Structure and Function of Animal Lectin, and Their Role in Biological Regulation.
| Project/Area Number |
60580139
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Teikyo University |
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Principal Investigator |
KASAI Ken-ichi Faculty of Pharmaceutical Sciences, Teikyo University, 薬学部, 教授 (40001052)
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| Co-Investigator(Kenkyū-buntansha) |
HIRABAYASHI Jun Faculty of Pharmaceutical Sciences, Teikyo University, 薬学部, 助手 (40156691)
ODA Yuko Faculty of Pharmaceutical Sciences, Teikyo University, 薬学部, 助手 (30129986)
OHYAMA Yuji Faculty of Pharmaceutical Sciences, Teikyo University, 薬学部, 助手 (90129982)
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| Project Period (FY) |
1985 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1986: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1985: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | Lectin / <beta> -Galactoside / Chick Embryo / Human Placenta / Amino Acid Sequence / Lack of Signal Sequence / Histchemistry / 結合組織 |
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| Research Abstract |
In order to elucidate biological significance of vertebrate <beta> -galactoside-binding lectins, those from chicken, mouse and human were investigated. As to chemical structure, complete amino acid sequence of one of two chick isolectins (14K type) was determined. It proved to be a unique protein because it was difficult to find out significantly homologous sequence in the present data base. Complete sequence of its cDNA was also determined and it was consistent with the amino acid sequence. It was suggested that initiator methionine is removed after biosynthesis and resultant N-terminal is acetylated. The result raised a new question about the mechanism of transportation of the lectin to outside of cells. Partial amino acid sequences were determined on chicken 16K and human placenta lectins. Significant homologies to some parts of chick 14K lectin were found. This suggested strong phylogenic relation between these lectins. In the course of investigation on the distribution of the human lectin, umbilical cord was found to contain relatively large amount of the lectin. Purified preparation showed that placenta and umbilical cord contain the identical lectin. Fluorescent antibody technique showed that the lectin was distributed mainly in connective tissue of umbilical cord. Both normal and tumor tisuues of liver and lung were found to contain large amount of the lectin. Monoclonal antibodies for chick 14K lectin were prepared. One of them seemed to be very useful because it can recognize conformational change of the lectin. As to biological activity of this family of the lectins, human placenta lectin was found to be able to stimulate production of some tumor cell killing factors by mouse and human macrophages.
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Report
(1 results)
Research Products
(12 results)
