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1 UMR8619, CNRS, ORSAY, France
* To whom correspondence should be addressed. E-mail: philippe.robin{at}bbmpc.u-psud.fr.
Endothelin-1 (ET-1), platelet-derived growth factor (PDGF) and epidermal growth factor (EGF) stimulated thymidine incorporation with different efficiency (PDGF >> EGF = ET-1) in rat myometrial cells. They also stimulated ERK activation which culminated at 5 min and then decline to reach a plateau (at 45 min: EGF > 90%, PDGF = 50%, ET-1 < 10% of maximum). Inhibition and down regulation of PKC demonstrated that ERK activation at 5 min involved PKC 
and 
for ET-1, and PKC alpha plus another PKC isoform for PDGF. By contrast, the EGF response did not involve PKC. Stimulation of Ras was more important with EGF than with PDGF, ET-1 being the weakest activator. The simultaneous incubation of the cells with EGF and ET-1 potentiated the ERK activation at 5 min and mimicked the plateau phase obtained with PDGF. Under these conditions thymidine incorporation was comparable to that induced by PDGF. Taken together our results indicated that the kinetic profile of ERK activation and its impact on cell proliferation can be modulated by the differential involvement of PKC isoforms and the amplitude of Ras activation.
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