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The nucleotide uridine trisphosphate (UTP) released to the extracellular milieu acts as a signaling molecule  via  activation of specific pyrimidine receptors (P2Y). P2Y receptors are G protein-coupled receptors expressed in many cell types. These receptors mediate several cell responses and they are involved in intracellular calcium mobilization. We investigated the role of the prostanoid PGE 2  in P2Y signaling in mouse embryonic fibroblasts (MEFs), since these cells are involved in different ontogenic and physiopathological processes, among them is tissue repair following proinflammatory activation. Interestingly, Ca 2+ -mobilization induced by UTP-dependent P2Y activation was reduced by PGE 2  when this prostanoid was produced by MEFs transfected with COX-2 or when PGE 2  was added exogenously to the culture medium. This Ca 2+ -mobilization was important for the activation of different metabolic pathways in fibroblasts. Moreover, inhibition of COX-2 with selective coxibs prevented UTP-dependent P2Y activation in these cells. The inhibition of P2Y responses by PGE 2  involves the activation of PKCs and PKD, a response that can be suppressed after pharmacological inhibition of these protein kinases. In addition to this, PGE 2  reduces the fibroblast migration induced by P2Y-agonists such as UTP. Taken together, these data demonstrate that PGE 2  is involved in the regulation of P2Y signaling in these cells.

mediators of inflammation

Sustained Release of Prostaglandin E2in Fibroblasts Expressing Ectopically Cyclooxygenase 2 Impairs P2Y-Dependent Ca2+-Mobilization