Bradykinin blocks the action of EGF, but not PDGF, on fibroblast division.
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.
Newman
E L
EL
Laboratory of Molecular Biophysics, University of Oxford, England.
Hyldahl
L
L
Larsson
O
O
Engström
W
W
Rees
A R
AR
D001769:Blood; D001920:Bradykinin / Q000494:pharmacology*; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D004247:DNA / Q000096:biosynthesis*; D004622:Embryo, Mammalian; D004789:Enzyme Activation / Q000187:drug effects; D004815:Epidermal Growth Factor / Q000494:pharmacology*; D005347:Fibroblasts / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D007334:Insulin-Like Growth Factor I / Q000494:pharmacology; D008168:Lung; D010982:Platelet-Derived Growth Factor / Q000494:pharmacology*; D011493:Protein Kinase C / Q000378:metabolism; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D010982:Platelet-Derived Growth Factor; D004815:Epidermal Growth Factor; D007334:Insulin-Like Growth Factor I; D004247:DNA; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate; D001920:Bradykinin