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Related Experiment Videos

Diglyceryl lipase activity in mouse platelets.

R C Franson, W I Rosenblum

    Thrombosis Research
    |November 15, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Mouse platelets exhibit significant diglyceryl lipase (DGL) activity, exceeding that of human or rat platelets. This enzyme activity in mouse platelets was notably inhibited by RHC80267.

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    Area of Science:

    • Biochemistry
    • Platelet Biology
    • Enzymology

    Background:

    • Platelets play crucial roles in hemostasis and thrombosis.
    • Diglyceryl lipase (DGL) is an enzyme involved in lipid metabolism.
    • Understanding DGL activity in different species' platelets is important for comparative physiology.

    Purpose of the Study:

    • To investigate and quantify the diglyceryl lipase (DGL) activity in mouse platelets.
    • To compare DGL activity in mouse platelets with that of human and rat platelets.
    • To assess the effect of RHC80267 on DGL activity in mouse platelets.

    Main Methods:

    • Enzyme activity assays were performed on isolated platelets from mice, humans, and rats.
    • Quantification of diglyceryl lipase (DGL) activity was measured in nanomoles per hour per 10(9) platelets.

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  • The effect of the inhibitor RHC80267 on DGL activity was evaluated in mouse platelets.

    • Main Results:

    • Mouse platelets demonstrated substantial DGL activity (138 +/- 29 nmols/hr/10(9) platelets).
    • Human platelets showed lower DGL activity (37 +/- 56 nmols/hr/10(9) platelets), and rat platelets had minimal activity (25 +/- 11 nmols/hr/10(9) platelets).
    • RHC80267 significantly inhibited DGL activity in mouse platelets, consistent with its known effects in other species.

    Conclusions:

    • Mouse platelets possess significantly higher diglyceryl lipase (DGL) activity compared to human and rat platelets.
    • The findings confirm the presence of DGL in rat platelets, contrary to previous reports.
    • RHC80267 effectively inhibits DGL activity in mouse platelets, suggesting conserved inhibitory mechanisms across species.