| Project/Area Number |
09670572
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Gastroenterology
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| Research Institution | KITASATO UNIVERSITY |
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Principal Investigator |
HOTTA Kyoko Kitasato University School of Medicine, Professor, 医学部, 教授 (10050402)
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| Co-Investigator(Kenkyū-buntansha) |
KOIZUMI Wasaburou Kitasato University School of Medicine, Assistant Professor, 医学部, 講師 (00195645)
OKAYASU Isao Kitasato University.School of Medicine, Professor, 医学部, 教授 (20014342)
ICHIKAWA Takafumi Kitasato University School of Medicine, Assistant Professor, 医学部, 講師 (30245378)
GOSO Yukinobu Kitasato University School of Medicine, Assistant Professor, 医学部, 講師 (20112659)
ISHIHARA Kazuhiko Kitasato Univ.Sch.Allied Health Sci., Professor, 医療衛生学部, 教授 (10104530)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥2,700,000 (Direct Cost: ¥2,700,000)
Fiscal Year 1998: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1997: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | Helicobacter pylori / Mucus gel / Monoclonal antibody / Gastric mucus / mucin / Gastric mucosa / Dot-blot / ドットブロット |
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| Research Abstract |
The effects of the gastric mucus on Helicobacterpylori (Hp) infection have been studied.
1. The gastric mucins were purified by Lysine-Sepharose chromatography from the gastric juice which were obtained from the individuals having blood group A, B, AB or 0. The inhibition assay by the mucins in the red blood cell agglutination caused by Hp showed that the gastric mucins were potent inhibitor. The results indicated that Np bound to the gastric mucins obtained from the gastric juice. The sialydase treatment of the mucins caused the loss of the binding of the mucins to Hp ; therefore, the sialic acid residue was needed for the binding. The blood type was not correlate with the binding.
2. The gastric mucins were purified from the human gastric mucosa. The methods were authorized from the experiments using the rat gastric mucosa. The purified human gastric mucins were separated to the surface and glandular mucosa-specific mucins using the gel-filtration and ion-exchange chromatography. The dot-blot analysis and ELISA using monoclonal antibody HIK1083 were used to detect the individual mucin. The mucins from the surface mucosa were different from those from the glandular mucosa on their size. Although the complete separation of both mucins have not yet been done, the crude mucins bound to Hp. The mucins from the antrum bound strongly to Hp compared to those from the corpus.
3. The gastric mucins were prepared from the rat and mouse stomach and they were compared to the human mucins on the binding capacity to Hp. The rat or mouse gastric mucins bound only slightly to Hp. The differences of the structure among the mucins have been characterized.
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