Phorbol myristate acetate-dependent association of protein kinase C alpha with phospholipase D1 in intact cells

Biochim Biophys Acta. 1997 Aug 16;1347(2-3):199-204. doi: 10.1016/s0005-2760(97)00083-0.

Abstract

A phospholipase D1 (PLD1) was purified from rat brain by the use of antibody-coupled protein A Sepharose. We found that protein kinase C alp (PKCalpha) stimulated PLD1 activity in the presence of phorbol myristate acetate (PMA). PMA-dependent association of PKCalpha with PLD1 was verified in NIH-3T3 fibroblast cells, and COS7 cells transiently expressing PLD1 as well as in vitro suggesting that the activation of PLD1 resulted from direct association of PKCalpha with PLD1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Animals
  • Brain / enzymology
  • COS Cells
  • Enzyme Activation
  • Mice
  • Phospholipase D / isolation & purification
  • Phospholipase D / metabolism*
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Tetradecanoylphorbol Acetate / pharmacology*

Substances

  • Protein Kinase C
  • Phospholipase D
  • phospholipase D1
  • Tetradecanoylphorbol Acetate