Acceleration by ceramide of calcium-dependent translocation of phospholipase A2 from cytosol to membranes in platelets

K. Kitatani, T. Oka, T. Murata, M. Hayama, S. Akiba, T. Sato

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


The effect of ceramide on Ca2+-dependent translocation of cytosolic phospholipase A2 (cPLA2) to membranes was studied. Pretreatment of platelets with sphingomyelinase or C6-ceramide (N-hexanoylsphingosine) led to apparent enhancement of Ca2+-ionophore A23187-stimulated arachidonic acid release but did not affect the cytosolic phospholipase A2 (cPLA2) activity. Under these conditions, the cPLA2 proteins in membranes increased significantly, compared with those by A23187 alone. Sphingomyelinase and C6-ceramide, but not C6-dihydroceramide, a control analog of C6-ceramide, also facilitated the Ca2+-dependent increase in the cPLA2 protein, as well as the activity, in membranes induced by addition of Ca2+ into platelet lysate. Protein kinase Cα, which possesses a Ca2+-dependent lipid binding domain, was increased in membranes in a Ca2+-dependent manner, but the increase was not accelerated by sphingomyelinase or C6-ceramide. These findings suggest that ceramide in membranes potentiates Ca2+-dependent cPLA2 translocation from cytosol to membranes, probably through modification of membrane phospholipid organization. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)296-302
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - 2000 Oct 15
Externally publishedYes


  • Ceramide
  • Enzyme translocation
  • Phospholipase A
  • Platelet membrane
  • Sphingomyelinase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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