Abstract
Anti-idiotypic antibodies have been raised against antibodies to retinol-binding protein (RBP) and to insulin. After absorption the anti-idiotypic antibodies recognized the antigen-combining sites of the antibodies used as the immunogen but of no other antibodies. Some of the anti-idiotypic antibodies raised against antibodies to RBP bound specifically to rat intestine epithelial cells, which have a physiological cell-surface receptor for RBP. The RBP receptor mediates the uptake of retinol from RBP to the cells. This uptake was abolished in a concentration-dependent manner by the anti-idiotypic antibodies, which obviously competed with RBP for binding to the receptor.Anti-idiotypic antibodies against antibodies to insulin inhibited the binding of (125)I-labeled insulin to isolated rat epididymal fat cells, whereas anti-idiotypic antibodies raised against antibodies to RBP had no effect. Furthermore, on interacting with young rat thymocytes, anti-idiotypic antibodies against antibodies to insulin stimulated the uptake by the cells of alpha-aminoisobutyric acid, thereby mimicking the effect of insulin. These results suggest that in some cases anti-idiotypic antibodies may be useful tools in elucidating structure-function relationships for cell-membrane receptors.