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J. Biol. Chem., Vol. 262, Issue 33, 15821-15824, 11, 1987
LJ Cruz, V de Santos, GC Zafaralla, CA Ramilo, R Zeikus, WR Gray and BM Olivera
The vasopressin-oxytocin family of peptides is of very ancient lineage,
found in organisms as diverse as hydra and man. Although these peptides
have been intensively studied in vertebrates, the presumably more extensive
invertebrate series was defined primarily by immunological methods. In this
report, we describe the purification and structures of two peptides of the
vasopressin-oxytocin family from molluscs ("Conopressins"), which were
found in the venom of fish-hunting marine snails of the genus Conus. The
biological activity observed when the two snail peptides are injected
intracerebrally into mice is very similar to that elicited by the
vertebrate neurohypophyseal hormones and presumably reflects their actions
upon a common receptor in the brain. The sequences of the purified peptides
reveal unique features not found in the vertebrate peptide series, most
notably an additional positive charge. These are the first members of the
invertebrate series of the vasopressin-oxytocin family to be characterized
biochemically. The sequences of these peptides are: from Conus geographus
venom, Lys- conopressin-G, Cys-Phe-Ile-Arg-Asn-Cys-Pro-Lys-Gly-NH2; and
from Conus striatus venom, Arg-conopressin-S,
Cys-Ile-Ile-Arg-Asn-Cys-Pro-Arg-Gly- NH2.
Invertebrate vasopressin/oxytocin homologs. Characterization of peptides from Conus geographus and Conus straitus venoms
Department of Biology, University of Utah, Salt Lake City 84112.
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