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Change in glycosylation of chicken transferrin glycans biosynthesized during embryogenesis and primary culture of embryo hepatocytes

1994; Oxford University Press; Volume: 4; Issue: 5 Linguagem: Inglês

10.1093/glycob/4.5.617

1460-2423

Pierre-Marie Jacquinot, Didier Leger, Jean-Miche Wieruszeski, Bernadette Coddeville, Jean Montreuil, Geneviève Spik,

Animal Genetics and Reproduction

Transferrins were isolated by immunoaffinity chromato-graphy from chicken serum, chicken embryo serum and from the culture medium of chicken embryo hepatocytes in primary culture. The glycovariants of these three transferrins were separated by ion-exchange chromatography using a fast protein liquid chromatography (FPLC) system. The structures of the oligosaccharide-alditols released by hydrazinolysis from the glycovariants were compared after analysis by a combination of methanolysis, methylatlon analysis and 1H-NMR spectroscopy. In the three transferrins analysed, the oligosaccharides were of the bian-tennary N-acetyllactosaminic type, having several prominent features. In particular, the embryo serum transferrin glycan differed from that of chicken serum transferrin by the presence of a bisecting N-acetylglucosamine, suggesting a developmental change in glycosylation. The glycan structure of the transferrin secreted by the embryo hepatocytes in primary culture was marked by the presence of fucose (αl-6) linked to the core N-acetylglucosamine, suggesting that expression of the fucosyltransferase activity is dependent on cell culture conditions. Moreover, comparative analysis of chicken serum transferrin and ovotransferrin glycans reinforces the idea that the glycosylation of two identical poly-peptide chains is organ specific.