Study on the nature of amphibian cellinteractions by novel technology
| Project/Area Number |
02454025
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
動物発生・生理学
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| Research Institution | Kyushu University |
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Principal Investigator |
YAMANA Kiyotaka Kyusyu Univ., Fac. of Sci., Professor, 理学部, 教授 (20037162)
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| Co-Investigator(Kenkyū-buntansha) |
NOMURA Kazuya Kyusyu Univ., Fac. of Sci., Assoc. Professor, 理学部, 助教授 (30150395)
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| Project Period (FY) |
1990 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥6,300,000 (Direct Cost: ¥6,300,000)
Fiscal Year 1991: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1990: ¥5,300,000 (Direct Cost: ¥5,300,000)
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| Keywords | Cadherin / Xenopus laevis / Newt / Glycolipid / Lactone / Frog / Glycoprotein / Substratum adhesion molecules / ガングリオシド / イモリ / 細胞接着複合体 |
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| Research Abstract |
What kind of molecules and what kind of interactions are involved in cell adhesion of developing frog embryos? By reverse PCR technique using cadherin consensus sequence primers, we isolated three new frog (Xenopus laevis) cadherin cDNAs and two newt (Cynops pyrrhogaster) cadhrin cDNAs. The entire base sequence of one of the frog cDNA clones was determined. The sequence had some similarity to frog EP-orXB-cadherin, but the sequence difference was apparent. At least five diffrent cadherins were expressed on one frog cell simultaneously. This observeation led us to a hypothesis that the cell adhension is mediated by supramolecular cadherin complexes present on cell surfaces. The DNA sequence was successfully used to design antisense oligonucleotides for antisense knocking out experiments of maternal cadherin mRNAs. By using time resolved streak-camera based fluorometry, we showed that one specific carbohydrate is associated with cadherins on cell surface. Several glycoproteins and glycol
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ipids had the carbohydrates, and this is the first identification of cadherin associated carbohydrate, the expression of which is regulated cell-cycle dependently. The possibility that these carbohydrates are on molecular chaperones for cadherin in being examined in our laboratory. The role of this carbohydrate in cell adhesion is apparent since the monoclinal antibody recognizing this carbohydrate (M4B raised by Prof. C. C. Wylie's group) disrupts Ca^<2+> dependent adhesion of frog blastula cells. We determined the structure of this epitope on neutral glycolipids from frog embryonic or somatic cells. The structure was entirely new, and we are now studying the receptor molecules for the carbohydrates participating Ca^<2+> dependent cell-cell interaction. Eptiope mapping of the monoclinal antibody FAD-II disrupting frog cell-substratum adhesion was also done, and the epitope was also on a neutral glycolipid. The possible roles of neutral glycolipids in cell adhesion are being examined in our laboratory. Less
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Report
(3 results)
Research Products
(5 results)
