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Bradykinin blocks the action of EGF, but not PDGF, on fibroblast division
Author(s) -
Newman E.Luke,
Hyldahl Louise,
Larsson Olle,
Engström Wilhelm,
Rees Anthony R.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81459-0
Subject(s) - bradykinin , platelet derived growth factor receptor , protein kinase c , receptor , epidermal growth factor , fibroblast , dna synthesis , chemistry , endocrinology , medicine , microbiology and biotechnology , kinase , growth factor , biology , biochemistry , dna , in vitro
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.