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Título

alpha-Adrenergic-mediated activation of human reconstituted fibrinogen receptor (integrin alphaIIbbeta3) in Chinese hamster ovary cells

AutorButta, Nora ; Larrucea, Susana ; González-Manchón, Consuelo ; Alonso, Sonia ; Parrilla, Roberto L.
Palabras claveα-adrenergic receptors
adhesion receptors/integrins
fibrinogen/ fibrin
gene expression
molecular biology methods
Fecha de publicacióndic-2004
EditorSchattauer
CitaciónThrombosis and Haemostasis 92(6):1368-1376(2004)
ResumenThis work reports the functional studies of CHO cells coexpressinga-adrenergic (aAR) and human fibrinogen (Fg) receptors(integrin αIibβ3). Stimulation of these cells with a-agonistsproduced a transient rise in the free cytosolic calcium (Ca++)accompanied by enhanced binding to soluble Fg, and theseeffects were prevented by specific aAR antagonists. The a-adrenergic-induced activation of αIibβ3 in CHO-αIibβ3-aARincreased the rate of adhesion and extension of cells onto Fgcoated plates, and also induced a soluble Fg- and αLIIb&abeta;3-dependentformation of cell aggregates, whereas no effects wereobserved by the stimulation of CHO-αIibβ3 cells.a-Adrenergic antagonists, the ligand mimetic peptide RGDS, pertussis toxin(PTX), or EDTA, they all prevented the a-adrenergic stimulationof adhesion and aggregation. However, inhibition of PKCprevented the a-adrenergic stimulation of cell adherence,whereas blocking the intracellular Ca++ mobilization impededthe stimulation of cell aggregation.The α-adrenergic activationwas associated with phosphorylation of a protein of ~100 kDaand proteins of the MAPK family. The former was selectivelyphosphorylated by α-adrenergic stimulation whereas the latterwere phosphorylated by the binding of cells to Fg and markedlyintensified by a-adrenergic stimulation
Descripción9 páginas, 8 figuras -- PAGS nros. 1368-1376
Versión del editorhttp://dx.doi.org/10.1160/TH04-02-0090
URIhttp://hdl.handle.net/10261/72825
DOI10.1160/TH04-02-0090
ISSN0340-6245
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