の創造(歯界展望/増刊号)、歯周病原細菌由来熱ショックタンパク質の病原性"医歯薬出版. 384 (2000)

    • Related Report
      2000 Annual Research Report

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Published: 2000-04-01   Modified: 2016-04-21  

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