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Related Experiment Videos

Platelet aggregation caused by dithiothreitol.

M B Zucker, N C Masiello

    Thrombosis and Haemostasis
    |February 28, 1984
    PubMed
    Summary
    This summary is machine-generated.

    Dithiothreitol (DTT) aggregates blood platelets by exposing fibrinogen receptors, independent of shape change or secretion. This platelet aggregation is pH-dependent and reversible with EDTA.

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    RENAL HYPERTENSION PRODUCED BY AN AMINO ACID.

    The Journal of experimental medicine·2009

    Area of Science:

    • Hematology
    • Biochemistry
    • Platelet Biology

    Background:

    • Dithiothreitol (DTT) is known to aggregate blood platelets in the presence of fibrinogen.
    • Prostaglandin E1 does not inhibit DTT-induced platelet aggregation.

    Purpose of the Study:

    • To confirm and further investigate the mechanism of DTT-induced platelet aggregation.
    • To elucidate the role of fibrinogen receptors in DTT-mediated platelet activation.

    Main Methods:

    • Platelet aggregation assays with DTT and 2-mercaptoethanol.
    • Assessing platelet shape change, dense granule secretion, and response to inhibitors.
    • Investigating the effect of pH and EDTA on aggregation.
    • SDS-PAGE analysis of platelet proteins and glycoproteins.

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  • Measuring 125I-labeled fibrinogen binding to platelets.

    • Main Results:

    • DTT (over 1 mM) and 2-mercaptoethanol (70 mM) induced platelet aggregation.
    • Aggregation was not linked to shape change or dense granule release.
    • Aggregation was inhibited at pH 6.5 and modulated by EDTA.
    • DTT-induced aggregation was not observed in thrombasthenic, EDTA-treated, or cold platelets.
    • Platelets stimulated with DTT showed increased binding of 125I-labeled fibrinogen.
    • SDS-PAGE revealed DTT reduced specific platelet proteins and glycoproteins (Ib, IIb, III).

    Conclusions:

    • DTT induces platelet aggregation by exposing fibrinogen receptors, not through typical activation pathways.
    • The process involves specific protein alterations and is sensitive to pH and divalent cations.
    • DTT provides a novel tool to study fibrinogen receptor exposure on platelets.