Changes in protein glycosylation during chick embryo development |
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Authors: | Patrice Codogno Bruno Bernard Jacqueline Font Michèle Aubery |
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Affiliation: | Laboratoire de Biologie et Pathologie Moléculaires des Glycoprotéines, U 180 INSERM, UER Biomédicale des Saints Pères, 45, rue des Saints Pères, 75006 Paris France |
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Abstract: | To investigate the molecular changes in cell-surface glycoproteins during chick embryo development, fibroblasts from 8- and 16-day embryos were extensively digested by pronase after (i) metabolic labeling with radioactive precursors and (ii) external labeling. Two main classes of glycopeptide pronase digestion product were distinguished by Sephadex G-50 column chromatography. The large material excluded was mostly composed of glycosaminoglycans. The small retarded glycopeptides underwent age-related modifications. Those in the 8-day cells were mainly N-linked, whereas 16-day cells contained both O- and N-linked glycopeptides. The evolution of high-mannose chains in younger cells to complex-type chains in the older cells is suggested by (i) the decrease in the mannose-to-galactose and mannose-to-N-acetylglucosamine ratio with embryo development, and (ii) the fact that endo-β-N-acetylglucosaminidase H treatment released more oligomannosyls from younger than from older embryo cell glycopeptides. Small glycopeptides were also more highly sialylated in 16-day cells than in 8-day cells. The present results provide the first biochemical evidence that both quantitative and qualitative modifications occur in cell-surface glycoconjugates during the late stages of chick embryo development. |
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Keywords: | Protein glycosylation Development Glycoconjugate (Chick embryo) |
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