Structure and function of cell binding domain of fish extracellular matrix components
| Project/Area Number |
10660202
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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 |
Fisheries chemistry
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| Research Institution | Nihon University |
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Principal Investigator |
UCHIDA Naoyuki Nihon University, Collage of Bioresources and Sciences, Department of Marine Science and Resources, Professor, 生物資源科学部, 教授 (80151885)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥4,000,000 (Direct Cost: ¥4,000,000)
Fiscal Year 1999: ¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1998: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | Tilapia / Eel / Japanese catfish / Carp / Hepatocyte / Plasm fibronectin / Collagen / Cell binding domain / ウシ / 繊維芽細胞 |
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| Research Abstract |
1. Japanese catfish hepatocyte (JCHC) which combined with Japanese catfish plasma fibronectin (JCpFN-I) and did not with bovine pFN (BpFN) was compared with eel hepatocyte (EHC) which combined with both pFNs in binding abilities to JCpFN-I, thermolytic fragments of JCpFN-I and BpFN, and subutilisin and pepsin-digested fragments of BpFN. The conclusions to be drawn from these results were as follows. (1) JCpFN-I and BpFN seemed to have individual two cell binding domain, one of them was EHC binding domain with integrin recognition sequence "RGD" and another was JCHC binding domain without RGD sequence. (2) More than two domains seemed to be necessary for successful binding between JCHC and TCpFN-I. (3) Defective binding ability of JCHC to BpFN seemed possible to be caused by the masking of JCHC binding domain in BpFN with a binding inhibition domain.
2. Tilapia hepatocyte (THC) which combined with Tilapia plasma fibronectin (TpFN-I) and did not with carp pFN (CpFN-I) was compared with eel hepatocyte (EHC) which combined with both pFNs in binding abilities to TpFN-I, thermolytic fragments of TpFN-I and CpFN-I, and pronase-digested fragments of CpFN-I. The conclusions to be drawn from these results were as follows. (1) TpFN-I and CpFN-I seemed to have individual two cell binding domain, one of them was EHC binding domain with RGD sequence and another was THC binding domain with RGD sequence. (2) Defective binding ability of THC to CpFN-I seemed possible to be caused by the masking of THC binding domain in CpFN-I with a binding inhibition domain.
3. The cell binding domain with 25 kDa was separated from CB-peptide of carp skin type I collagen. The cell binding domain had a binding ability to carp fin fibroblast with RGD-dependent manner and carp hepatocyte. The amino terminal region (24 residues) consisted of 8 repeats of Gly-X-Y and two residues of Pro. Suggesting that the cell binding domain had loose conformation.
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Report
(3 results)
Research Products
(3 results)
