A role for calcium in sphingosine 1‐phosphate‐induced phospholipase D activity in C2C12 myoblasts

FEBS Letters

Meacci, Elisabetta¹  Cencetti, Francesca¹  Farnararo, Marta¹  Bruni, Paola¹  Nuti, Francesca¹  Becciolini, Laura¹  Donati, Chiara¹ 

[1] Dipartimento di Scienze Biochimiche, Università di Firenze, Viale G.B. Morgagni 50, 50134 Firenze, Italy

关键词: Sphingosine 1-phosphate;    Phospholipase D;    C2C12 myoblast;    Calcium;    Calmodulin;    Calcineurin;    S1P;    sphingosine 1-phosphate;    PLD;    phospholipase D;    PtdCho;    phosphatidylcholine;    BK;    bradykinin;    PKC;    protein kinase C;    PtdEtOH;    phosphatidylethanol;    AM;    acetoxymethyl ester;    CaM;    calmodulin;   

DOI  :  10.1016/S0014-5793(02)02866-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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, Ca²⁺ response evoked by sphingosine 1-phosphate (S1P) also participates to the enzyme regulation. Ca²⁺ 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 Ca²⁺-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 Ca²⁺-independent manner, ruling out its possible role in agonist-mediated regulation of PLD.

【 授权许可】

Unknown