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Title 

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

Authors 

Jang Hee HongSeo Ok OhMichael LeeYoung Rok KimDong Uk KimGang Min HurJae Heun LeeKyu LimByung Doo HwangSeung Kiel Park

Publisher 

Elsevier

Issue Date 

2001

Citation 

Biochemical and Biophysical Research Communications, vol. 281, no. 5, pp. 1337-1342

Keywords 

phospholipase Dmitogen activated protein kinasephosphatidic acidprotein kinase Clysophosphatidic acidGi protein

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.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1006/bbrc.2001.4517

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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