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Related Experiment Video

Updated: Mar 12, 2026

Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets
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A Flow Cytometry-Based Assay for Procoagulant Platelet Polyphosphate.

Linda Labberton1,2, Andy T Long2, Sandra J Gendler3

  • 1Clinical Chemistry, Department of Molecular Medicine and Surgery, Karolinska Institutet and University Hospital, Stockholm, Sweden.

Cytometry. Part B, Clinical Cytometry
|November 5, 2016
PubMed
Summary
This summary is machine-generated.

We developed a new assay to measure polyphosphate on activated human platelets. This assay shows that long-chain polyphosphate binds to platelet surfaces, offering potential for thrombosis biomarker development.

Keywords:
biomarkerflow cytometryplateletspolyphosphate

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Area of Science:

  • Biochemistry
  • Hematology
  • Cell Biology

Background:

  • Platelet polyphosphate is an inorganic polymer released from dense granules upon platelet activation.
  • It plays a role in blood coagulation.
  • Measuring polyphosphate on platelet surfaces is crucial for understanding its function.

Purpose of the Study:

  • To develop and validate an assay for measuring polyphosphate on the surface of procoagulant human platelets.
  • To investigate the binding characteristics of different chain lengths of polyphosphate to platelets.
  • To assess the impact of platelet activation on surface polyphosphate levels.

Main Methods:

  • Utilized a fluorescently labeled exopolyphosphatase deletion mutant (PPX_Δ12-Alexa488) as a polyphosphate probe.
  • Employed flow cytometry to quantify PPX_Δ12-Alexa488 binding to platelets.
  • Stimulated platelets with thrombin receptor agonist (Trap6) and ADP to induce activation and polyphosphate release.

Main Results:

  • PPX_Δ12-Alexa488 signal increased dose-dependently with long-chain polyphosphate binding to platelets.
  • Short-chain polyphosphate in the supernatant did not bind to the platelet surface.
  • Platelet activation with Trap6 and ADP led to increased surface polyphosphate accumulation and a higher PPX_Δ12-Alexa488 signal.

Conclusions:

  • Long-chain polyphosphate binds to platelet plasma membranes.
  • The developed assay is a promising tool for measuring polyphosphate-platelet interactions in platelet-rich plasma.
  • Further research is warranted to explore polyphosphate as a potential biomarker for thrombosis.