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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, TGPark, JBLee, SDHong, SKim, JHKim, YYi, KSBae, SHannun, YAObeid, LMSuh, PGRyu, 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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류성호RYU, SUNG HO
Dept of Life Sciences
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