Regulation mechanism of tissue remodeling by gloycosylation change-Functional modulation of extracellular matrix molecule, vitronectin, by its glycosylation change
| Project/Area Number |
12680607
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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 | Ochanomizu University |
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Principal Investigator |
OGAWA Haruko Ochanomizu University, Graduate School, Associate Professor, 大学院・人間文化研究科, 助教授 (90143700)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2001: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2000: ¥2,800,000 (Direct Cost: ¥2,800,000)
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| Keywords | vitronectin / collagen / extracellular matrix / tissue remodeling / multimerization / ultracellular matrix / glycosylation / cirrhosis |
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| Research Abstract |
Vitronectin (VN), a multifunctional glycoprotein present in the extracellular matrix and plasma, plays a role in cell adhesion, cellular motility and matrix remodeling. Some of these binding activities are affected by changes in glycosylation of VN and collagen-binding activity is enhanced by decreased glycosylation of VN during liver regeneration after a partial hepatectomy. In this study, the activating mechanism of vitronectin by its glycosylation and biological significance of it was studied.
The effect of glycosylation on multimerization of VN was studied by analytical untracentrifugation to elucidate the modulation mechanism of the biological activity by glycans. Sedimentation velocity analysis at pH 4.5, an optimum pH for collagen binding, indicated that multimerization of VN was more remarkable than that at pH 7.5. Neuraminidase-treated VN formed a multimer larger than that of VN incubated without the enzyme. N-glycanase treatment gradually increased the size of the VN multimer.
… More
The stability of VN multimer against the denaturing agent was measured by sedimentation equilibrium analyzes at various concentrations of guanidine-HCl. The neuraminidase-treated or N-glycanase-treated VN remained in a multimer form at a guanidine-HCl concentration in which control VN dissociate*! Into monomers, enhancing thus the multimer stability of deglycosylated VNs. These results suggest that deglycosylated VN increased the size and stability of the multimer to eventually enhance the collagen binding activity by multivalent effect.
On the other hand, changes of VN in cirrhotic plasma (LC-VN) indicated that sialylation was elevated. LCVN to exhibit decreased binding to type I collagen. Collagen-binding studies of plasma before and after urea-treatment indicated that the active form of VN increased in cirrhotic plasma. These changes indicate the glycosylation changes of LC-VN and the increase of active VN in cirrhotic plasma may contribute to the matrix incorporation of VN and subsequent repair or remodeling processes. Less
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Report
(3 results)
Research Products
(24 results)
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[Publications] Suzuki, R., Yamada, S., Uchibori-Iwaki, H., Oda-Tamai, S., Kato, S. Akamatsu., N., Yoneda, A., and Ogawa, H.: "Changes in glycosylation and collagen binding of witronection in liver cirrhosis"New Develop in Glycomedicine ICS. 1223H. 103-107 (2001)
Description
「研究成果報告書概要(欧文)」より
Related Report
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[Publications] Uchibori-Iwaki, H., Yoneda, A., Oda-Tamai, S., Kato, S., Akamatsu, N., Otsuka, M., Murase, K., Kojima, K., Suzuki, R., Maeya, Y., and Ogawa, H.: "The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma"Glycobiology. 10. 865-874 (2000)
Description
「研究成果報告書概要(欧文)」より
Related Report
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