Platelet-derived growth factor treatment decreases the affinity of the epidermal growth factor receptors of Swiss 3T3 cells.
Platelet-derived growth factor (PDGF) inhibits markedly (90%) the binding of a low concentration (0.5 ng/ml) of 125I-labeled epidermal growth factor (125I-EGF) to Swiss 3T3 cells in a dose, time, and temperature-dependent manner. In contrast, PDGF inhibits the binding of a high concentration (20 ng/ml) of 125I-EGF by only 20%. Detailed Scatchard analysis of 125I-EGF binding to Swiss 3T3 cells at 4 degrees C, after a 2-h incubation with a saturating level of PDGF at 37 degrees C, demonstrates that this PDGF pretreatment does not change the number of EGF receptors (70,000 sites/cell), but causes a large decrease in the affinity of the receptors, from a mixed population of 0.5-12 ng/ml, to an affinity of 13 ng/ml. A parallel treatment at 37 degrees C with EGF itself causes a 70% decrease in the number of EGF receptors. Therefore, we conclude, in contrast to previous reports, that PDGF (unlike EGF) does not cause down-regulation of EGF receptors. Rather PDGF induces a potent, temperature-dependent change in the affinity of the EGF receptor population ("transmodulation").
D000818:Animals; D001667:Binding, Competitive; D002478:Cells, Cultured; D004815:Epidermal Growth Factor / Q000378:metabolism* / Q000494:pharmacology; D066246:ErbB Receptors; D007700:Kinetics; D051379:Mice; D010982:Platelet-Derived Growth Factor / Q000494:pharmacology*; D011956:Receptors, Cell Surface / Q000378:metabolism*
D010982:Platelet-Derived Growth Factor; D011956:Receptors, Cell Surface; D004815:Epidermal Growth Factor; D066246:ErbB Receptors