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

  • Taehoon G. Lee
  • , Jong Bae Park
  • , Sang Do Lee
  • , Seungbum Hong
  • , Jae Ho Kim
  • , Yong Kim
  • , Kye Sook Yi
  • , Sunsik Bae
  • , Yusuf A. Hannun
  • , Lina M. Obeid
  • , Pann Ghill Suh
  • , Sung Ho Ryu
  • Pohang University of Science and Technology
  • Duke University

Research output: Contribution to journalArticlepeer-review

65 Scopus citations

Abstract

A phospholipase D1 (PLD1) was purified from rat brain by the use of antibody-coupled protein A Sepharose. We found that protein kinase Cα (PKCα)) stimulated PLD1 activity in the presence of phorbol myristate acetate (PMA). PMA-dependent association of PKCα 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 PKCα with PLD1.

Original languageEnglish
Pages (from-to)199-204
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume1347
Issue number2-3
DOIs
StatePublished - Aug 16 1997

Keywords

  • Antibody
  • Immunoaffinity-purification
  • Immunoprecipitation
  • Phorbol myristate acetate
  • Phospholipase D1
  • Protein kinase Cα

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