Receptor-mediated activation of phospholipase D by sphingosine 1-phosphate in skeletal muscle C2C12 cells. A role for protein kinase C

FEBS Lett. 1999 Aug 27;457(2):184-8. doi: 10.1016/s0014-5793(99)01033-9.

Abstract

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 PKCalpha, PKCdelta and PKClambda, however, only PKCalpha and PKCdelta played a role in PLD activation since low concentrations of GF109203X and rottlerin, a selective inhibitor of PKCdelta, prevented PLD stimulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Enzyme Activation
  • GTP-Binding Proteins / physiology
  • Isoenzymes / metabolism*
  • Lysophospholipids*
  • Mice
  • Muscle, Skeletal / cytology
  • Muscle, Skeletal / drug effects*
  • Muscle, Skeletal / metabolism
  • Pertussis Toxin
  • Phospholipase D / metabolism*
  • Protein Kinase C / metabolism
  • Sphingosine / analogs & derivatives*
  • Sphingosine / pharmacology
  • Subcellular Fractions
  • Virulence Factors, Bordetella / pharmacology

Substances

  • Isoenzymes
  • Lysophospholipids
  • Virulence Factors, Bordetella
  • sphingosine 1-phosphate
  • Pertussis Toxin
  • Protein Kinase C
  • Phospholipase D
  • GTP-Binding Proteins
  • Sphingosine

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