Intracellular expression of the truncated extracellular domain of c-erbB-3/HER3.

Srinivasan, R. and Leverton, K.E. and Sheldon, H. and Hurst, H.C. and Sarraf, C. and Gullick, W.J. (2001) Intracellular expression of the truncated extracellular domain of c-erbB-3/HER3. Cellular Signalling, 13 (5). pp. 321-330. ISSN 0898-6568. (Access to this publication is restricted)

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http://dx.doi.org/10.1016/S0898-6568(01)00155-3

Abstract

The ERBB3 gene is expressed as a 6.2- and a 1.4-kb transcript. The former encodes the full-length transmembrane protein and the latter a truncated extracellular fragment consisting of 140 amino acids of the c-erbB-3 protein followed by 43 unique residues. We have examined the expression of the two ERBB3 transcripts by Northern blotting in cancer cell lines and normal human fetal and adult tissues. We expressed the truncated receptor fragment and showed that it was glycosylated, probably with a single N-linked complex sugar chain, and that the protein was a 58-kDa disulphide-linked dimer. We were able to crosslink iodinated neuregulin (NRG)-1beta to the full-length solubilised receptor but not to the truncated dimeric protein. Using Western blot analysis, the truncated protein was shown to be present in cell lysates and, using immunoelectron microscopy, in vesicular structures within cells and associated with the plasma cell membrane.

Item Type: Article
Uncontrolled keywords: erbB-3; HER-3; Glycosylation; Growth factor; Growth factor receptor; Breast cancer
Subjects: Q Science
R Medicine > RC Internal medicine > RC0254 Neoplasms. Tumors. Oncology (including Cancer)
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Faculties > Science Technology and Medical Studies > School of Biosciences > Biomedical Research Group
Depositing User: Sue Davies
Date Deposited: 19 Dec 2007 17:46
Last Modified: 21 Mar 2014 12:39
Resource URI: http://kar.kent.ac.uk/id/eprint/32 (The current URI for this page, for reference purposes)
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