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Suh, Pann-Ghill
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Phorbol myristate acetate-dependent association of protein kinase C alpha with phospholipase D1 in intact cells

Author(s)
Lee, Taehoon G.Park, Jong BaeLee, Sang DoHong, SeungbumKim, Jae HoKim, YongYi, Kye SookBae, SunsikHannun, Yusuf AObeid, Lina MSuh, Pann-GhillRyu, Sung Ho
Issued Date
1997-08
DOI
10.1016/S0005-2760(97)00083-0
URI
https://scholarworks.unist.ac.kr/handle/201301/16491
Fulltext
http://www.sciencedirect.com/science/article/pii/S0005276097000830#
Citation
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
Publisher
Elsevier BV
ISSN
0005-2760

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