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Cell binding fragments from a sponge proteoglycan-like aggregation factor.

G N Misevic, J E Jumblatt, M M Burger

    The Journal of Biological Chemistry
    |June 25, 1982
    PubMed
    Summary
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    Marine sponge aggregation factor (MAF) uses distinct sites for cell binding and self-binding. Fragments of MAF retain cell-binding properties, suggesting polyvalent binding sites crucial for species-specific recognition.

    Area of Science:

    • Marine Biology
    • Biochemistry
    • Cellular Recognition

    Background:

    • The marine sponge Microciona prolifera aggregation factor (MAF) is a large proteoglycan.
    • MAF mediates species-specific cell-cell recognition via distinct binding sites.

    Purpose of the Study:

    • To characterize the cell-binding properties of MAF.
    • To investigate the role of MAF fragments in cell aggregation.

    Main Methods:

    • Protease treatment and dissociation procedures were used to generate MAF fragments.
    • Species-specific cell binding assays and MAF-binding assays were performed.

    Main Results:

    • Seven uronic acid-rich glycoprotein fragments of MAF were produced.
    • All fragments retained species-specific cell binding and inhibited MAF-promoted aggregation.

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  • Fragments did not bind to MAF-conjugated agarose beads, indicating they represent the cell-binding site.

    • Conclusions:

    • The cell-binding site of MAF is likely polyvalent, with binding affinity decreasing with fragment size.
    • High valency of binding sites explains MAF's specificity and large size for mediating aggregation.