G protein-coupled receptor agonist-stimulated expression of ATF3/LRF-1 and c-myc and comitogenic effects in hepatocytes do not require EGF receptor transactivation

2004 ◽  
Vol 201 (3) ◽  
pp. 349-358 ◽  
Author(s):  
Laila S. Nilssen ◽  
John Ødegård ◽  
G. Hege Thoresen ◽  
Anders Molven ◽  
Dagny Sandnes ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Agonist ◽  
Egf Receptor ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled ◽  
Receptor Transactivation

scholarly journals Involvement of Nuclear Factor-κB and Apoptosis Signal-Regulating Kinase 1 in G-Protein–Coupled Receptor Agonist–Induced Cardiomyocyte Hypertrophy

Circulation ◽  
2002 ◽  
Vol 105 (4) ◽  
pp. 509-515 ◽  
Author(s):  
Shinichi Hirotani ◽  
Kinya Otsu ◽  
Kazuhiko Nishida ◽  
Yoshiharu Higuchi ◽  
Takashi Morita ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Agonist ◽  
Nuclear Factor Κb ◽  
Cardiomyocyte Hypertrophy ◽  
Nuclear Factor ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF

Nature ◽  
10.1038/47260 ◽  
1999 ◽  
Vol 402 (6764) ◽  
pp. 884-888 ◽  
Author(s):  
Norbert Prenzel ◽  
Esther Zwick ◽  
Henrik Daub ◽  
Michael Leserer ◽  
Reimar Abraham ◽  
...  
Keyword(s):  
G Protein ◽  
Egf Receptor ◽  
G Protein Coupled Receptors ◽  
G Protein Coupled ◽  
Receptor Transactivation

scholarly journals Shedding of c-Met is regulated by crosstalk between a G-protein coupled receptor and the EGF receptor and is mediated by a TIMP-3 sensitive metalloproteinase

2001 ◽  
Vol 114 (6) ◽  
pp. 1213-1220
Author(s):  
D. Nath ◽  
N.J. Williamson ◽  
R. Jarvis ◽  
G. Murphy
Keyword(s):  
Growth Factor ◽  
G Protein ◽  
Egf Receptor ◽  
Growth Factor Receptor ◽  
Receptor Activation ◽  
Ectodomain Shedding ◽  
G Protein Coupled Receptor ◽  
Cell Matrix ◽  
Cell Matrix Interactions ◽  
G Protein Coupled

A wide repertoire of transmembrane proteins are proteolytically released from the cell surface by a process known as ‘ectodomain shedding’, under both normal and pathophysiological conditions. Little is known about the physiological mechanisms that regulate this process. As a model system, we have investigated the metalloproteinase-mediated cleavage of the hepatocyte growth factor receptor, Met. We show that epidermal growth factor (EGF) receptor activation, either directly by EGF or indirectly via the G-protein coupled receptor (GPCR) agonist lysophosphatidic acid (LPA), induces cleavage of Met through activation of the Erk MAP kinase signalling cascade. The tyrosine kinase activity of the EGFR was a prerequisite for this stimulation, since treatment of cells with a synthetic inhibitor of this receptor, AG1478, completely abrogated shedding. The metalloproteinase mediating Met cleavage was specifically inhibited by the tissue inhibitor of metalloproteinases (TIMP)-3, but not by TIMP-1 or TIMP-2. Furthermore, the level of Met shedding could be modulated by different cell-matrix interactions. Our results indicate that ectodomain shedding is a highly regulated process that can be stimulated by EGFR signalling pathways and integrin ligation.

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