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Annexin V binding to platelets is agonist, time and temperature dependent
Biomedical Diagnostics Institute (BDI) Programme, Molecular & Cellular Therapeutics, Royal College of Surgeons in Ireland (RCSI), Dublin, Ireland.ORCID iD: 0000-0002-1920-3962
Biomedical Diagnostics Institute (BDI) Programme, Molecular & Cellular Therapeutics, Royal College of Surgeons in Ireland (RCSI), Dublin, Ireland.
Biomedical Diagnostics Institute (BDI) Programme, Molecular & Cellular Therapeutics, Royal College of Surgeons in Ireland (RCSI), Dublin, Ireland.ORCID iD: 0000-0001-9862-1398
Biomedical Diagnostics Institute (BDI) Programme, Molecular & Cellular Therapeutics, Royal College of Surgeons in Ireland (RCSI), Dublin, Ireland.ORCID iD: 0000-0001-5548-3263
2010 (English)In: Platelets, ISSN 0953-7104, E-ISSN 1369-1635, Vol. 21, no 4, p. 289-296Article in journal (Refereed) Published
Abstract [en]

Platelets bind annexin V when stimulated with combinations of platelet agonists such as collagen and thrombin. Previous studies have demonstrated significant heterogeneity of platelets binding annexin V. The relative role of the thrombin protease-activated receptors (PARs), PAR1 and PAR4, together with different methods of platelet preparation on annexin V binding to platelets is unclear. We therefore investigated the role of PAR1- and PAR4-activating peptides in combination with collagen-related peptide on annexin V binding. In diluted whole blood, PAR1- and PAR4-activating peptides were as effective as thrombin in inducing annexin V binding. However, in washed platelets, PAR-activating peptides were less potent than thrombin at inducing annexin V binding. This difference was more pronounced when experiments were performed at 37 degrees C compared to room temperature. In studies of diluted whole blood, platelet rich plasma and washed platelets, platelets incubated at room temperature bound more annexin V than platelets incubated at 37 degrees C. We also saw a significant effect of time on annexin V binding, in that more annexin V bound to platelets with longer incubation times. In conclusion, PAR1 and PAR4-activating peptides were as effective as thrombin in inducing annexin V binding in combination with collagen-related peptide in diluted whole blood and platelet rich plasma, but not in washed platelets. In addition, incubation temperature and time has a strong influence on annexin V binding to platelets. Thus variations in these conditions may explain the differences observed between previous studies.

Place, publisher, year, edition, pages
Taylor & Francis, 2010. Vol. 21, no 4, p. 289-296
Keywords [en]
Blood platelets, annexin V, flow cytometry, PAR1, PAR4, GPVI
National Category
Cell Biology
Identifiers
URN: urn:nbn:se:oru:diva-66163DOI: 10.3109/09537101003660564ISI: 000279900800008PubMedID: 20230207Scopus ID: 2-s2.0-77952077218OAI: oai:DiVA.org:oru-66163DiVA, id: diva2:1193412
Available from: 2018-03-26 Created: 2018-03-26 Last updated: 2018-04-05Bibliographically approved

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Ramström, Sofia

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