Inhibition of epidermal growth factor binding to mouse cultured cells by fibroblast-derived growth factor. Evidence for an indirect mechanism.

Fibroblast-derived growth factor (FDGF), a basic, heat- and acid-stable polypeptide partially purified from the serum-free conditioned medium of BHK cells transformed by simian virus 40, is a potent mitogen for Swiss 3T3 cells and causes a marked reduction in 125I-labeled epidermal growth factor (125I-EGF) binding to these cells. The activity which inhibits EGF binding coelutes with the growth-stimulating activity after gel filtration, ion exchange chromatography, and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Both cellular responses are elicited by the same range of FDGF concentration in several murine cell types.

Melittin stimulates Na entry, Na-K pump activity and DNA synthesis in quiescent cultures of mouse cells.

Melittin, an amphipatic polypeptide, increases several fold the activity of Na-K pump in quiescent Swiss 3T3 cells. As with other growth factors, melittin increases the activity of the pump by increasing Na entry into the cell. In contrast, other early responses are not elicited by the toxin.