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Reversibility of thrombin-induced decrease in platelet glycoprotein Ib function

H Lu¹, S Menashi, I Garcia

¹INSERM U 353, Hôpital Saint Louis, Paris, France.

British Journal of Haematology

|September 1, 1993

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Thrombin at low concentrations reversibly reduces platelet adhesion by internalizing glycoprotein Ib/IX. Higher concentrations cause irreversible aggregation and degranulation, indicating a dose-dependent effect on platelet function.

Area of Science:

Hematology
Cell Biology
Biochemistry

Background:

Thrombin binding to platelets causes glycoprotein (GP) Ib/GP IX complex redistribution.
This redistribution impairs platelet adhesion to von Willebrand factor (vWF) in the subendothelium.

Purpose of the Study:

To investigate the dose-dependent effects of thrombin on platelet function.
To determine the reversibility of thrombin-induced changes in GP Ib function and localization.

Main Methods:

Assessing platelet aggregation and degranulation.
Measuring GP Ib function using ristocetin-induced platelet agglutination.
Employing immuno-electromicroscopy to visualize GP Ib localization.

Main Results:

Related Experiment Videos

Low thrombin concentrations (<0.04 U/ml) reversibly decreased GP Ib function and caused its translocation to the surface-connected canalicular system (SCCS).
Higher thrombin concentrations (>0.05 U/ml) induced irreversible platelet aggregation and degranulation.
Thrombin inhibitors restored GP Ib function and localization at low thrombin concentrations, but not at high concentrations.

Conclusions:

Thrombin affects platelets in a dose-dependent manner.
Low-dose thrombin-induced reduction in GP Ib function is a reversible phenomenon.
Reversibility is linked to the translocation of GP Ib from the SCCS back to the plasma membrane.