Antipeptide antibodies directed against cytoplasmic rhodopsin sequences recognize the beta-adrenergic receptor.

Antibodies were made against synthetic peptides that correspond to cytoplasmic domains of rhodopsin, the photopigment protein of the retinal rod. These antipeptide antibodies recognized rhodopsin as detected by immunoblot analysis. Antibodies directed against the cytoplasmic loop between transmembrane domains 1 and 2, as well as those directed against the serine/threonine-rich region of the COOH terminus of bovine rhodopsin, also recognized purified beta-adrenergic receptor isolated from mouse S49 lymphoma cells. In addition, antibodies raised against membrane-associated rhodopsin recognized the beta-adrenergic receptor. Both the antipeptide and anti-rhodopsin antibodies were able to detect a 65-kDa protein band corresponding to the molecular weight of the beta-adrenergic receptor in membranes derived from human placenta, rat adipocytes, and S49 mouse lymphoma cells. Putative recognition sites for the rhodopsin antibodies on the beta-adrenergic receptor are identified, and the significance of the homology between the two proteins is discussed.