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Glycobiology, 2000, Vol. 10, No. 9 865-874
© 2000 Oxford University Press

The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma

Haruhi Uchibori-Iwaki3, Atsuko Yoneda1,3, Sachie Oda-Tamai4, Shigemi Kato4, Nobu Akamatsu4, Megumi Otsuka5, Kotono Murase6, Kyoko Kojima6, Risa Suzuki6, Yuko Maeya3, Mayumi Tanabe3 and Haruko Ogawa2,3

3Course of Advanced Biosciences, Graduate School of Humanities and Sciences, 4Department of Biochemistry, St. Marianna University School of Medicine, Sugao, Miayamae-ku, Kawasaki, Kanagawa, Japan, 5Department of Nutrition and Food Science and 6Department of Chemistry, Faculty of Sciences, Ochanomizu University, Otsuka, Bunkyo-ku, Tokyo 112–8610, Japan

Vitronectin is a multifunctional glycoprotein present in the extracellular matrix and plasma. Changes in rat vitronectin were studied during liver regeneration after partial hepatectomy. Carbohydrate concentrations of vitronectin decreased to 2/3 of sham-operated rats at 24 h after partial hepatectomy. Carbohydrate composition and lectin reactivity indicated that N-glycosylation and sialylation of vitronectin changed markedly after partial hepatectomy, while amino acid composition did not change significantly. We previously showed that deN-glycosylation of vitronectin in vitro affects collagen binding among various ligands (Yoneda et al., Biochemistry (1998) 37, 6351–6360). Vitronectins from partially hepatectomized rats at 24 h were found to exhibit markedly enhanced binding to type I collagen. The effect of sialylation on collagen binding was further examined using enzymatically deglycosylated vitronectin of nonoperated rats. Collagen binding increased by 1.2 times after deN-glycosylation of vitronectin, while it increased more than 2.9 times after desialylation. Various glycosyltransferases in liver are known to change after partial hepatectomy, including the attenuation of N-oligosaccharide transferase. The findings therefore suggest that the collagen binding of vitronectin is modulated by the alteration of peptide glycosylation caused by postoperative physiological changes of glycosyltransferases and that the change may contribute to tissue remodeling processes.

1 Present address: Biosignaling Department, National Institute of Bioscience and Human Technology, 1–1 Higashi, Tsukuba, Ibaraki, Japan

2 To whom correspondence should be addressed


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