Vasopressin receptors: structural functional relationships and role in neural and endocrine regulation.

Abstract

Vasopressin (VP) is the biologically active peptide whose endocrine and neural actions, chemical structure, biosynthesis and receptors were described before any other peptide hormone. In this respect, VP has fulfilled an important role as a prototype peptide in the fields of endocrinology and neurosciences, and has always been on the brink of novel advances and concepts. VP was described originally as an entity in posterior pituitary extracts that led to antidiuresis and vasoconstriction, hence its name. In the 1950s it was purified from this gland and its chemical structure determined, an achievement by Vincent du Vigneaud that was honored by the Nobel prize in 1955 (Du Vigneaud 1956). It turned out to be a nonapeptide with an internal disulfide bridge and amidated C terminus, Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-G1yNH2, and to be closely related to oxytocin (OT). VP has been the leading component in the concepts of neurosecretion and neuropeptides (Bargmann 1966; De Wied 1997). The VP/OT signaling system is evolutionarily old as is illustrated by the presence of highly similar peptides and receptors in diverse metazoans such as mollusca, arthropoda, annelida and chordata.