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Controling the duration and amplitude of mitogen-activated protein kinase (MAPK) signaling is an important element in deciding cell fate. One group of intracellular negative regulators of MAPK activity is a subfamily of the dual specificity phosphatase (DUSP) superfamily, of which up to 16 members have been described in the ovarian granulosa cells. Growth factors stimulate proliferation of granulosa cells through MAPK, protein kinase C (PKC), and AKT pathways, although it is not known which pathways control DUSP expression in these cells. The aim of the present study was to identify which pathways were involved in the regulation of DUSP expression using a well-established serum-free culture system for bovine granulosa cells. Stimulation of cells with FGF2 increased  DUSP1, DUSP5,  and  DUSP6  mRNA abundance in a time- and dose-dependent manner, and increased DUSP5 and DUSP6 protein accumulation. None of the other eleven DUSP measured were regulated by FGF2. Pharmacological inhibition of MAPK3/1 signaling decreased FGF2-stimulated  DUSP1 ,  DUSP5,  and  DUSP6  mRNA levels ( P   &lt; 0.05), whereas inhibition of PKC did not affect the expression of these three DUSPs. Abundance of FGF2-dependent  DUSP6  mRNA was reduced by inhibition of phospholipase C (PLC) or by chelating calcium, but  DUSP5  mRNA abundance was not affected. Abundance of basal  DUSP1  and  DUSP6 , but not  DUSP5  mRNA was increased by the addition of the calcium ionophore A23187. We conclude that FGF2 stimulation of  DUSP5  abundance requires MAPK3/1 whereas  DUSP6  mRNA accumulation is dependent on calcium signaling as well as MAPK3/1 activation, suggesting complex regulation of physiologically important DUSPs in the follicle.

Regulation of dual specificity phosphatases by fibroblast growth factor signaling pathways in bovine granulosa cells