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Changes in glycosylation and collagen binding of vitronectin in liver cirrhosis
Background: Vitronectins (VN) are multifunctional adhesive glycoproteins that are present in plasma and the extracellular matrix of most tissues. We previously reported that the collagen-binding activity of VN is enhanced by a change in glycosylation in vitro and during liver regeneration after part...
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Published in: | International Congress series 2001-12, Vol.1223, p.103-107 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Background: Vitronectins (VN) are multifunctional adhesive glycoproteins that are present in plasma and the extracellular matrix of most tissues. We previously reported that the collagen-binding activity of VN is enhanced by a change in glycosylation in vitro and during liver regeneration after partial hepatectomy in vivo [Glycobiology 10 (2000) 865]. To elucidate the glycan modulation, changes of VN in cirrhosis were studied.
Methods: VNs purified from patients' and normal plasma were examined for plasma concentration, reactivities against antibodies and lectins by dot blotting, carbohydrate composition, and collagen-binding activity by ELISA.
Results: Plasma concentrations of VN declined in chronic liver diseases in the order of hepatitis>cirrhosis>hepatocellular carcinoma with cirrhosis. Lectin reactivities and carbohydrate analyses of VN from cirrhotic plasma (LC-VN) indicated that sialylation was elevated. LC-VN exhibited 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.
Conclusions: The attenuated collagen-binding activity of LC-VN is attributable to a change of glycosylation. The increase of active VN in cirrhotic plasma may contribute to the matrix incorporation of VN and subsequent repair or remodeling processes. |
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ISSN: | 0531-5131 1873-6157 |
DOI: | 10.1016/S0531-5131(01)00456-3 |