Characterization of the receptor for platelet-derived growth factor on human fibroblasts. Demonstration of an intimate relationship with a 185,000-Dalton substrate for the platelet-derived growth factor-stimulated kinase.

摘要: The receptor for platelet-derived growth factor (PDGF) on human foreskin fibroblasts has been characterized. molecular weight of the PDGF-receptor complex was estimated by affinity labeling techniques to about 200,000, as determined sodium dodecyl sulfate-gel electrophoresis performed under reducing conditions. Subtraction Mr reduced PDGF (18,000 15,000) gives a proper 185,000 (+/- 10,000). mobility in similar whether or not agents were present, suggesting that may be single chain protein. hydrodynamic size 125I-PDGF-receptor after solubilization with Triton X-100, corresponded approximately 320,000, gel chromatography. contributions from X-100 and PDGF, respectively, 200,000 itself, an estimate good agreement value obtained affinity-labeling experiments. Several lectins analyzed their ability inhibit binding 125I-PDGF its receptor. It found wheat germ agglutinin lectin Crotalaria juncea effective inhibitors inhibitory effects could neutralized N-acetylglucosamine galactose, contains these sugars. properties compared those 185,000-Da component, being major substrate membrane-bound PDGF-stimulated kinase. component behaved electrophoresis, without present. Further, co-eluted Sepharose 6B column, had same inhibited Finally, immobilized beads, it PDGF-binding activity. We conclude PDGF-dependent kinase are intimately related probably identical molecules.