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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
Main Authors: Suzuki, Risa, Yamada, Sadako, Uchibori-Iwaki, Haruhi, Oda-Tamai, Sachie, Kato, Shigemi, Akamatsu, Nobu, Yoneda, Atsuko, Ogawa, Haruko
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Language:English
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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.
ISSN:0531-5131
1873-6157
DOI:10.1016/S0531-5131(01)00456-3