fmrfamide and benzoquinonium

fmrfamide has been researched along with benzoquinonium* in 2 studies

Other Studies

2 other study(ies) available for fmrfamide and benzoquinonium

ArticleYear
The effect of the nematode peptides SDPNFLRFamide (PF1) and SADPNFLRFamide (PF2) on synaptic transmission in the parasitic nematode Ascaris suum.
    Parasitology, 1995, Volume: 110 ( Pt 4)

    The action of two peptides isolated from the nematode Panagrellus redivivus, PF1 (SDPNFLRFamide) and PF2 (SADPNFLRFamide) have been studied on synaptic transmission in the motornervous system of the parasitic nematode Ascaris suum. Intracellular recordings were made from Ascaris somatic muscle cells and excitatory junction potentials (EJPs) elicited by stimulation of the ventral nerve cord. The EJPs were cholinergic as they were blocked by the Ascaris nicotinic receptor antagonist, benzoquinonium. PF1 caused a slow hyperpolarization, similar to the action of this peptide first reported by Bowman, Geary & Thompson (1990) and further characterized by Franks et al. (1994). The hyperpolarization was accompanied by a marked decrease in the amplitude of the EJPs with an EC50 of 311 +/- 30 nM (n = 5). This inhibition is unlikely to be due to a post-synaptic site of action of the peptide as the muscle cell input conductance was not significantly altered by PF1 and furthermore the response to bath-applied acetylcholine was not inhibited by PF1 at concentrations up to 10 microM (n = 6). PF2 also inhibited the EJPs in a similar manner to PF1. These studies indicate that both of the peptides isolated from the free-living nematode Panagrellus redivivus have biological activity in the parasitic nematode Ascaris suum. PF1 and PF2 have inhibitory actions in contrast to the predominantly excitatory actions of the Ascaris endogenous peptides AF1 (KNEFIRFamide) and AF2 (KHEYLRFamide). The potent actions of the Panagrellus neuropeptides PF1 and PF2 in Ascaris suggest that peptides with a similar or identical sequence may also occur in Ascaris and have an inhibitory role in the motornervous system.

    Topics: Acetylcholine; Action Potentials; Amino Acid Sequence; Animals; Ascaris suum; Female; FMRFamide; Helminth Proteins; Molecular Sequence Data; Muscles; Nematoda; Neuropeptides; Nicotinic Antagonists; Quaternary Ammonium Compounds; Receptors, Nicotinic; Synapses; Synaptic Transmission

1995
Neuropeptides regulate the cardiac activity of a prosobranch mollusc, Rapana thomasiana.
    Cell and tissue research, 1992, Volume: 269, Issue:2

    Involvement of neuropeptides in the regulation of cardiac activity in a prosobranch mollusc, Rapana thomasiana, was studied physiologically as well as immunohistochemically. A catch-relaxing peptide (CARP) showed strong inhibitory effects on the heart with a lower threshold than acetylcholine. The action of CARP was in contrast to that of another neuropeptide, FMRFamide, which has previously been shown to enhance the heart beat. Benzoquinonium blocked the effects of acetylcholine and stimulation of right cardiac nerves 1 and 3 b, but not those of CARP, suggesting that the effects of nerve stimulation are mainly due to the release of acetylcholine. Immunohistochemical examinations demonstrated that FMRFamide-like and CARP-like immunoreactive neurons are distributed in the visceral ganglia. Although a neuron appeared to show weak immunoreactivity to both antisera, evidence for the coexistence of peptides in a single neuron was not exhibited. Positive immunoreactivity to FMRFamide and CARP antisera also appeared in right cardiac nerves 1 and 3. In the heart, FMRFamide- and CARP-like immunoreactive fibers were restricted to the atrium and the aortic end of the ventricle, consistent with the morphological observation of innervation. The present results suggest that FMRFamide- and CARP-like peptides are involved in regulating the heart beat.

    Topics: Acetylcholine; Amino Acid Sequence; Animals; Cardiotonic Agents; FMRFamide; Heart; Immunohistochemistry; Invertebrate Hormones; Molecular Sequence Data; Mollusca; Neuropeptides; Oligopeptides; Quaternary Ammonium Compounds; Sequence Homology

1992