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
ISSN1879-145X
AutoresTaehoon 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
ResumoA 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.
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