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Related Experiment Videos

Platelet factor XIII is activated by calpain.

Y Ando, S Imamura, Y Yamagata

    Biochemical and Biophysical Research Communications
    |April 14, 1987
    PubMed
    Summary

    Calpain, a calcium-dependent cysteine proteinase, activates platelet factor XIII, a key clotting protein. This action, similar to thrombin, suggests calpain

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    Area of Science:

    • Biochemistry
    • Proteolysis
    • Hemostasis

    Background:

    • Platelet factor XIII (FXIII) is crucial for blood clot stabilization.
    • Calpain is a calcium-dependent cysteine protease involved in various cellular processes.

    Purpose of the Study:

    • To investigate the effect of calpain on the activation of platelet factor XIII.
    • To compare calpain-mediated FXIII activation with thrombin-induced activation.

    Main Methods:

    • Enzymatic assays measuring FXIII activation.
    • Limited proteolysis analysis of the FXIII alpha subunit.
    • Inhibition studies using EDTA, leupeptin, and calpastatin.

    Main Results:

    • Calpain I activated platelet factor XIII to 76% of the maximum level achieved by thrombin.
    • Limited proteolysis of the FXIII alpha subunit by calpain produced a 76 kDa fragment, similar to thrombin's action.
    • Calpain-mediated FXIII activation was inhibited by EDTA, leupeptin, and calpastatin.

    Conclusions:

    • Calpain is capable of activating platelet factor XIII.
    • The findings suggest calpain plays a role in the intracellular activation of platelet factor XIII.
    • Calpain's action on FXIII provides insights into hemostatic regulation.

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