Bradykinin blocks the action of EGF, but not PDGF, on fibroblast division

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Abstract
Quiescent fibroblasts derived from human fetal lung can be stimulated to reinitiate DNA synthesis by sequential addition of 3 nM IGF‐1 and a low concentration (8 pM) of EGF or by continuous exposure to 10% fetal calf serum or 10 ng/ml PDGF. Bradykinin blocks the IGF‐1 and EGF‐dependent signals without affecting the response to serum or PDGF. it activates protein kinase C and its anti‐mitogenic effect is abolished after this kinase has been down‐regulated. Bradykinin has no effect on the binding affinity of the EGF receptor whereas phorbol ester induces its ‘transmodulation’ to low affinity.