Unknown

Dataset Information

0

A novel form of oxytocin in New World monkeys.


ABSTRACT: 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.

SUBMITTER: Lee AG 

PROVIDER: S-EPMC3130245 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications


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  ...[more]

Similar Datasets

| S-EPMC4418824 | biostudies-literature
| S-EPMC4928571 | biostudies-literature
| S-EPMC1524723 | biostudies-literature
| S-EPMC6412371 | biostudies-literature
| S-EPMC4776464 | biostudies-literature
| S-EPMC8049090 | biostudies-literature
| S-EPMC4470872 | biostudies-literature
| S-EPMC1626214 | biostudies-literature
| S-EPMC4839179 | biostudies-literature
| S-EPMC5609184 | biostudies-literature