| Project/Area Number |
07680659
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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 |
Structural biochemistry
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| Research Institution | Teikyo University |
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Principal Investigator |
KASAI Ken-ichi Teikyo Univ., Fac.Pharm.Sci., Professor, 薬学部, 教授 (40001052)
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| Co-Investigator(Kenkyū-buntansha) |
ARATA Yoichiro Teikyo Univ., Fac.Pharm.Sci., Assistant Professor, 薬学部, 助手 (90246017)
HIRABAYASHI Jun Teikyo Univ., Fac.Pharm.Sci., Lecturer, 薬学部, 講師 (40156691)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1996: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1995: ¥1,000,000 (Direct Cost: ¥1,000,000)
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| Keywords | Galectin / Neatode / C.elegans / Glycoconjugate / Lectin / ガクレチン / 皮膚 |
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| Research Abstract |
The complete structure of the gene for 32-kDa galection of the nematode Caenorhabditis elegans, which is the firstly found invertebrate galectin, was determined. Only two introns were found. The insertion position of one intron corresponds to those found in the cases of vertebrate galectins, while that of the other was unique. We also found another galectin from C.elegans, which corresponds to the proto type of vertebrates, cloned its cDNA,and determined its whole structure. The finding that both vertebrates and C.elegans have a similar set of galectins strongly suggests the existence of common biological roles that shuould be indespensable for multicellular animals. Since many galectin-like sequences (abou 10) have been found in the genome of C.elegans as a result of the genome project, these sequences were cloned from a cDNA library into an expression vector in order to confirm whether they are functional genes or not. Some sequences were shown to actually encode proteins having sugar-binding ability. It is interesting that C.elegans has as many galectins as mammals do. Glycoproteins as possible candidates for endogenous ligands for galectins have been isolated, and their structural features are now being investigated. Localization of galectins investigated by immunohistochemical technique also indicated the existence of common biological functions between C.elegans and mammals. An efficient analytical procedure based on capillary electrophoresis for comparison of functions of galectins of different origins was also developed in this research project.
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