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Cell wall glycoproteins: structure and function.

K Roberts, C Grief, G J Hills

    Journal of Cell Science. Supplement
    |January 1, 1985
    PubMed
    Summary
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    Hydroxyproline-rich glycoproteins are key structural cell wall components in plants and algae. Research reveals their detailed structure, synthesis, and function, particularly volvin in Chlamydomonas reinhardii.

    Area of Science:

    • Plant Biology
    • Cell Biology
    • Biochemistry

    Background:

    • Hydroxyproline-rich glycoproteins (HRGPs) are crucial but poorly understood structural elements in plant cell walls.
    • Similar molecules are found in algae, forming ordered cell surface arrays.

    Purpose of the Study:

    • To review the occurrence, chemistry, synthesis, secretion, cross-linking, and functions of HRGPs in higher plants.
    • To investigate algal cell wall glycoproteins using advanced imaging techniques.
    • To detail the structure and function of volvin, a major HRGP in Chlamydomonas reinhardii.

    Main Methods:

    • High-resolution electron microscopy and computer image reconstruction to model algal cell surface arrays.
    • Chemical and structural analysis of volvin.
    • Monoclonal antibody production for studying volvin's oligosaccharide side-chains.

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  • Immunofluorescence and immunogold labeling to determine synthesis sites and secretion pathways.

    • Main Results:

    • Three-dimensional models of ordered algal cell surface glycoprotein arrays were generated.
    • The structure and chemistry of volvin were elucidated.
    • Antibodies revealed developmental and cell-cycle-dependent regulation of antigenic determinants.
    • Sites of synthesis and secretion of volvin were identified.

    Conclusions:

    • HRGPs play vital structural roles in diverse plant and algal cell walls.
    • Volvin's structure and regulation provide insights into cell wall biogenesis.
    • Understanding HRGPs aids in comprehending cell wall assembly and function, with implications for other glycoproteins like mating agglutinins.