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Giordano, S., Di Renzo, M. F., Narsimhan, R. P., Cooper, C. S. 
ORCID: https://orcid.org/0000-0003-2013-8042, Rosa, C. and Comoglio, P. M.
(1989)
Biosynthesis of the protein encoded by the c-met proto-oncogene.
Oncogene, 4 (11).
pp. 1383-1388.
ISSN 0950-9232
Abstract
The proto-oncogene c-met encodes a transmembrane protein with structural features of a growth factor receptor. We have previously shown that the c-met protein (c-Met) is a heterodimer of two disulphide linked chains of 50 kd (α) and 145 kd (β). In this work we have studied the biosynthesis of the c-met product in a gastric carcinoma cell line (GTL-16) where the c-met gene is amplified and overexpressed. Following metabolic labelling of the cells in the presence of tunicamycin, anti-met antibodies immunoprecipitate a protein of 150 kd. In pulse-chase experiments carried out in the absence of tunicamycin, a 170 kd product appears first. Within the next few minutes, this precursor modifies its SDS migration, probably as a consequence of modification(s) of its intra-chain disulphide bonds. After 45 min of chase, this single polypeptide precursor is cleaved to form a 50 kd α subunit and a 145 kd β subunit that are joined by disulphide bonds in an αβ complex with an apparent molecular weight of 190 kd. The presence of N-linked oligosaccharides in both the precursor and the mature protein was shown by enzymatic de-glycosylation of the immunoprecipitated proteins. The half-life of the mature protein was calculated to be approximately 5 h. The c-met protein has similar structure and biosynthesis in other human cell lines.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | molecular biology,genetics,cancer research,sdg 3 - good health and well-being ,/dk/atira/pure/subjectarea/asjc/1300/1312 |
| 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/86559 |
| DOI: |
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