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Thrombin binding to thrombasthenic platelets.

G C White, E F Workman, R L Lundblad

    The Journal of Laboratory and Clinical Medicine
    |January 1, 1978
    PubMed
    Summary
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    Platelets from Glanzmann's thrombasthenia patients have normal thrombin binding despite altered glycoproteins. This indicates intact thrombin receptors and suggests GPIIb/GPIII are not crucial for thrombin interaction or platelet response.

    Area of Science:

    • Hematology
    • Biochemistry
    • Cell Biology

    Background:

    • Glanzmann's thrombasthenia is a rare bleeding disorder affecting platelet function.
    • Platelet glycoproteins GPIIb and GPIII are critical for aggregation but their role in thrombin binding is unclear.

    Purpose of the Study:

    • To investigate the role of platelet glycoproteins GPIIb and GPIII in alpha-thrombin binding and serotonin release in Glanzmann's thrombasthenia.

    Main Methods:

    • Iodination of platelet surface glycoproteins.
    • Measurement of [125I] alpha-thrombin binding to normal and thrombasthenic platelets.
    • Assay of [14C]serotonin release from stimulated platelets.

    Main Results:

    • Thrombasthenic platelets showed decreased iodination of GPIIb and GPIII but normal alpha-thrombin binding.

    Related Experiment Videos

  • Thrombin binding to thrombasthenic platelets exhibited biphasic kinetics, similar to normal platelets.
  • Serotonin release in response to thrombin was comparable between normal and thrombasthenic platelets.

    • Conclusions:

    • Platelet thrombin receptors are functionally intact in Glanzmann's thrombasthenia.
    • Platelet glycoproteins GPIIb and GPIII are not essential for initial thrombin binding or signal transduction leading to serotonin release.