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Glycosylation and Ligand-Binding Activities of Rat Plasma Fibronectin During Liver Regeneration After Partial Hepatectomy

Kotone Sano, Miho Asahi, Maiko Yanagibashi, Noritaka Hashii, Satsuki Itoh, Nana Kawasaki, Haruko Ogawa

Carbohydr Res. 2008 Sep 8;343(13):2329-35.

PMID: 18490007

Abstract:

Fibronectin (FN) is a multifunctional glycoprotein present in the extracellular matrix (ECM) and plasma. We previously reported that the glycosylation and ligand-binding of vitronectin (VN) change markedly after partial hepatectomy (PH). Here we show the changes of FN during liver regeneration. The yields of purified sham-operated (SH-) and PH-FN were higher than that of non-operated (NO)-FN, while binding activities of FNs to ECM ligands were changed only slightly by hepatectomy. The carbohydrate concentration of PH-FN decreased to 66% of that of NO- and SH-FN. By using LC/MS(n), eight kinds of complex-type N-glycan structures were found to be present in all FNs, and bi- and trisialobiantennary glycans were the major structures. Fucosylation was markedly increased, while O-acetylation of sialic acid was found to be decreased in PH-FN. The alterations in glycosylation and biological activities of FN after PH are different from those of VN, suggesting that these glycoproteins play different biological functions in tissue remodeling.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP83380829-C Vitronectin from rat plasma Vitronectin from rat plasma 83380-82-9 Price
IAR4241155 Fibronectin rat plasma Fibronectin rat plasma Price
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