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Quantitation of microparticles released from coated-platelets.

G L Dale1, G Remenyi, P Friese

  • 1Department of Medicine, W.K. Warren Medical Research Institute, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. george-dale@ouhsc.edu

Journal of Thrombosis and Haemostasis : JTH
|August 17, 2005
PubMed
Summary

Dual agonist stimulation of platelets generates coated-platelets that release microparticles. These microparticles express specific surface markers and their release is enhanced by compounds affecting the mitochondrial permeability transition pore.

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Area of Science:

  • Hematology
  • Cell Biology
  • Biochemistry

Background:

  • Coated-platelets are a sub-population of platelets generated by dual stimulation with thrombin and convulxin.
  • These cells retain procoagulant proteins and express phosphatidylserine (PS).

Purpose of the Study:

  • To investigate the release of microparticles from coated-platelets using a novel methodology.
  • To characterize the surface markers and release kinetics of these microparticles.

Main Methods:

  • Platelets were labeled with Bodipy-maleimide and stimulated with convulxin plus thrombin.
  • Fluorescence confocal microscopy and flow cytometry were employed to detect and quantify microparticles.
  • Analysis included assessing surface markers like glycoprotein IIb/IIIa, glycoprotein Ib, CD9, and PS.

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Main Results:

  • Dual agonist stimulation (thrombin and convulxin) induced the release of microparticles (0.3-0.5 microm) from coated-platelets.
  • Microparticles were positive for glycoprotein IIb/IIIa, glycoprotein Ib, CD9, and PS, but negative for fibrinogen and thrombospondin.
  • Activation produced significantly more microparticles (15 +/- 5 per coated-platelet) compared to single agonist stimulation. Phenylarsine oxide and diamide enhanced microparticle release.

Conclusions:

  • Coated-platelets, generated by dual agonist stimulation, release phosphatidylserine-exposing microparticles.
  • The release of these microparticles is dependent on dual activation and can be modulated by agents affecting the mitochondrial permeability transition pore.