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

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Title
Enhancement of lysophosphatidic acid-induced ERK phosphorylation by phospholipase D1 via the formation of phosphatidic acid
Author(s)
Jang Hee Hong; Seo Ok Oh; Michael Lee; Young Rok Kim; Dong Uk Kim; Gang Min Hur; Jae Heun Lee; Kyu Lim; Byung Doo Hwang; Seung Kiel Park
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 281, no. 5, pp. 1337-1342
Publication Year
2001
Abstract
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 (ERK) 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 ERK 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 ERK phosphorylation.
Keyword
Gi proteinphospholipase Dmitogen activated protein kinasephosphatidic acidprotein kinase Clysophosphatidic acid
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1006/bbrc.2001.4517
Type
Article
Appears in Collections:
Division of Biomedical Research > Rare Disease Research Center > 1. Journal Articles
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