Source:http://linkedlifedata.com/resource/pubmed/id/17032311
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
2006-11-2
|
pubmed:abstractText |
The association of hepatocyte growth factor (HGF) with its high-affinity receptor (c-Met) has been shown to induce mitogenesis, motogenesis and morphogenesis in a variety of cell types. Various point mutations in c-Met have been identified in hereditary and sporadic papillary renal carcinomas as well as in other carcinomas. In the present study, we examined the effects of c-Met point mutations on the morphology of a porcine aortic endothelial (PAE) cell line. When cultured in three-dimensional collagen gel, PAE cells formed branching tubule structures, and HGF treatment caused breakdown of the structures and induced a scattered morphology. The exogenous expression of c-Met point mutants inhibited the formation of tubules. HGF treatment induced the formation of tubules by PAE cells expressing some c-Met mutants, but it induced the scattering of PAE cells expressing other c-Met mutants. The presence of a low concentration of a mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) inhibitor cancelled the inhibitory effect of the c-Met point mutations on the formation of tubules. These results suggest that c-Met point mutations affect the extracellular signal-regulated kinase (ERK) signaling required for the formation of tubules by PAE cells, and HGF binding changes the conformation of c-Met mutants, leading to the different signals required for formation of tubules and cell scattering.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-met
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
1347-9032
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
97
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1343-50
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:17032311-Animals,
pubmed-meshheading:17032311-Aorta,
pubmed-meshheading:17032311-Cells, Cultured,
pubmed-meshheading:17032311-Endothelium, Vascular,
pubmed-meshheading:17032311-Hepatocyte Growth Factor,
pubmed-meshheading:17032311-MAP Kinase Kinase Kinases,
pubmed-meshheading:17032311-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:17032311-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:17032311-Phenotype,
pubmed-meshheading:17032311-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:17032311-Proto-Oncogene Proteins c-met,
pubmed-meshheading:17032311-Signal Transduction,
pubmed-meshheading:17032311-Swine
|
pubmed:year |
2006
|
pubmed:articleTitle |
Inhibitory effect of c-Met mutants on the formation of branching tubules by a porcine aortic endothelial cell line.
|
pubmed:affiliation |
Department of Biological Sciences, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|