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Título

Agonist-induced aggregation of Chinese hamster ovary cells coexpressing the human receptors for fibrinogen (integrin alphaIIbbeta3) and the platelet-activating factor: dissociation between adhesion and aggregation

AutorLarrucea, Susana ; González-Manchón, Consuelo ; Butta, Nora ; García Arias-Salgado, Elena ; Shen, Linnan; Sánchez Ayuso, Matilde ; Parrilla, Roberto L.
Fecha de publicación15-abr-2002
EditorAmerican Society of Hematology
CitaciónBlood 99(8):2819-2827(2002)
ResumenThis work reports the establishment of a Chinese hamster ovary (CHO) cell line stably coexpressing the human αIIbβ3 integrin and the platelet-activating factor receptor (PAFR). These cells aggregate in response to PAF in a Ca++, αIIbβ3, and soluble fibrinogen (Fg)–dependent manner that is prevented by PAF antagonists or αIIbβ3 blockade. The aggregating response is accompanied by enhanced binding of fibrinogen and the activation-dependent IgM PAC1. This model has permitted us to identify, for the first time, intracellular signals distinctly associated with either αIIbβ3-mediated adhesion or aggregation. Nonreceptor activation of protein kinase C (PKC) by phorbol ester produced cellular adhesion and spreading onto immobilized Fg, but it was not a sufficient signal to provoke cellular aggregation. Moreover, inhibition of PKC impeded the PAF stimulation of cellular adhesion, whereas the aggregation was not prevented. The PAF-induced cellular aggregation was distinctly associated with signaling events arising from the liganded Fg receptor and the agonist-induced stimulation of a calcium/calmodulin-dependent signaling pathway. Sustained tyrosine phosphorylation of both mitogen-activated protein kinase (MAPK) and an approximately 100-kd protein was associated with the PAF-induced aggregation, whereas phosphorylation of focal adhesion kinase (FAK) was preferably associated with cellular adherence and spreading onto immobilized Fg.
Descripción9 páginas, 10 figuras, 1 tabla -- PAGS nros. 2819-2827
Versión del editorhttp://dx.doi.org/10.1182/blood.V99.8.2819
URIhttp://hdl.handle.net/10261/73588
DOI10.1182/blood.V99.8.2819
ISSN0006-4971
E-ISSN1528-0020
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