Transfer of functional EGF receptors to an IL3-dependent cell line

✍ Scribed by Mary K. L. Collins; Julian Downward; Atsushi Miyajima; Kazuo Maruyama; Ken-Ichi Arai; Richard C. Mulligan

• Book ID: 102887137
• Publisher: John Wiley and Sons
• Year: 1988
• Tongue: English
• Weight: 655 KB
• Volume: 137
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1041370212

✦ Synopsis

Epidermal growth factor (EGF) is a small protein that acts as a mitogen for various epidermal, epithelial, and fibroblastic cells that bear specific EGF receptors. The molecule that binds EGF is a 175-kD transmembrane protein, with an extracellular ligand binding domain and an intracellular domain that possesses tyrosine kinase activity, thought to be involved in the mitogenic signalling process. Here we have constructed a recombinant murine retrovirus that transduces a human cDNA encoding the 175-kD protein and used this retrovirus to infect BAF3, a murine, bone marrow-derived cell line, which is dependent on the haematopoietic factor interleukin-3 (IL3) for its growth in culture. The EGF receptors expressed in the infected cells exhibit two affinity states, as well as EGF-stimulated autophosphorylation. Furthermore, EGF can replace IL3 in supporting short-term proliferation of these cells. These data identify functional properties of the EGF receptor upon expression of the 175-kD EGF binding protein in a haemotopoietic cell that does not express endogenous receptors. They also suggest that gene transfer of growth factor receptors to heterologous cells may allow novel growth stimuli to be exploited.