| pubmed-article:7937865 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C0034802 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C1336620 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C1149299 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C0015272 | lld:lifeskim |
| pubmed-article:7937865 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:7937865 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:7937865 | pubmed:dateCreated | 1994-11-10 | lld:pubmed |
| pubmed-article:7937865 | pubmed:abstractText | Epidermal growth factor (EGF) and type alpha transforming growth factor (TGF-alpha) bind to a specific region in subdomain III of the extracellular portion of the EGF receptor (EGFR). Binding leads to receptor dimerization, auto-and transphosphorylation on intracellular tyrosine residues, and activation of signal transduction pathways. We compared the binding and biological actions of EGF and TGF-alpha in Chinese hamster ovary (CHO) cells expressing either wild-type human EGFR (HER497R) or a variant EGFR that has an arginine-to-lysine substitution in the extracellular domain at codon 497 (HER497K) within subdomain IV of EGFR. Both receptors exhibited two orders of binding sites with radioiodinated EGF (125I-EGF). Similar results were obtained with 125I-TGF-alpha in cells expressing HER497R. In contrast, only one order of low-affinity binding sites was seen with 125I-TGF-alpha in the case of HER497K. Although EGF and TGF-alpha enhanced tyrosine phosphorylation of both receptors, CHO cells expressing HER497K exhibited an attenuated growth response to EGF and TGF-alpha and a reduced induction of the protooncogenes FOS, JUN, and MYC. Moreover, high concentrations of TGF-alpha (5 nM) inhibited growth in these cells but not in cells expressing HER497R. These findings indicate that a region in subdomain IV of EGFR regulates signal transduction across the cell membrane and selectively modulates that binding characteristics of TGF-alpha. | lld:pubmed |
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| pubmed-article:7937865 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7937865 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7937865 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7937865 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7937865 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7937865 | pubmed:author | pubmed-author:KorcMM | lld:pubmed |
| pubmed-article:7937865 | pubmed:author | pubmed-author:KobrinM SMS | lld:pubmed |
| pubmed-article:7937865 | pubmed:author | pubmed-author:HopeCC | lld:pubmed |
| pubmed-article:7937865 | pubmed:author | pubmed-author:MoriaiTT | lld:pubmed |
| pubmed-article:7937865 | pubmed:author | pubmed-author:SpeckLL | lld:pubmed |
| pubmed-article:7937865 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7937865 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:7937865 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:7937865 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7937865 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7937865 | pubmed:pagination | 10217-21 | lld:pubmed |
| pubmed-article:7937865 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7937865 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7937865 | pubmed:articleTitle | A variant epidermal growth factor receptor exhibits altered type alpha transforming growth factor binding and transmembrane signaling. | lld:pubmed |
| pubmed-article:7937865 | pubmed:affiliation | Department of Medicine, University of California, Irvine 92717. | lld:pubmed |
| pubmed-article:7937865 | pubmed:publicationType | Journal Article | lld:pubmed |
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