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

1997; Elsevier BV; Volume: 1347; Issue: 2-3 Linguagem: Inglês

10.1016/s0005-2760(97)00083-0

ISSN

1879-145X

Autores

Taehoon G. Lee, Jong Bae Park, Sang Do Lee, Seungbum Hong, Jae Ho Kim, Yong Kim, Kye Sook Yi, Sun-Sik Bae, Yusuf A. Hannun, Lina M. Obeid, Pann‐Ghill Suh, Sung Ho Ryu,

Tópico(s)

Metabolism, Diabetes, and Cancer

Resumo

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.

Referência(s)