BIOCHIMICA ET BIOPHYSICA ACTA - LIPIDS AND LIPID METABOLISM, v.1347, no.2-3, pp.199 - 204
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 alpha (PKC alpha) stimulated PLD1 activity in the presence of phorbol myristate acetate (PMA). PMA-dependent association of PKC alpha with PLD1 was verified in NLH-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 PKC alpha with PLD1. (C) 1997 Elsevier Science B.V