Abstract
Lysophosphatidylcholine (lyso-PC), a natural lipid generated through the action of phospholipase A2 on membrane phosphatidylcholine, has been implicated in atherogenesis and the inflammatory process. In vitro studies have established a role for lyso-PC in modulation of gene expression and other cellular responses including differentiation and proliferation. There is also evidence that lyso-PC may act as an intracellular second messenger transducing signals elicited from membrane-associated receptors. The mechanisms behind the diverse activities of lyso-PC are poorly understood. We report, in this study, that treatment of cultured cells with exogenous lyso- PC, at nontoxic concentrations, potently induced activator protein-1 (AP-1) DNA binding and transcriptional activity independent of well known AP-1 activators, protein kinase C or mitogen-activated protein kinases ERK1 and ERK2. Lyso-PC also activated the c-Jun N-terminal kinase (JNK/SAPK), a recently characterized member of the mitogen-activated protein kinase family, known to activate AP-1. The stimulated JNK and AP-1 activities probably mediate or contribute to some bioactive effects of lyso-PC.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 13683-13689 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 272 |
| Issue number | 21 |
| DOIs | |
| State | Published - May 23 1997 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Lysophosphatidylcholine stimulates activator protein 1 and the c-Jun N- terminal kinase activity. / Fang, Xianjun; Gibson, Spencer; Flowers, Michele; Furui, Tatsuro; Bast, Robert C.; Mills, Gordon.
In: Journal of Biological Chemistry, Vol. 272, No. 21, 23.05.1997, p. 13683-13689.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Lysophosphatidylcholine stimulates activator protein 1 and the c-Jun N- terminal kinase activity
AU - Fang, Xianjun
AU - Gibson, Spencer
AU - Flowers, Michele
AU - Furui, Tatsuro
AU - Bast, Robert C.
AU - Mills, Gordon
PY - 1997/5/23
Y1 - 1997/5/23
N2 - Lysophosphatidylcholine (lyso-PC), a natural lipid generated through the action of phospholipase A2 on membrane phosphatidylcholine, has been implicated in atherogenesis and the inflammatory process. In vitro studies have established a role for lyso-PC in modulation of gene expression and other cellular responses including differentiation and proliferation. There is also evidence that lyso-PC may act as an intracellular second messenger transducing signals elicited from membrane-associated receptors. The mechanisms behind the diverse activities of lyso-PC are poorly understood. We report, in this study, that treatment of cultured cells with exogenous lyso- PC, at nontoxic concentrations, potently induced activator protein-1 (AP-1) DNA binding and transcriptional activity independent of well known AP-1 activators, protein kinase C or mitogen-activated protein kinases ERK1 and ERK2. Lyso-PC also activated the c-Jun N-terminal kinase (JNK/SAPK), a recently characterized member of the mitogen-activated protein kinase family, known to activate AP-1. The stimulated JNK and AP-1 activities probably mediate or contribute to some bioactive effects of lyso-PC.
AB - Lysophosphatidylcholine (lyso-PC), a natural lipid generated through the action of phospholipase A2 on membrane phosphatidylcholine, has been implicated in atherogenesis and the inflammatory process. In vitro studies have established a role for lyso-PC in modulation of gene expression and other cellular responses including differentiation and proliferation. There is also evidence that lyso-PC may act as an intracellular second messenger transducing signals elicited from membrane-associated receptors. The mechanisms behind the diverse activities of lyso-PC are poorly understood. We report, in this study, that treatment of cultured cells with exogenous lyso- PC, at nontoxic concentrations, potently induced activator protein-1 (AP-1) DNA binding and transcriptional activity independent of well known AP-1 activators, protein kinase C or mitogen-activated protein kinases ERK1 and ERK2. Lyso-PC also activated the c-Jun N-terminal kinase (JNK/SAPK), a recently characterized member of the mitogen-activated protein kinase family, known to activate AP-1. The stimulated JNK and AP-1 activities probably mediate or contribute to some bioactive effects of lyso-PC.
UR - http://www.scopus.com/inward/record.url?scp=0030959278&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030959278&partnerID=8YFLogxK
U2 - 10.1074/jbc.272.21.13683
DO - 10.1074/jbc.272.21.13683
M3 - Article
C2 - 9153219
AN - SCOPUS:0030959278
VL - 272
SP - 13683
EP - 13689
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 21
ER -