Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences

Abstract

Each of six peptides derived from the human epidermal growth factor (EGF) receptor very closely matches a part of the deduced sequence of the v-erb-B transforming protein of avian erythroblastosis virus (AEV). In all, the peptides contain 83 amino acid residues, 74 of which are shared with v-erb-B. The AEV progenitor may have acquired the cellular gene sequences of a truncated EGF receptor (or closely related protein) lacking the external EGF-binding domain but retaining the transmembrane domain and a domain involved in stimulating cell proliferation. Transformation of cells by AEV may result, in part, from the inappropriate acquisition of a truncated EGF receptor from the c-erb-B gene.

Reg I-knockout mice reveal its role in regulation of cell growth that is required in generation and maintenance of the villous structure of small intestine

“…In general, malignant transformation results from aberrations in growth factor signal-transduction pathways that normally operate to control cell proliferation. A component of the pathway, either extracellular (Doolittle et al, 1983) or intracellular (Yamamoto et al, 1983;Downward et al, 1984), undergoes a qualitative or quantitative change, leading to constitutive activation of the growth signal and making the cell refractory to external control. In the case of Reg-signaling system in the colonic cells, quantitative change of extracellular component, that is, aberrant overexpression of Reg I, is reported to be important in the colon cancer development (Macadam et al, 2000).…”

Diffuse EGFR staining is associated with reduced overall survival in locally advanced oesophageal squamous cell cancer

“…Three of the factors studied (epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (HER-2) and CD117) are tyrosine kinase receptors, defined by an extracellular ligand-binding specific site, a transmembrane domain and an intracellular domain with tyrosine-kinase activity. Epidermal growth factor receptor and HER-2 belong to the c-erb receptor family (Downward et al, 1984;Coussens et al, 1985), and are implicated in cell proliferation, differentiation and migration in physiological processes. In cancerogenesis, their overexpression leads to abnormal cell proliferation (Ullrich and Schlessinger, 1990;Klapper et al, 2000;Olayioye et al, 2000).…”

Growth inhibition of human lung adenocarcinoma cells by antibodies against epidermal growth factor receptor and by ganglioside GM3: involvement of receptor-directed protein tyrosine phosphatase(s)

“…A relation between the EGF/EGFR system and malignant cell transformation has been well established in experimental systems (Downward et al, 1984;Hayman et al, 1985;Derynck et al, 1987;Di Fiore et al, 1987;Velu et al, 1987). More importantly, EGFR expression in human breast tumours has been correlated with a poor prognosis (Perez et al, 1984;Sainsbury et al, 1985;Received 17April 1996Revised 7 August 1996 Accepted 8 August 1996 Correspondence to: R Perez and F-D Bohmer Macias et al, 1986Macias et al, , 1987aKlijn et al, 1992), and a link between EGFR activity and the malignant process has also been suggested for a number of other epithelial tumours, including non-small-cell lung cancer (NSCLC) (Khazaie et al, 1993;Modjtahedi and Dean, 1994;Fontanini et al, 1995).…”