A Chimeric EGFR/neuReceptor in Functional Analysis of theneuOncoprotein
Autor: | Heikki Lehväslaiho, L Lehtola, Päivi J. Koskinen, Kari Alitalo |
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Rok vydání: | 1992 |
Předmět: |
Receptor
ErbB-2 Tropomyosin receptor kinase B Transfection Tropomyosin receptor kinase C Receptor tyrosine kinase Mice 03 medical and health sciences 0302 clinical medicine Epidermal growth factor Proto-Oncogene Proteins Animals Radiology Nuclear Medicine and imaging Phosphorylation Protein kinase A 030304 developmental biology 0303 health sciences Epidermal Growth Factor biology 3T3 Cells Hematology General Medicine Protein-Tyrosine Kinases Molecular biology Recombinant Proteins ErbB Receptors Oncology 030220 oncology & carcinogenesis ROR1 biology.protein Signal transduction Tyrosine kinase Cell Division Signal Transduction |
Zdroj: | Acta Oncologica. 31:147-150 |
ISSN: | 1651-226X 0284-186X |
DOI: | 10.3109/02841869209088895 |
Popis: | As the factor binding to the neu protein has been unknown, it has not been possible to confirm experimentally the proposed growth-factor receptor like functions of the neu protein. To approach this problem we constructed a recombinant receptor which enabled ligand regulation of the neu tyrosine kinase. The hybrid receptor consisted of the extracellular ligand binding, transmembrane and protein kinase C-substrate domains joined to the intracellular tyrosine kinase and carboxyl-terminal domains of the neu protein. Several properties of NIH3T3 cells carrying this construct were tested. We obtained the first experimental evidence that the neu proto-oncogene has mitogenic and transforming activities only in the presence of a ligand stimulating its tyrosine kinase activity. Various cellular and molecular biological parameters indicated that the chimeric receptor behaved very similarly to the EGFR. Also, this chimeric receptor has allowed us to compare the constitutive oncogenic and the ligand-activated non-oncogenic activities of the neu tyrosine kinase. In the future we plan to focus on characterization of possible differences between EGFR and neu signalling in more differentiated cellular backgrounds. |
Databáze: | OpenAIRE |
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