Biosynthesis of the protein encoded by the c-met proto-oncogene

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

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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
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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/86559
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