English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/158689
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Título

Human endoglin as a potential new partner involved in platelet–endothelium interactions

AutorRossi, Elisa; Blanco, Francisco J. ; Langa, Carmen ; González-Manchón, Consuelo ; Bernabéu, Carmelo
Palabras claveHHT
Hereditary hemorrhagic telangiectasia
TGF-β
RGD
Preeclampsia
CXCL12
Fecha de publicación28-oct-2017
EditorSpringer
CitaciónCell. Mol. Life Sci. (2017)
ResumenComplex interactions between platelets and activated endothelium occur during the thrombo-inflammatory reaction at sites of vascular injuries and during vascular hemostasis. The endothelial receptor endoglin is involved in inflammation through integrin-mediated leukocyte adhesion and transmigration; and heterozygous mutations in the endoglin gene cause hereditary hemorrhagic telangiectasia type 1. This vascular disease is characterized by a bleeding tendency that is postulated to be a consequence of telangiectasia fragility rather than a platelet defect, since platelets display normal functions in vitro in this condition. Here, we hypothesize that endoglin may act as an adhesion molecule involved in the interaction between endothelial cells and platelets through integrin recognition. We find that the extracellular domain of human endoglin promotes specific platelet adhesion under static conditions and confers resistance of adherent platelets to detachment upon exposure to flow. Also, platelets adhere to confluent endothelial cells in an endoglin-mediated process. Remarkably, Chinese hamster ovary cells ectopically expressing the human αIIbβ3 integrin acquire the capacity to adhere to myoblast transfectants expressing human endoglin, whereas platelets from Glanzmann’s thrombasthenia patients lacking the αIIbβ3 integrin are defective for endoglin-dependent adhesion to endothelial cells. Furthermore, the bleeding time, but not the prothrombin time, is significantly prolonged in endoglin-haplodeficient (Eng+/−) mice compared to Eng+/+ animals. These results suggest a new role for endoglin in αIIbβ3 integrin-mediated adhesion of platelets to the endothelium, and may provide a better understanding on the basic cellular mechanisms involved in hemostasis and thrombo-inflammatory events.
Descripción16 p.-7 fig. Rossi. E. et al.
Versión del editorhttp://dx.doi.org/10.1007/s00018-017-2694-7
URIhttp://hdl.handle.net/10261/158689
DOI10.1007/s00018-017-2694-7
ISSN1420-682X
E-ISSN1420-9071
Aparece en las colecciones: (CIB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
CMLS_Rossi_2017.pdfArtículo principal1,88 MBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.