Glycosylation and ligand-binding activities of rat plasma fibronectin during liver regeneration after partial hepatectomy.
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.
Sano
Kotone
K
Graduate School of Humanities and Sciences, Ochanomizu University, 2-1-1 Otsuka, Bunkyo-ku, Tokyo 112-8610, Japan.
Asahi
Miho
M
Yanagibashi
Maiko
M
Hashii
Noritaka
N
Itoh
Satsuki
S
Kawasaki
Nana
N
Ogawa
Haruko
H
D000818:Animals; D002468:Cell Physiological Phenomena; D004305:Dose-Response Relationship, Drug; D005109:Extracellular Matrix / Q000378:metabolism; D005353:Fibronectins / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry; D006031:Glycosylation; D006498:Hepatectomy / Q000379:methods*; D008024:Ligands; D008107:Liver Diseases / Q000378:metabolism; D008115:Liver Regeneration; D019158:N-Acetylneuraminic Acid / Q000737:chemistry; D011485:Protein Binding; D051381:Rats; D019096:Vitronectin / Q000737:chemistry
D005353:Fibronectins; D006023:Glycoproteins; D008024:Ligands; D019096:Vitronectin; D019158:N-Acetylneuraminic Acid