title: Pharmacological characterization of melanocortin receptors in fish suggests an important role for ACTH.
abstract: The melanocortin (MC) receptor subtypes have distinctive characteristic binding profiles. We found that the trout and Fugu MC4 receptors have similar affinity for alpha-MSH and beta-MSH and a much higher affinity for ACTH than does the human MC4 receptor. The Fugu MC1 and the trout and Fugu MC5 receptors also have higher affinity for ACTH-derived peptides than alpha-, beta-, or gamma-MSH. It is tempting to speculate that ACTH-derived peptides may have played an important role as "original" ligands at the MC receptors, while the specificity of the different subtypes for the alpha-, beta-, and gamma-MSH peptides may have appeared at later stages during vertebrate evolution.
authors.affiliation: Department of Neuroscience, Biomedical Center, Uppsala University, Sweden. tatjana.haitina@neuro.uu.se
authors.forename: Tatjana
authors.initials: T
authors.lastname: Haitina
authors.forename: Janis
authors.initials: J
authors.lastname: Klovins
authors.forename: Helgi B
authors.initials: HB
authors.lastname: Schiöth
mesh_terms: D000324:Adrenocorticotropic Hormone / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology*; D000818:Animals; D005399:Fishes / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D044101:Receptors, Melanocortin / Q000378:metabolism*
chemical_list: D044101:Receptors, Melanocortin; D000324:Adrenocorticotropic Hormone