This work reports the functional studies of CHO cells coexpressing -adrenergic (AR) and human fibrinogen (Fg) receptors (integrin IIb3). Stimulation of these cells with -agonists produced a transient rise in the free cytosolic calcium (Ca) accompanied by enhanced binding to soluble Fg, and these effects were prevented by specific AR antagonists. The -adrenergic-induced activation of IIb3 in CHO-IIb3-AR increased the rate of adhesion and extension of cells onto Fg coated plates, and also induced a soluble Fg- and Iib3-dependent formation of cell aggregates, whereas no effects were observed by the stimulation of CHO-IIb3 cells. -Adrenergic antagonists, the ligand mimetic peptide RGDS, pertussis toxin (PTX), or EDTA, they all prevented the -adrenergic stimulation of adhesion and aggregation. However, inhibition of PKC prevented the -adrenergic stimulation of cell adherence, whereas blocking the intracellular Ca mobilization impeded the stimulation of cell aggregation. The -adrenergic activation was associated with phosphorylation of a protein of 100kDa and proteins of the MAPK family. The former was selectively phosphorylated by -adrenergic stimulation whereas the latter were phosphorylated by the binding of cells to Fg and markedly intensified by -adrenergic stimulation.
Print ISSN: 0340-6245
Volume: 92, 12/2004
Pages: 1368 - 1376