Stimulation of protein kinase C (PKC) activity in resting Swiss 3T3 cells by prostaglandin F2α

Prostaglandin F2α (PGF2α), a mitogen for resting Swiss 3T3 cells, rapidly stimulates phosphorylation of an 80 kDa protein (80 K). 1-Oleoyl-2-acetylglycerol (OAG) and 12-O-tetradecanoyl phorbol-13-acetate (TPA) both protein kinase C (PKC) activators, also elicit 80 K phosphorylation. In contrast PGE1...

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Detalles Bibliográficos
Publicado: 1992
Materias:
DNA
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v297_n1-2_p175_Goin
http://hdl.handle.net/20.500.12110/paper_00145793_v297_n1-2_p175_Goin
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Sumario:Prostaglandin F2α (PGF2α), a mitogen for resting Swiss 3T3 cells, rapidly stimulates phosphorylation of an 80 kDa protein (80 K). 1-Oleoyl-2-acetylglycerol (OAG) and 12-O-tetradecanoyl phorbol-13-acetate (TPA) both protein kinase C (PKC) activators, also elicit 80 K phosphorylation. In contrast PGE1, PGE2 or PGF2β, which are non-mitogenic in these cells, had tittle or no action on this event. However PGE1 and PGE2 potentiate the PGF2α proliferative effect but do not enhance its action on 80 K phosphorylation. These results suggest that PGF2α mitogenic induction involves PKC signalling pathway activation while its enhancement by PGE1 or PGE2 occurs through a different mechanism(s). © 1992.