| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2005: ¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 2004: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Research Abstract |
Recently, the microdomain on cell surface is considered to be important for cell signaling. In order to investigate the receptor molecules for Helicobacter pylori, this study involved the analysis of adhesion of H.pylori tomicrodomain of a human gastric cancer cell line, KATO III. The microdomain was isolated as low density fractions from the homogenate of KATO III cells by means of sucrose density gradient centrifugation. In the direct adhesion experiment, Helicobacter pylori clearly adhered to the low density fraction, suggesting that the glycosphingolipids contained in the microdomain is involved in the adhesion of the bacteria. Then, we tried to separate the glycolipid. The glycolipids were extracted from the domain, and separated to neutral and acidic gllycolipids by DEAE-Sehadex. The bacteria adhered to the neutral glycolipid fraction strongly, indicating that a part of neutral glycolipids is a candidate for the receptor of Helicobacter pylori. Therefore, we tried to identify the receptor glycolipid.
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