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Basic studies on the biological functions and possibilities of clinical applications of an intestinal IgG Fc binding site.

Research Project

Project/Area Number 04670400
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 内科学一般
Research InstitutionKITASATO INSTITUTE

Principal Investigator

HAMADA Yoshiki  Kitasato Institute Hospital, 病院, 内科医長 (00137994)

Co-Investigator(Kenkyū-buntansha) KOBAYASHI Kensuke  Tokyo Dental Collage Ichikawa Hosp., 市川病院, 内科医長
Project Period (FY) 1992 – 1993
Project Status Completed (Fiscal Year 1993)
Budget Amount *help
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1993: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1992: ¥1,000,000 (Direct Cost: ¥1,000,000)
KeywordsIgG Fc binding site / mucus
Research Abstract

Intestinal mucus is very important in protecting the intestinal mucosa against various harmful antigens, however the mechanisms involved are incompletely defined. Recently, we identified a binding site for the Fc region of IgG(FcIBS) associated with goblet cell mucin in human intestine. We documented that FcIBS could bind antibodies-bacterial complexes. This time we investigated the following biological functions of FcIBS and tried to establish recombinant FcIBS.1) Establishment of recombinant FcIBS : Human colonic epithelium were separated from colonic mucosa. Fraction of mRNA was gained from poly(A) fraction of the colonic epithelia extract. This fraction containing mRNA was injected into the ovum of Xenopus leavis and translated into FcIBS protein. However we could not make cDNA of FcIBS.2) Effect of FcIBS on growth of bacteria : Culture of RDEC-1 both in the presence of anti-RDEC-1 IgG and 10K supernatant of colonic homogenate resulted in a significant reduction of colony number in growth of bacteria. Culture of human pathogenic E.Coli(0111) or Salmonella typhimurium(04) both in the presence of anti-bacterial IgG and 10K supernatant of colonic homogenate has resemble results to that of RDEC-1. These results suggested that FcIBS may play a role in preventing bacteria from attaching to the epithelial surface of the intestine. 3) Inhibition of complement binding by FcIBS : When anti-sheep red blood cells (SRBC) IgG were pre-incubated with affinity-purified FcIBS, the ability of the antibodies to lyse SRBC in the presence of complement was inhibited significantly. These results suggested that FcIBS may interfere the activation of complement and the tissue injury associated with immune complex formation on the epithelium.

Report

(3 results)
  • 1993 Annual Research Report   Final Research Report Summary
  • 1992 Annual Research Report
  • Research Products

    (1 results)

All Other

All Publications (1 results)

  • [Publications] Y.HAMADA: "Tumor necrosis factor-α decrases expression of the interstinal IgG Fc binding Site by HT29-N2 Cells" Immunology. 74. 298-303 (1991)

    • Related Report
      1992 Annual Research Report

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Published: 1992-04-01   Modified: 2016-04-21  

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