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
Citation
Tg. Lee et al., PHORBOL-MYRISTATE ACETATE-DEPENDENT ASSOCIATION OF PROTEIN-KINASE-C-ALPHA WITH PHOSPHOLIPASE D1 IN INTACT-CELLS, Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1347(2-3), 1997, pp. 199-204
Citations number
26
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta, L. Lipids and lipid metabolism → ACNP
ISSN journal
00052760
Volume
1347
Issue
2-3
Year of publication
1997
Pages
199 - 204
Database
ISI
SICI code
0005-2760(1997)1347:2-3<199:PAAOP>2.0.ZU;2-C
Abstract
A phospholipase D1 (PLD1) was purified from rat brain by the use of an tibody-coupled protein A Sepharose. We found that protein kinase C alp ha (PKC alpha) stimulated PLD1 activity in the presence of phorbol myr istate 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.