A role for calcium in sphingosine 1-phosphate-induced phospholipase D activity in C2C12 myoblasts |
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Authors: | Meacci Elisabetta Becciolini Laura Nuti Francesca Donati Chiara Cencetti Francesca Farnararo Marta Bruni Paola |
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Institution: | Dipartimento di Scienze Biochimiche, Università di Firenze, Viale G.B. Morgagni 50, 50134 Firenze, Italy. |
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Abstract: | Receptor-regulated phospholipase D (PLD) is a key signaling pathway implicated in the control of fundamental biological processes. Here evidence is presented that in addition to protein kinase C (PKC) and Rho GTPases, Ca(2+) response evoked by sphingosine 1-phosphate (S1P) also participates to the enzyme regulation. Ca(2+) was found critical for PKC(alpha)-mediated PLD activation. Moreover, S1P-induced PLD activity resulted diminished by calmodulin inhibitors such as W-7 and CGS9343B implicating its involvement in the process. A plausible candidate for Ca(2+)-dependent PLD regulation by S1P was represented by calcineurin, in view of the observed reduction of the stimulatory effect by cyclosporin A. In contrast, monomeric GTP-binding protein Ral was translocated to membranes by S1P in a Ca(2+)-independent manner, ruling out its possible role in agonist-mediated regulation of PLD. |
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