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A role for calcium in sphingosine 1‐phosphate‐induced phospholipase D activity in C2C12 myoblasts
Author(s) -
Meacci Elisabetta,
Becciolini Laura,
Nuti Francesca,
Donati Chiara,
Cencetti Francesca,
Farnararo Marta,
Bruni Paola
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02866-1
Subject(s) - phospholipase d , microbiology and biotechnology , sphingosine , protein kinase c , chemistry , phospholipase c , signal transduction , rhoa , phospholipase , biochemistry , biology , receptor , enzyme
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 PKCα‐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.