Abstract |
Lysophosphatidic acid (LPA) and endothelin-1 (ET-1), two ligands for G-protein coupled receptors (GPCRs), induce activation of mitogen activated protein kinase (MAPK). Surprisingly, LPA and ET-1 did not induce MAPK activation in SK-N-MC neuroepithelioma cells, even though these GPCR ligands evoked a rapid, transient rise in intracellular free Ca2+ concentration in these cells, indicating that SK-N-MC cells express functional LPA- and ET-1-receptors. Transient transfection of the EGFR into SK-N-MC cells, which do not express endogenous EGFR, potentiated LPA- and ET-1-induced MAPK activation. LPA and ET-1 did not enhance basal level tyrosine phosphorylation of the transfected EGFR in SK-N-MC cells. Even though the mechanism of LPA- and ET-1-induced MAPK activation in EGFR-transfected SK-N-MC cells remains to be determined definitively, our results provide strong evidence that the EGFR links these GPCRs to MAPK activation.
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Authors | A Buist, L G Tertoolen, J den Hertog |
Journal | Biochemical and biophysical research communications
(Biochem Biophys Res Commun)
Vol. 251
Issue 1
Pg. 6-10
(Oct 09 1998)
ISSN: 0006-291X [Print] United States |
PMID | 9790898
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Copyright | Copyright 1998 Academic Press. |
Chemical References |
- Endothelin-1
- Lysophospholipids
- Receptors, Cell Surface
- ErbB Receptors
- Calcium-Calmodulin-Dependent Protein Kinases
- GTP-Binding Proteins
- Calcium
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Topics |
- Animals
- COS Cells
- Calcium
(metabolism)
- Calcium-Calmodulin-Dependent Protein Kinases
(metabolism)
- Drug Synergism
- Endothelin-1
(pharmacology)
- Enzyme Activation
(drug effects)
- ErbB Receptors
(biosynthesis, metabolism, physiology)
- GTP-Binding Proteins
(metabolism, physiology)
- Humans
- Lysophospholipids
(metabolism)
- Neuroectodermal Tumors, Primitive, Peripheral
(metabolism)
- Receptors, Cell Surface
(physiology)
- Transcriptional Activation
- Tumor Cells, Cultured
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