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Related Experiment Videos

Platelet factor XIII. The collagen receptor?

Y Saito, T Imada, J Takagi

    The Journal of Biological Chemistry
    |January 25, 1986
    PubMed
    Summary

    Platelet Factor XIII, a zymogen form of transglutaminase, may act as the collagen receptor on platelet surfaces. Specific antibodies against it trigger platelet aggregation, suggesting a key role in collagen-induced responses.

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    Area of Science:

    • Biochemistry
    • Hematology
    • Molecular Biology

    Background:

    • Platelet activation by collagen is a critical step in hemostasis and thrombosis.
    • The specific platelet proteins involved in collagen binding and subsequent activation remain incompletely understood.

    Purpose of the Study:

    • To identify platelet proteins that bind to collagen.
    • To investigate the role of identified proteins in collagen-induced platelet aggregation.

    Main Methods:

    • Affinity chromatography using collagen-Sepharose and gelatin-Sepharose.
    • Polyacrylamide gel electrophoresis (PAGE).
    • Immunoprecipitation and enzymic activity assays.

    Main Results:

    • A major platelet protein, identified as platelet Factor XIII (a zymogen transglutaminase), did not bind to denatured collagen (gelatin).
    • Specific immunoglobulins against platelet Factor XIII induced platelet aggregation independently, requiring Ca2+ and inhibited by aspirin and prostacyclin.

    Conclusions:

    • The zymogen form of platelet Factor XIII may be surface-localized and function as a collagen receptor.
    • Platelet Factor XIII plays a significant role in collagen-induced platelet aggregation.

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