Premium
Receptor‐mediated activation of phospholipase D by sphingosine 1‐phosphate in skeletal muscle C2C12 cells
Author(s) -
Meacci Elisabetta,
Vasta Valeria,
Donati Chiara,
Farnararo Marta,
Bruni Paola
Publication year - 1999
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(99)01033-9
Subject(s) - rottlerin , phospholipase d , pld2 , c2c12 , protein kinase c , skeletal muscle , myocyte , pertussis toxin , microbiology and biotechnology , phospholipase c , sphingosine , chemistry , stimulation , receptor , signal transduction , biology , biochemistry , endocrinology , g protein , phospholipid , membrane , phosphatidylcholine , myogenesis
The present study showed that sphingosine 1‐phosphate (SPP) induced rapid stimulation of phospholipase D (PLD) in skeletal muscle C2C12 cells. The effect was receptor‐mediated since it was fully inhibited by pertussis toxin. All known SPP‐specific receptors, Edg‐1, Edg‐3 and AGR16/H218, resulted to be expressed in C2C12 myoblasts, although at a different extent. SPP‐induced PLD activation did not involve membrane translocation of PLD1 or PLD2 and appeared to be fully dependent on protein kinase C (PKC) catalytic activity. SPP increased membrane association of PKCα, PKCδ and PKCλ, however, only PKCα and PKCδ played a role in PLD activation since low concentrations of GF109203X and rottlerin, a selective inhibitor of PKCδ, prevented PLD stimulation.