Phorbol myristate acetate-dependent association of protein kinase C alpha with phospholipase D1 in intact cells
SCIE
SCOPUS
- Title
- Phorbol myristate acetate-dependent association of protein kinase C alpha with phospholipase D1 in intact cells
- Authors
- Lee, TG; Park, JB; Lee, SD; Hong, S; Kim, JH; Kim, Y; Yi, KS; Bae, S; Hannun, YA; Obeid, LM; Suh, PG; Ryu, SH
- Date Issued
- 1997-08-16
- Publisher
- ELSEVIER SCIENCE BV
- 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.
- Keywords
- phospholipase D1; protein kinase C alpha; antibody; immunoaffinity-purification; phorbol myristate acetate; immunoprecipitation; ADP-RIBOSYLATION FACTOR; GTP-BINDING PROTEIN; SIGNAL-TRANSDUCTION; ACTIVATION; RHOA; MEMBRANE; RAT; GRANULOCYTES; HYDROLYSIS; ISOZYMES
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/21237
- DOI
- 10.1016/S0005-2760(97)00083-0
- ISSN
- 0005-2760
- Article Type
- Article
- Citation
- BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM, vol. 1347, no. 2-3, page. 199 - 204, 1997-08-16
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