Structure, Function, and Diseases of Fibronectin and Vitronectin
| Project/Area Number |
62490007
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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 |
広領域
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| Research Institution | Ochanomizu University |
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Principal Investigator |
HAYASHI Masao Department of Biology, Ochanomizu University, 理学部, 助教授 (60110516)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥5,500,000 (Direct Cost: ¥5,500,000)
Fiscal Year 1988: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1987: ¥4,500,000 (Direct Cost: ¥4,500,000)
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| Keywords | Vitronectin / Glycoprotein / Blood / Collagen / Monoclonal antibody / Purification / Cell spreading / ドメイン / 細胞接着因子 / 細胞伸展因子 / 糖タクパク質 / 血奨 / 血清 |
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| Research Abstract |
Vitronectin discovered in 1983 is a new plasma glycoprotein, which has been shown to have biological activities concerning cell spreading, blood coagulation, and complement action.
We have investigated the structure and function of vitronectin and the results we have obtained are as follows.
1. We have developed the method to measure vitronectin concentration in human blood immunologically. (1) The concentration of vitronectin in human plasma was remarkably low in the person having liver failures. (2) Human blood samples could be classified into three distinct vitronectin types depending on the ratios of 65 kDa and 75 kDa polypeptides of vitronectin. (3) The vitronection blood type was not related with any deseases tested so far. 2. We have succeeded in purification of vitronectin from plasma or sera of bovine, horse, chicken, porcine, and rabbit with the same new procedure developed for human plasma very recently by us. 3. We have cloned 4 mouse hybridoma producing anti-human vitronection monoclomal antibodies, M1, M2, M4, and M5. Using these monoclonal antibodies, collagen-binding domain of vitronectin was suggested to exist on the N-terminal half of vitronectin molecule. 4. We have purified a few vitronectin fragments cleaved with formic acid. One of these fragments seemed to correspond to the collagen-binding domain.
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Report
(3 results)
Research Products
(23 results)
