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Giordano, S., Ponzetto, C., Di Renzo, M. F., Cooper, C. S. 
ORCID: https://orcid.org/0000-0003-2013-8042 and Comoglio, P. M.
(1989)
Tyrosine kinase receptor indistinguishable from the c-met protein.
Nature, 339 (6220).
pp. 155-156.
ISSN 0028-0836
Abstract
GROWTH factor receptors with protein tyrosine kinase activity are central to the control of proliferation of both normal and malignant cells1-3. Using anti-phosphotyrosine antibodies4, we have previously identified a transmembrane glycoprotein with abnormally high protein tyrosine kinase activity in a human gastric tumour cell line (GTL-16)5,6. Electrophoresis under non-reducing conditions revealed that this kinase (relative molecular mass 145,000 (145 K)) is disulphide-linked to a 50K chain in an αβ-complex of 190K (p190). From its novel two-chain structure, we deduced that p190 was the prototype of a new class of tyrosine kinase receptors. We now show that p190 is indistinguishable from the protein encoded by the c-met protooncogene and that the αβ-subunit structure is conserved in other human cell lines. We also show that the high level of p190 found in the GTL-16 cell line is accompanied by amplification and overexpression of c-met. This provides the first example of a functional alteration of c-met in a human tumour cell line.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | general ,/dk/atira/pure/subjectarea/asjc/1000 |
| Faculty \ School: | Faculty of Medicine and Health Sciences > Norwich Medical School |
| UEA Research Groups: | Faculty of Medicine and Health Sciences > Research Groups > Cancer Studies |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 18 Jul 2022 17:31 |
| Last Modified: | 23 Oct 2022 04:03 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/86555 |
| DOI: | 10.1038/339155a0 |
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