STRUCTURAL AND FUNCTIONAL EVOLUTION OF THE VASOPRESSIN OXYTOCIN SUPERFAMILY - VASOPRESSIN-RELATED CONOPRESSIN IS THE ONLY MEMBER PRESENT INLYMNAEA, AND IS INVOLVED IN THE CONTROL OF SEXUAL-BEHAVIOR
Re. Vankesteren et al., STRUCTURAL AND FUNCTIONAL EVOLUTION OF THE VASOPRESSIN OXYTOCIN SUPERFAMILY - VASOPRESSIN-RELATED CONOPRESSIN IS THE ONLY MEMBER PRESENT INLYMNAEA, AND IS INVOLVED IN THE CONTROL OF SEXUAL-BEHAVIOR, The Journal of neuroscience, 15(9), 1995, pp. 5989-5998
It has been suggested that the gene duplication that led to the format
ion of the vasopressin/oxytocin two-gene family occurred early during
vertebrate evolution. However, the existence of both vasopressin- and
oxytocin-related peptides in invertebrates suggests that this duplicat
ion may have occurred much earlier, although there is no evidence for
the co-occurrence of vasopressin- and oxytocin-related peptides in the
same invertebrate species, We report here that in Lymnaea only the va
sopressin-related peptide Lys-conopressin, but not an oxytocin-related
peptide, is present. Moreover, it is very likely that an oxytocin-lik
e cDNA or gene is absent. The conopressin gene is expressed in neurons
that control male sexual behavior, and its gene products are present
in the penis nerve and the vas deferens, Conopressin induces muscular
contractions of the vas deferens and inhibits central neurons that con
trol female reproductive behavior. Thus, although structurally related
to vasopressin, conopressin has functional and behavioral characteris
tics typical for oxytocin. Physiological and receptor binding data sug
gest that conopressin and [Ile(8)]-conopressin, a synthetic oxytocin-l
ike analog of conopressin, are functionally equivalent in Lymnaea, and
that the chemical nature of the amino acid residue at position 8 does
not result in a functional difference. Therefore, we suggest that inv
ertebrates contain only a single member of the vasopressin/oxytocin ge
ne family and that the amino acid change that distinguishes vasopressi
n from oxytocin is functionally neutral in invertebrates.