Enhancement of lysophosphatidic acid-induced ERK phosphorylation by phospholipase D1 via the formation of phosphatidic acid

被引：27

作者：

Hong, JH

Oh, SO

Lee, M

Kim, YR

Kim, DU

Hur, GM

Lee, JH

Lim, K

Hwang, BD

Park, SK

机构：

[1] Chungnam Natl Univ, Coll Med,Sch Med, Dept Biochem, Joong Gu, Taejon 301130, South Korea

[2] Chungnam Natl Univ, Sch Med, Dept Pharmacol, Joong Gu, Taejon 301130, South Korea

[3] Pusan Natl Univ, Sch Med, Dept Physiol, Suh Gu, Pusan 609735, South Korea

[4] Korea Res Inst Biosci & Biotechnol, Taejon, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2001年 / 281卷 / 05期

基金：

新加坡国家研究基金会;

关键词：

phospholipase D; mitogen activated protein kinase; phosphatidic acid; protein kinase C; lysophosphatidic acid; G(i) protein;

D O I：

10.1006/bbrc.2001.4517

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We made stable cell lines overexpressing PLD1 (GP-PLD1) from GP+envAm12 cell, a derivative of NIH 3T3 cell. PLD1 activity and extracellular signal-regulated kinase (ERR) phosphorylation were enhanced in GP-PLD1 cells by the treatment of lysophosphatidic acid (LPA). In contrast, these LPA-induced effects were attenuated with the pretreatment of pertussis toxin (PTX) or protein kinase C (PKC) inhibitor. Moreover, accumulation of phosphatidic acid (PA), a product of PLD action, potentiated the LPA-induced ERR activation in GP-PLD1 cells while blocking of PA production with the treatment of 1-butanol attenuated LPA-induced ERK phosphorylation. From these results, we suggest that LPA activate PLD1 through pertussis toxin-sensitive G protein and PKC dependent pathways, then PA produced from PLD1 activation facilitate ERR phosphorylation. (C) 2001 Academic Press.

引用

页码：1337 / 1342

页数：6

共 27 条

[1] Ras-dependent mitogen-activated protein kinase activation by G protein-coupled receptors - Convergence of G(i)- and G(q)-mediated pathways on calcium/calmodulin, Pyk2, and Src kinase [J].