Abstract
Isolated cell bodies of the locust vasopressin-like immunoreactive (VPLI) neurons, analyzed by HPLC separation and radioimmune assay, contain three arginine vasopressin-like peptides: a previously identified monomer (Fl, Cys-Leu-Ile-Thr-Asn-Cys-Pro-Arg-Gly-NH2) and its antiparallel homodimer (F2), but also the previously unreported parallel homodimer (PDm). VPLI neuron activity significantly reduces the level of cAMP in the CNS. Of the three synthetic peptides, only the monomer (F1, 10(-8) and 10(-6) M) is capable of inhibiting a forskolin-stimulated increase in cAMP in isolated neural membranes. The antiparallel (F2) and parallel dimers (PDm) of this peptide have no effect on this second messenger.
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