Biosynthesis and degradation of the arginine-vasopressin-like insect diuretic hormone, a neurohormone in the migratory locust.

The migratory locust (Locusta migratoria) contains two neuropeptides structurally related to mammalian arginine-vasopressin: a 9-residue monomer, without known biological activity, and its antiparallel dimer: the arginine-vasopressin-like insect diuretic hormone which increases urine production at the Malpighian tubules level. We demonstrate hereunder that a transformation monomer-to-dimer-to a degradative product occurs in several steps. (1) A transformation monomer-to-dimer takes place in the suboesophageal ganglion, the site of biosynthesis of the monomer, obviously enzymatically controlled. (2) Monomer and dimer are simultaneously released from the suboesophageal ganglion into the haemolymph where the transformation monomer-to-dimer continues. (3) Dimer is then transported to its target-tissue, the Malpighian tubules, where it is degradated by another enzymatic process.