TRH receptors in fish.

The brains of goldfish and other teleosts contain high-affinity binding sites for [3H][3-methyl-His2]thyrotropin-releasing hormone [( 3H]MeTRH) which closely resemble TRH receptors in mammalian brain and pituitary gland in apparent dissociation constant (KD = 3-4 nM), in pharmacology for eight TRH analogs, and in exhibiting marked regional differences in the density of binding sites, with highest binding in the cerebrum and lowest in the cerebellum. Fish brain differs from mammalian brain in containing a prominent additional class of much lower affinity [3H]MeTRH binding sites (KD about 15 microM), of unknown nature, which also exhibit regional differences. Fish pituitary glands contain high-affinity [3H]MeTRH binding sites, but insufficient tissue has prevented full characterization. Little or no saturable binding of [3H]MeTRH was detected in several goldfish peripheral tissues.