Linked Life Data

10595738

Source:http://linkedlifedata.com/resource/pubmed/id/10595738

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2000-1-4
pubmed:abstractText
Human glioma cells frequently overexpress epidermal growth factor receptor (EGFR). We found that the CrkII proto-oncogene product was associated with the EGFR in human glioma cells in the absence of epidermal growth factor (EGF). EGF stimulation of glioma cells induced the phosphorylation of tyrosine 221 of the CrkII protein, which correlates with its dissociation from the EGFR. By contrast, Shc and Grb2 were inducibly associated with the EGFR in response to EGF stimulation of glioma cells. In A431 cells, epidermoid carcinoma cells which overexpress EGFR, CrkII was tyrosine-phosphorylated and associated with the EGFR in an EGF-dependent manner. Therefore, the dissociation of CrkII from the EGFR upon stimulation with EGF appears to be specific to glioma cells. The Cbl oncogene product was also tyrosine-phosphorylated in U87MG glioma cells upon EGF stimulation. However, unlike in other cell lines, CrkII was not inducibly bound to Cbl in U87MG glioma cells. Thus, EGF-dependent binding of CrkII to phosphotyrosine-containing proteins appears to be suppressed in glioma cells. To evaluate the physiological role of dissociation of CrkII from EGFR, we expressed the CrkII-23 mutant in glioma cells. CrkII-23 mutant, which was isolated as a suppressor gene of the EGF-dependent transformation of NRK cells, binds constitutively to EGFR. We found that expression of CrkII-23 inhibited the anchorage-independent growth of the glioma cells in the presence of EGF. Taken together, these data implicate EGF-dependent dissociation of CrkII from EGFR in the oncogenicity of human glioma cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0910-5050
pubmed:author
pubmed:issnType
Print
pubmed:volume
90
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1096-103
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10595738-Cell Adhesion, pubmed-meshheading:10595738-Cell Division, pubmed-meshheading:10595738-Epidermal Growth Factor, pubmed-meshheading:10595738-Gene Expression Regulation, Neoplastic, pubmed-meshheading:10595738-Glioma, pubmed-meshheading:10595738-Humans, pubmed-meshheading:10595738-Kinetics, pubmed-meshheading:10595738-Phosphorylation, pubmed-meshheading:10595738-Phosphotyrosine, pubmed-meshheading:10595738-Protein Binding, pubmed-meshheading:10595738-Protein Kinases, pubmed-meshheading:10595738-Proto-Oncogene Proteins, pubmed-meshheading:10595738-Proto-Oncogene Proteins c-crk, pubmed-meshheading:10595738-Proto-Oncogenes, pubmed-meshheading:10595738-Receptor, Epidermal Growth Factor, pubmed-meshheading:10595738-Tumor Cells, Cultured, pubmed-meshheading:10595738-src Homology Domains
pubmed:year
1999
pubmed:articleTitle
Epidermal growth factor-dependent dissociation of CrkII proto-oncogene product from the epidermal growth factor receptor in human glioma cells.
pubmed:affiliation
Department of Pathology, National Institute of Infectious Diseases, Tokyo.
pubmed:publicationType
Journal Article