Tyrosine kinase receptor indistinguishable from the c-met protein

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

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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
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Depositing User: LivePure Connector
Date Deposited: 18 Jul 2022 17:31
Last Modified: 13 Aug 2022 02:25
URI: https://ueaeprints.uea.ac.uk/id/eprint/86555
DOI: 10.1038/339155a0

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