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2003 Fiscal Year Final Research Report Summary

Inhibitory effect of human α_2-plasmin inhibitor and it's intensified compound by S-nitrosylation on the activity of arginine-specific cysteine proteinase from Porphyromonas gingivalis.

Research Project

Project/Area Number 13671931
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Morphological basic dentistry
Research InstitutionFukuoka Dental College

Principal Investigator

KAMINISHI Hidenori  Fukuoka Dental College, Infection Biology, Professor, 歯学部, 教授 (90084300)

Co-Investigator(Kenkyū-buntansha) AKAIKE Takaaki  Kumamoto University, Medical Microbiology, Professor, 医学部, 助教授 (20231798)
TAKEUCHI Hisako  Fukuoka Dental College, Infection Biology, Research Assistant, 歯学部, 助手 (50198800)
OGURA Rieko  Fukuoka Dental College, Infection Biology, Research Assistant, 歯学部, 助手 (80320331)
HAMAMOTO Takayoshi  The Chemo-Sero-Therapeutic Research Institute, Research Fellow, 研究員
Project Period (FY) 2001 – 2003
KeywordsP. gingivalis / gingipain / α_2-plasmin inhibitor / S-nitrosylation / α2アンチプラスミン / α1プロテアーゼインヒビター / ベジクル
Research Abstract

We investigated the effect of human α_2-plasmin inhibitor (α_2PI) and S-nitrosylated α_2-plasmin inhibitor (S-NO-α_2PI) on the activity of arginine-specific cysteine proteinase (gingipain, RGP) from Porphyromonas gingivalis, an aetiological bacterium of adult periodontitis, with the use of fluorogenic substrates. We discovered that human α_2PI as well as S-NO-α_2PI play a inhibitory effect to the RGP in a dose-dependent manner. The α_2PI, one of the members of serpin family, is well known as a specific inhibitor of plasmin, a typical serine proteinase. However, few studies have been reported concerning the inhibitory potency of humoral factors, such as α_1-protease inhibitor or α_2-macroglobulin, against cysteine proteinases especially RGP. In this study, we found a novel function of α_2PI as a potent inhibitor of RGP. The inhibitory potencies of the S-nitrosylated derivative against both human plasmin and RGP were slightly higher than those of the intact α_2PI. These results strongly suggest that S-NO-α_2PI is a useful tool for preventing the virulence of P. gingivalis.

  • Research Products

    (5 results)

All Other

All Publications (5 results)

  • [Publications] 上西秀則, 小倉理恵子 ほか: "α_2プラスミンインヒビターおよびそのニトロソ化物はPorphyromonas gingivalisプロテアーゼの活性を阻害する"医学と生物学. 148. 27-31 (2004)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] 上西秀則, 長 環, 小倉理恵子: "真菌の遺伝学"日本臨牀. 61. 785-792 (2003)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Inoue Y, Fukushima T., et al.: "Antibacterial characteristics of newly developed amphiphilic lipids and DNA-lipid complexes against bacteria."J.Biomed.Mater.Res.. 65A. 203-208 (2003)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Cho T., Toyoda M., et al.: "Isolation and sequencing of the Candida albicans MSI3, a putative novel member of the HSP7O family."Yeast. 20. 149-156 (2002)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Hidenori KAMINISHI, Rieko OGURA, Mika TOYODA, Tamaki CHO, Takayoshi HAMAMOTO: "Inhibitory Effect of Human α_2-Plasmin Inhibitor and It's S-Nitrosylated Derivative on the Activity of Arginine-Specific Cysteine Proteinase from Porphyromonas gingivalis."Medicine and Biology. 148,(6). 27-31 (2004)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2005-04-19  

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