Premium
Transfer of functional EGF receptors to an IL3‐dependent cell line
Author(s) -
Collins Mary K. L.,
Downward Julian,
Miyajima Atsushi,
Maruyama Kazuo,
Arai KenIchi,
Mulligan Richard C.
Publication year - 1988
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041370212
Subject(s) - epidermal growth factor , biology , microbiology and biotechnology , autophosphorylation , receptor , cell surface receptor , growth factor , tyrosine kinase , signal transduction , protein kinase a , biochemistry , kinase
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 on 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.