Human transforming growth factors induce tyrosine phosphorylation of EGF receptors

Abstract

Cultured cell lines of human tumour origin as well as cells transformed by various RNA tumour viruses secrete low molecular weight polypeptide transforming growth factors (TGFs)^1,2. In addition to competing with epidermal growth factor (EGF) for binding to its cellular receptor, TGFs can transform morphologically fibroblast and epithelial cells in culture^1–3. In view of accumulating evidence that tyrosine phosphorylation activity is associated with the transforming genes of various tumour viruses^4–13, we determined whether phosphotyrosine levels were elevated in these human tumour cells. We show here that TGFs produced by human tumour cells induce phosphorylation of specific tyrosine acceptor sites in the 160,000-molecular weight (160 K) EGF receptor.