2024-03-28T20:36:27Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/728252020-10-20T13:04:10Zcom_10261_86com_10261_1col_10261_339
00925njm 22002777a 4500
dc
Butta, Nora
author
Larrucea, Susana
author
González-Manchón, Consuelo
author
Alonso, Sonia
author
Parrilla, Roberto L.
author
2004-12
This 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
Thrombosis and Haemostasis 92(6):1368-1376(2004)
0340-6245
http://hdl.handle.net/10261/72825
10.1160/TH04-02-0090
α-adrenergic receptors
adhesion receptors/integrins
fibrinogen/ fibrin
gene expression
molecular biology methods
alpha-Adrenergic-mediated activation of human reconstituted fibrinogen receptor (integrin alphaIIbbeta3) in Chinese hamster ovary cells