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Related Experiment Videos

Structure and function of platelet glycocalicin

G A Jamieson, T Okumura, M Hasitz

    Thrombosis and Haemostasis
    |February 29, 1980
    PubMed
    Summary

    Platelet glycocalicin, a glycoprotein, inhibits platelet aggregation. Its thrombin-binding activity resides in its peptide tail, suggesting a single class of thrombin binding site on platelets.

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    Area of Science:

    • Biochemistry
    • Hematology
    • Molecular Biology

    Background:

    • Platelet glycocalicin is a major glycoprotein on the platelet surface.
    • Its role in platelet function, particularly aggregation, is of significant interest.

    Purpose of the Study:

    • To review current knowledge on platelet glycocalicin structure and function.
    • To elucidate the specific domains responsible for thrombin binding and inhibition of platelet aggregation.

    Main Methods:

    • Purification of soluble glycocalicin from homogenized platelets.
    • Assays to measure inhibition of thrombin- or ristocetin-induced platelet aggregation.
    • Characterization of thrombin binding activity in relation to glycocalicin structure.
    • Analysis of platelets from patients with Bernard-Soulier disease and chymotrypsin-modified platelets.

    Main Results:

    • Purified glycocalicin inhibits thrombin- and ristocetin-induced platelet aggregation.
    • Thrombin binding activity is localized to the peptide tail (Mr 45,000) of glycocalicin.
    • Glycocalicin is functionally and immunologically identical to membrane-bound glycoprotein I.
    • Thrombin binding is proportional to the amount of glycocalicin/glycoprotein I present in modified platelets and those from Bernard-Soulier patients.

    Conclusions:

    • Platelet glycocalicin plays a crucial role in regulating platelet aggregation.
    • The peptide tail of glycocalicin contains the primary binding site for thrombin.
    • These findings support the existence of a single class of thrombin binding sites on platelets, mediated by glycoprotein I/glycocalicin.

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