
Oxytocin is widely believed to be present and structurally identical in all placental mammals. Here, we report that multiple species of New World monkeys possess a novel form of oxytocin, [P8] oxytocin. This mutation arises from a substitution of a leucine to a proline in amino acid position 8. Further analysis of this mutation in Saimiri sciureus (squirrel monkey) indicates that [P8] oxytocin is transcribed and translated properly. This mutation is specific to oxytocin, as the peptide sequence for arginine vasopressin, a structurally related nonapeptide, is unaltered. These findings dispel the notion that all placental mammals possess a ‘universal’ oxytocin sequence, and highlight the need for research on the functional significance of this novel nonapeptide in New World monkeys.
Molecular Sequence Data, mesotocin, Oxytocin, Medical Toxicology, Chemicals and Drugs, Platyrrhini, oxytocin receptor, Arginine Vasopressin, New World monkey, oxytocin, squirrel monkey, Mutation, Medicine and Health Sciences, Animals, Amino Acid Sequence, arginine vasopressin
Molecular Sequence Data, mesotocin, Oxytocin, Medical Toxicology, Chemicals and Drugs, Platyrrhini, oxytocin receptor, Arginine Vasopressin, New World monkey, oxytocin, squirrel monkey, Mutation, Medicine and Health Sciences, Animals, Amino Acid Sequence, arginine vasopressin
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