Insulin/Insulin-like Growth Factor I Hybrid Receptors Have Different Biological Characteristics Depending on the Insulin Receptor Isoform Involved

The insulin receptor (IR) and the insulin-like growth factor I receptor (IGF-IR) have a highly homologous structure, but different biological effects. Insulin and IGF-I half-receptors can heterodimerize, leading to the formation of insulin/IGF-I hybrid receptors (Hybrid-Rs) that bind IGF-I with high...

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Veröffentlicht in:	The Journal of biological chemistry 2002-10, Vol.277 (42), p.39684-39695
Hauptverfasser:	Pandini, Giuseppe, Frasca, Francesco, Mineo, Rossana, Sciacca, Laura, Vigneri, Riccardo, Belfiore, Antonino
Format:	Artikel
Sprache:	eng
Schlagworte:	3T3 Cells Animals Binding, Competitive Blotting, Western Bromodeoxyuridine - pharmacology Cell Division Cell Line Cell Movement Chemotaxis DNA, Complementary - metabolism Dose-Response Relationship, Drug Fibroblasts - metabolism Genetic Vectors Humans Insulin - metabolism Insulin-Like Growth Factor I - metabolism Insulin-Like Growth Factor II - metabolism Ligands Mice Microscopy, Fluorescence Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases - metabolism Phosphorylation Protein Binding Protein Isoforms Protein-Serine-Threonine Kinases Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-akt Receptor, IGF Type 1 - chemistry Receptor, Insulin - chemistry Recombinant Fusion Proteins - chemistry Reverse Transcriptase Polymerase Chain Reaction Signal Transduction Time Factors Transfection Tumor Cells, Cultured
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