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Sulfatide-binding proteins.

D D Roberts

    Chemistry and Physics of Lipids
    |December 15, 1986
    PubMed
    Summary
    This summary is machine-generated.

    Cell adhesion proteins specifically bind sulfatides, a type of sulfated glycolipid, with high affinity. This interaction, dependent on glycolipid structure, influences protein binding and cell interactions.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Glycobiology

    Background:

    • Sulfatides and other sulfated glycolipids are prevalent in various tissues.
    • Cell adhesion proteins like laminin, thrombospondin, and von Willebrand factor are known to interact with cell surface molecules.

    Purpose of the Study:

    • To review methods for characterizing the specific binding of cell adhesion proteins to sulfated glycolipids.
    • To investigate the binding characteristics and specificity of laminin, thrombospondin, and von Willebrand factor to sulfatides.

    Main Methods:

    • Utilizing surface-adsorbed glycolipids to assess protein-glycolipid interactions.
    • Characterizing binding specificity by testing against various anionic lipids, including gangliosides, phospholipids, and cholesterol 3-sulfate.
    • Analyzing binding kinetics, including saturation and affinity, and evaluating the impact of oligosaccharide structure on binding avidity.

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    Main Results:

    • Laminin, thrombospondin, and von Willebrand factor exhibit specific binding to sulfatides.
    • These proteins do not bind to other anionic lipids such as gangliosides, phospholipids, or cholesterol 3-sulfate.
    • Binding to sulfatides is saturable and demonstrates relatively high affinity, with avidity influenced by glycolipid oligosaccharide structure.

    Conclusions:

    • The specific binding of cell adhesion proteins to sulfatides is a key interaction.
    • This interaction may explain the hemagglutinating activities of these proteins.
    • The binding to sulfatides on erythrocyte membranes suggests a role in broader cell-cell interactions.