Linked Life Data

11745410

Source:http://linkedlifedata.com/resource/pubmed/id/11745410

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-12-17
pubmed:abstractText
We previously reported that ganglioside GD1a, which is highly expressed in poorly metastatic FBJ-S1 cells, inhibits the serum-induced motility of FBJ-LL cells and that the metastatic potential of FBJ-LL cells is completely suppressed by enforced GD1a expression (Hyuga et al., Int J Cancer 1999;83:685-91). We recently discovered that hepatocyte growth factor (HGF) induces FBJ-LL cell motility. In the present study, the HGF-induced motility of FBJ-S1 cells was found to be one-thirtieth that of FBJ-LL cells. This motility of GD1a-expressing transfectants, which were produced by transfection of FBJ-LL cells with GM2/GD2 synthase cDNA, decreased with increases in their GD1a expression and HGF induced almost no motility in GD1a-pretreated FBJ-LL cells, indicating that GD1a inhibits the HGF-induced motility of FBJ-LL cells. The expression of the HGF receptor c-Met on FBJ-S1 cells, FBJ-LL cells, transfectants and a mock-transfectant was almost the same. The level of tyrosine phosphorylation of c-Met after HGF stimulation in FBJ-S1 cells, GD1a-pretreated FBJ-LL cells and a GD1a-expressing transfectant was significantly lower than in FBJ-LL cells and a mock-transfectant. These findings suggested that GD1a inhibits the HGF-induced motility of FBJ-LL cells through suppression of tyrosine phosphorylation of c-Met. HepG2 cells, a human hepatoma cell line, were used to investigate whether GD1a interferes with other cancer cells expressing c-Met. HepG2 cells did not express GD1a. HGF induced cell scattering of HepG2 cells and the scattering was inhibited by pretreating the cells with GD1a. The c-Met in the cells was autophosphorylated by stimulation with HGF, but after treating the cells with GD1a, the HGF-induced autophosphorylation of c-Met was suppressed. These results suggest that GD1a acts as a negative regulator of c-Met in cancer cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0020-7136
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
328-34
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11745410-Actins, pubmed-meshheading:11745410-Animals, pubmed-meshheading:11745410-Blotting, Western, pubmed-meshheading:11745410-Cell Movement, pubmed-meshheading:11745410-DNA, Complementary, pubmed-meshheading:11745410-Flow Cytometry, pubmed-meshheading:11745410-G(M1) Ganglioside, pubmed-meshheading:11745410-Gangliosides, pubmed-meshheading:11745410-Hepatocyte Growth Factor, pubmed-meshheading:11745410-Mice, pubmed-meshheading:11745410-Neoplasms, pubmed-meshheading:11745410-Phosphorylation, pubmed-meshheading:11745410-Precipitin Tests, pubmed-meshheading:11745410-Proto-Oncogene Proteins c-met, pubmed-meshheading:11745410-Signal Transduction, pubmed-meshheading:11745410-Stress Fibers, pubmed-meshheading:11745410-Time Factors, pubmed-meshheading:11745410-Transfection, pubmed-meshheading:11745410-Tumor Cells, Cultured, pubmed-meshheading:11745410-Tyrosine
pubmed:year
2001
pubmed:articleTitle
Ganglioside GD1a inhibits HGF-induced motility and scattering of cancer cells through suppression of tyrosine phosphorylation of c-Met.
pubmed:affiliation
Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, Setagayaku, Tokyo, Japan. hyuga@nihs.go.jp
pubmed:publicationType
Journal Article