PMID- 10595738
OWN - NLM
STAT- MEDLINE
DCOM- 20000104
LR  - 20190513
IS  - 0910-5050 (Print)
IS  - 0910-5050 (Linking)
VI  - 90
IP  - 10
DP  - 1999 Oct
TI  - Epidermal growth factor-dependent dissociation of CrkII proto-oncogene product
      from the epidermal growth factor receptor in human glioma cells.
PG  - 1096-103
AB  - 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.
FAU - Katayama, H
AU  - Katayama H
AD  - Department of Pathology, National Institute of Infectious Diseases, Tokyo.
FAU - Hashimoto, Y
AU  - Hashimoto Y
FAU - Kiyokawa, E
AU  - Kiyokawa E
FAU - Nakaya, M
AU  - Nakaya M
FAU - Sakamoto, A
AU  - Sakamoto A
FAU - Machinami, R
AU  - Machinami R
FAU - Kurata, T
AU  - Kurata T
FAU - Mochizuki, N
AU  - Mochizuki N
FAU - Matsuda, M
AU  - Matsuda M
LA  - eng
PT  - Journal Article
PL  - Japan
TA  - Jpn J Cancer Res
JT  - Japanese journal of cancer research : Gann
JID - 8509412
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Proto-Oncogene Proteins c-crk)
RN  - 21820-51-9 (Phosphotyrosine)
RN  - 62229-50-9 (Epidermal Growth Factor)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.10.1 (ErbB Receptors)
SB  - IM
MH  - Cell Adhesion
MH  - Cell Division
MH  - Epidermal Growth Factor/*pharmacology
MH  - ErbB Receptors/drug effects/*metabolism
MH  - Gene Expression Regulation, Neoplastic
MH  - Glioma
MH  - Humans
MH  - Kinetics
MH  - Phosphorylation
MH  - Phosphotyrosine/metabolism
MH  - Protein Binding
MH  - Protein Kinases/genetics/*metabolism
MH  - *Proto-Oncogene Proteins
MH  - Proto-Oncogene Proteins c-crk
MH  - *Proto-Oncogenes
MH  - Tumor Cells, Cultured
MH  - src Homology Domains
PMC - PMC5926002
EDAT- 1999/12/14 00:00
MHDA- 1999/12/14 00:01
CRDT- 1999/12/14 00:00
PHST- 1999/12/14 00:00 [pubmed]
PHST- 1999/12/14 00:01 [medline]
PHST- 1999/12/14 00:00 [entrez]
AID - S0910505099801744 [pii]
AID - 10.1111/j.1349-7006.1999.tb00683.x [doi]
PST - ppublish
SO  - Jpn J Cancer Res. 1999 Oct;90(10):1096-103. doi:
      10.1111/j.1349-7006.1999.tb00683.x.