Membrane fluidity and platelet aggregation: dibucaine permits ristocetin-induced platelet aggregation with low-molecular-weight von Willebrand multimers
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Updated: Sep 13, 2026

Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells
Published on: October 27, 2009
E Gjønnaess1, N O Solum, F Brosstad
1Research Institute for Internal Medicine, Rikshospitalet, University of Oslo, Norway.
Abstract:
The effects of brief incubation of platelets with dibucaine were studied. Membrane fluidity was increased after incubation with 1 mM dibucaine for 1 min as determined by fluorescence polarization. Platelet aggregation was increased when ristocetin was employed as modulator and normal plasma used as a source of von Willebrand factor (vWF). In contrast, aggregation was decreased with botrocetin. After cryoprecipitation the supernatant, which contained predominantly low-molecular-weight vWF multimers, was effective with ristocetin only after prior incubation of the platelets with dibucaine. This indicates that low-molecular-weight vWF multimers can also support ristocetin-induced aggregation when the membrane fluidity is increased. This idea was supported by the use of plasma from a patient with von Willebrand disease type IIa. Being a multimeric protein, von Willebrand factor contains multiple binding sites for glycoprotein Ib (GP Ib). GP Ib-dependent aggregation by agents that do not contain multiple binding sites, i.e. wheat germ agglutinin or polyclonal antibodies to GP Ib, was decreased after brief incubation with dibucaine. These observations are discussed in relation to the hypothesis that the increased membrane fluidity allows an increased number of GP Ib molecules to bind to each vWF multimer.
Insights
Briefly incubating platelets with dibucaine increases membrane fluidity, enhancing ristocetin-induced aggregation with low-molecular-weight von Willebrand factor (vWF) multimers. This suggests increased fluidity may facilitate more glycoprotein Ib (GP Ib) binding to vWF.
Area of Science:
- Biochemistry
- Hematology
- Cell Biology
Background:
- Platelet function is crucial for hemostasis.
- Von Willebrand factor (vWF) plays a key role in platelet adhesion and aggregation.
- GP Ib is a critical receptor for vWF-mediated platelet interactions.
Purpose of the Study:
- To investigate the impact of altered platelet membrane fluidity on platelet aggregation.
- To explore the role of membrane fluidity in mediating interactions between vWF and GP Ib.
Main Methods:
- Platelet incubation with dibucaine to alter membrane fluidity.
- Measurement of membrane fluidity using fluorescence polarization.
- Assessment of platelet aggregation induced by ristocetin, botrocetin, wheat germ agglutinin, and anti-GP Ib antibodies.
Main Results:
- Dibucaine increased platelet membrane fluidity.
- Ristocetin-induced platelet aggregation was enhanced with low-molecular-weight vWF multimers after dibucaine treatment.
- Botrocetin-induced aggregation was decreased.
- GP Ib-dependent aggregation by wheat germ agglutinin or anti-GP Ib antibodies was reduced.
Conclusions:
- Increased platelet membrane fluidity, induced by dibucaine, facilitates ristocetin-induced aggregation mediated by low-molecular-weight vWF multimers.
- The findings support a model where enhanced membrane fluidity promotes increased binding of GP Ib molecules to vWF multimers.
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