Analysis of the peptide content of the locust vasopressin-like immunoreactive (VPLI) neurons

Richard A. Baines, Kevin S J Thompson, Richard C. Rayne, Jonathan P. Bacon

    Research output: Contribution to journalArticlepeer-review

    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 (F1, 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 10-6M) 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. © 1995.
    Original languageEnglish
    Pages (from-to)799-807
    Number of pages8
    JournalPeptides
    Volume16
    Issue number5
    Publication statusPublished - 1995

    Keywords

    • cAMP
    • Inhibition
    • Insect
    • Locusta migratoria
    • Neuropeptide

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