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Correlation between fibrinogen binding to human platelets and platelet aggregability.

E I Peerschke, M B Zucker, R A Grant

    Blood
    |May 1, 1980
    PubMed
    Summary

    This study explored how fibrinogen binds to human platelets and how this binding relates to platelet aggregation. Using labeled fibrinogen, the researchers found that the binding is specific and reaches a maximum within one minute. They observed that the number of receptors per platelet is consistent across donors and that binding is affected by pH, chelating agents, and disease states. The study showed that platelets unable to bind fibrinogen could not aggregate with ADP and calcium, even though they could still change shape. These findings suggest a strong link between fibrinogen binding and the ability of platelets to aggregate. The results also highlight the importance of environmental and pathological conditions in this process. The study contributes to a better understanding of platelet function and the role of fibrinogen in both normal and disease states.

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    Area of Science:

    • Platelet biology within hematology
    • Molecular interactions in coagulation research

    Background:

    Platelet aggregation is a key event in hemostasis and thrombosis. It is known that fibrinogen plays a role in this process by bridging platelets. However, the precise relationship between fibrinogen binding and platelet aggregability remained unclear. Prior research has shown that fibrinogen binds to platelets activated by adenosine diphosphate (ADP), but the extent and conditions of this interaction were not fully characterized. The nature of the binding—whether specific or nonspecific—was also uncertain. No prior work had resolved the exact number of receptors per platelet or the impact of pH and chelating agents on this process. This gap motivated a more detailed investigation into the binding characteristics of fibrinogen to human platelets. The study aimed to clarify the conditions under which fibrinogen binds and how this binding relates to platelet aggregation. By addressing these uncertainties, the research contributes to a better understanding of platelet function in both health and disease.

    Purpose Of The Study:

    This study aimed to investigate the binding of fibrinogen to human platelets and its relationship with platelet aggregability. The researchers focused on determining the specificity and saturation of the interaction between fibrinogen and platelets. They also sought to quantify the number of receptors per platelet and assess the influence of various conditions on this binding. The motivation for the study arose from the need to clarify the mechanisms underlying platelet aggregation and the role of fibrinogen in this process. The researchers wanted to understand whether fibrinogen binding is a necessary step for aggregation to occur. By using labeled fibrinogen and different experimental conditions, they aimed to provide a clearer picture of the interaction. The study also aimed to evaluate the impact of pH, chelating agents, and disease states on fibrinogen binding. These findings could help improve the understanding of platelet function in both normal and pathological conditions.

    Keywords:
    Platelet aggregationFibrinogen interactionPlatelet functionCoagulation research

    Frequently Asked Questions

    The study suggests that fibrinogen binding correlates with platelet aggregability, as platelets unable to bind fibrinogen could not aggregate with ADP and CaCl2.

    The researchers tested pH 6.5, EDTA, apyrase, and platelets from patients with thrombasthenia and Bernard-Soulier syndrome.

    125iodine-labeled fibrinogen was used to quantify binding to gel-filtered human platelets under various experimental conditions.

    EDTA caused much of the bound fibrinogen to dissociate from platelets and inhibited binding when present during incubation.

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    Main Methods:

    The researchers used 125iodine-labeled fibrinogen to study its binding to human gel-filtered platelets. They measured the binding at different time points and fibrinogen concentrations. The experiments were conducted with platelets from nine healthy donors to determine the number of receptors per platelet. The researchers tested the effect of pH, chelating agents like EDTA, and apyrase on the binding process. They also included platelets from patients with thrombasthenia and Bernard-Soulier syndrome to assess the impact of these conditions. The binding was quantified by measuring the amount of labeled fibrinogen remaining on the platelets after incubation. The researchers evaluated the dissociation of bound fibrinogen after treatment with apyrase or EDTA. They also examined the ability of platelets to aggregate in the presence of ADP and CaCl2. These methods allowed the team to assess the relationship between fibrinogen binding and platelet aggregability under various conditions.

    Main Results:

    The binding of 125iodine-labeled fibrinogen to platelets reached a maximum within 1 minute. The receptors became saturated when the fibrinogen concentration approached 0.8 mg/ml. The average number of receptors per platelet was 12,896 with a standard deviation of 2,456. Much of the bound fibrinogen dissociated after incubation with apyrase or EDTA. Binding was significantly reduced at pH 6.5 and in the presence of EDTA. Platelets from three thrombasthenic patients showed markedly inhibited binding, but not those from a Bernard-Soulier syndrome patient. Fibrinogen binding was also nearly absent after 8 minutes of incubation with EDTA at 37 degrees C and pH 7.8. Platelets under these conditions could not aggregate with ADP and CaCl2, although they retained the ability to change shape. These results suggest a strong correlation between fibrinogen binding and platelet aggregability. The findings indicate that the binding is specific and influenced by environmental and pathological factors.

    Conclusions:

    The authors propose that the binding of fibrinogen to platelets is a specific and saturable process. The study suggests that this binding is closely related to the platelets' ability to aggregate. The number of receptors per platelet was found to be consistent across nine donors. The results indicate that the binding is affected by pH, chelating agents, and disease states. The study supports the idea that fibrinogen binding is necessary for aggregation to occur. The findings also highlight the importance of calcium and pH in maintaining this interaction. The researchers suggest that the absence of binding under certain conditions correlates with the inability to aggregate. These conclusions are based on the observed effects of various treatments on fibrinogen binding and aggregability. The study contributes to the understanding of platelet function in both normal and pathological states. The results provide insights into the mechanisms underlying platelet aggregation and the role of fibrinogen in this process.

    The average number of receptors per platelet was 12,896 with a standard deviation of 2,456.

    Platelets from thrombasthenic patients showed inhibited fibrinogen binding, while those from Bernard-Soulier syndrome patients did not.