Antibodies to deduced sequences of the insulin receptor distinguish conserved and nonconserved regions in the IGF-I receptor.
Antipeptide antibodies directed to two amino acid sequences predicted from the cDNA encoding the insulin proreceptor have been used to study the relationship between the human receptors for insulin and insulin-like growth factor I (IGF-I). An antibody directed to a cytoplasmic domain near the membrane spanning region of the proreceptor inhibited the protein tyrosine kinase activity of both receptors whereas an antibody directed to the C terminus of the insulin receptor showed no cross-reactivity with the IGF-I receptor. The results establish that the cloned cDNA from the human placenta encodes the insulin receptor and not the closely related IGF-I receptor, that the IGF-I and insulin receptors share a specific amino acid sequence necessary for the expression of enzymatic activity, and that the C terminus of the insulin receptor is not conserved in the IGF-I receptor.
D000595:Amino Acid Sequence; D000906:Antibodies; D004247:DNA / Q000032:analysis; D006657:Histones / Q000378:metabolism; D006801:Humans; D010446:Peptide Fragments / Q000276:immunology*; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors; D011972:Receptor, Insulin / Q000276:immunology*
D000906:Antibodies; D006657:Histones; D010446:Peptide Fragments; D004247:DNA; D011505:Protein-Tyrosine Kinases; D011972:Receptor, Insulin