β-arrestin-1 participates in thrombosis and regulates integrin aIIbβ3 signalling without affecting P2Y receptors desensitisation and function
| Autor: | Schaff, Mathieu, Receveur, Nicolas, Bourdon, Catherine, Ohlmann, Philippe, Lanza, François, Gachet, Christian, Mangin, Pierre Henri |
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| Přispěvatelé: | UMR_S949, Biologie et pharmacologie des plaquettes sanguines: hémostase, thrombose, transfusion, Université de Strasbourg (UNISTRA)-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Strasbourg (UNISTRA)-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Université de Strasbourg (UNISTRA)-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by ARMESA (Association de Recherche et Développement en Médecine et Santé Publique). Mathieu Schaff was supported by a ″Bourse Grenelle″ from the French government. |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Platelets
MESH: Signal Transduction MESH: Carotid Arteries MESH: Microscopy Electron Scanning MESH: Phosphorylation MESH: Mice Transgenic AKT MESH: Mesenteric Arteries MESH: Enzyme-Linked Immunosorbent Assay αIIbβ3 [SDV.BC]Life Sciences [q-bio]/Cellular Biology MESH: Receptors Purinergic P2Y MESH: Platelet Glycoprotein GPIIb-IIIa Complex MESH: Cell Adhesion MESH: Calcium MESH: Fibrinogen MESH: P-Selectin MESH: Animals MESH: Arrestins MESH: Thrombosis MESH: Mice thrombosis MESH: Blood Platelets MESH: Hemorrhage β-arrestins |
| Zdroj: | Thrombosis and Haemostasis Thrombosis and Haemostasis, Schattauer, 2012, 107 (4), pp.735-48. ⟨10.1160/TH11-06-0430⟩ |
| ISSN: | 0340-6245 |
| DOI: | 10.1160/TH11-06-0430⟩ |
| Popis: | International audience; β-arrestin-1 (β-arr1) and β-arrestin-2 (β-arr2) are cytosolic proteins well-known to participate in G protein-coupled receptor desensitisation and signalling. We used genetically-inactivated mice to evaluate the role of β-arr1 or β-arr2 in platelet function, P2Y receptor desensitisation, haemostasis and thrombosis. Platelet aggregation, soluble fibrinogen binding and P-selectin exposure induced by various agonists were near normal in β-arr1-/- and β-arr2-/- platelets. In addition, deficiency in β-arr1 or β-arr2 was not critical for P2Y receptors desensitisation. A functional redundancy between β-arr1 and β-arr2 may explain these unchanged platelet responses. Interestingly, β-arr1-/- but not β-arr2-/- mice were protected against laser- and FeCl3-induced thrombosis. The tail bleeding times, number of rebleeds and volume of blood loss were unchanged in β-arr1-/- and β-arr2-/- mice, suggesting no defect in haemostasis. β-arr1-/- platelet activation upon adhesion to immobilised fibrinogen was inhibited, as attested by a 37 ± 5% (n = 3, p |
| Databáze: | OpenAIRE |
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