Articlegreen1994

Structure, function, and phylogeny of [Arg8]vasotocinreceptors from teleost fish and toad.

Stefan Mahlmann · Wolfgang Meyerhof · Holger Hausmann · Jörg Heierhorst · Christiane Schönrock · H. Zwiers +2 more

151 citations0/0 files storedProceedings of the National Academy of Sciences

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Neuroendocrine regulation and behavior Neuropeptides and Animal Physiology Cardiovascular, Neuropeptides, and Oxidative Stress Research

Abstract

[Arg8]Vasotocin (AVT) is considered to be the most primitive known vertebrate neurohypophyseal peptide of the vasopressin/oxytocin hormone family and may thus be ancestral to all the other vertebrate peptide hormones. The molecular evolution of the corresponding receptor family has now been studied by cloning an AVT receptor, consisting of 435 amino acid residues, from the teleost fish, the white sucker Catostomus commersoni. Frog oocytes injected with the AVT receptor-encoding cRNA respond to the application of AVT, but not to its structural and functional counterpart isotocin, by an induction of membrane chloride currents indicating the coupling of the AVT receptor to the inositol phosphate/calcium pathway. The pharmacological properties of the expressed AVT receptor show that it represents, or is closely related to, an ancestral nonapeptide receptor: oxytocin, aspargtocin, mesotocin, and vasopressin activated the receptor, but other members of the vasopressin/oxytocin family tested showed little or no potency; antagonists of the mammalian vasopressin V1 and oxytocin receptors blocked the AVT response. Comparison of AVT receptor sequences spanning transmembrane domains two to five, deduced by cloning cDNAs from the Pacific salmon Oncorhynchus kisutch, the cave-dwelling fish Astyanax fasciatus, and the anuran Xenopus laevis, with those of their mammalian counterparts emphasizes amino acid residues that are involved in hormone binding. The presence of a 5.0-kb transcript in various teleost tissues (pituitary, liver, gills, swim bladder, and lateral line) points to a physiological role for the fish AVT receptor in metabolic, osmoregulatory, and sensory processes.

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References

1992Structure and expression of a human oxytocin receptor 1992Molecular cloning and expression of a rat Via arginine vasopressin receptor 1991Reflex control of magnocellular vasopressin and oxytocin secretion 1988125I-labelled d(CH2)5[Tyr(Me)2,Thr4,Tyr-NH29]OVT: a selective oxytocin receptor ligand

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