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Related Experiment Videos

Changes in protein glycosylation during chick embryo development.

P Codogno, B Bernard, J Font

    Biochimica Et Biophysica Acta
    |October 25, 1983
    PubMed
    Summary

    Cell-surface glycoproteins undergo significant changes during chick embryo development. Researchers found distinct N-linked and O-linked glycopeptides, with increased sialylation in older embryos, indicating crucial molecular alterations.

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    Area of Science:

    • Developmental Biology
    • Glycobiology
    • Cell Biology

    Background:

    • Cell-surface glycoproteins play vital roles in cellular processes.
    • Understanding molecular changes during embryonic development is crucial for developmental biology.
    • Glycoconjugates are key components of the cell surface.

    Purpose of the Study:

    • To investigate molecular modifications in cell-surface glycoproteins during chick embryo development.
    • To characterize age-related changes in glycopeptide structures and linkages.

    Main Methods:

    • Fibroblasts from 8- and 16-day chick embryos were metabolically and externally labeled.
    • Pronase digestion followed by Sephadex G-50 column chromatography was used to analyze glycopeptides.
    • Enzyme treatments (endo-beta-N-acetylglucosaminidase H) and ratio analysis (mannose-to-galactose, mannose-to-N-acetylglucosamine) were employed.

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    Main Results:

    • Two main glycopeptide classes were identified: glycosaminoglycans and smaller glycopeptides.
    • Younger (8-day) cells primarily had N-linked glycopeptides, while older (16-day) cells had both N-linked and O-linked types.
    • Glycopeptides evolved from high-mannose to complex-type structures, with increased sialylation in older cells.

    Conclusions:

    • Significant quantitative and qualitative changes occur in cell-surface glycoconjugates during late chick embryo development.
    • These findings provide the first biochemical evidence of such modifications.
    • The study highlights the dynamic nature of cell-surface glycoconjugates during embryogenesis.