title: Expression and bioactivity of allatostatin-like neuropeptides in helminths.
abstract: Allatostatins are the largest family of known arthropod neuropeptides. To date more than 150 different arthropod type-A allatostatins have been identified and are characterized by the C-terminal signature, (Y/F)XFG(L/I)amide. Using specific allatostatin antisera, positive immunoreactivity has been identified within the central and peripheral nervous systems of the flatworm (platyhelminth) Procerodes littoralis and the roundworm (nematode) Panagrellus redivivus. Comparative analyses of the allatostatin-like immunoreactivity and that of other known helminth neuropeptides (FMRFamide-like peptides [FLPs]) indicate differences in the distribution of these peptide families. Specific differences in neuropeptide distribution have been noted within the pharyngeal innervation of flatworms and in the cephalic papillary neurons of nematodes. In arthropods, type-A allatostatins have functions that include potent myoactivity. In this study, seven members of the allatostatin superfamily induced concentration-dependent contractions of flatworm muscle fibres. Pharmacological studies indicate that these peptides do not interact with muscle-based FLP receptors. The type-A allatostatins, therefore, represent the second family of neuropeptides that induce muscle contraction in flatworms. Although the majority of arthropod type-A allatostatins examined did not affect the somatic body wall muscle or the ovijector of the pig nematode, Ascaris suum, two type-A allatostatins (GDGRLYAFGLamide and DRLYSFGLamide) exhibited significant inhibitory effects on the A. suum ovijector at 10 microM. These data suggest that allatostatin-like peptides and receptors occur in helminths. Further, although arthropod type-A allatostatins display inter-phyla activities, their receptors are less compelling as potential targets for broad-spectrum parasiticides (endectocides) than FLP receptors.
authors.affiliation: Parasitology Research Group, School of Biology and Biochemistry, Queen's University Belfast, Medical Biology Centre, 97 Lisburn Road, Northern Ireland, UK. a.mousley@qub.ac.uk
authors.forename: Angela
authors.initials: A
authors.lastname: Mousley
authors.forename: Christy L
authors.initials: CL
authors.lastname: Moffett
authors.forename: Hanne
authors.initials: H
authors.lastname: Duve
authors.forename: Alan
authors.initials: A
authors.lastname: Thorpe
authors.forename: David W
authors.initials: DW
authors.lastname: Halton
authors.forename: Timothy G
authors.initials: TG
authors.lastname: Geary
authors.forename: David P
authors.initials: DP
authors.lastname: Thompson
authors.forename: Aaron G
authors.initials: AG
authors.lastname: Maule
authors.forename: Nikki J
authors.initials: NJ
authors.lastname: Marks
mesh_terms: D000818:Animals; D001200:Ascaris / Q000737:chemistry; D001681:Biological Assay; D005260:Female; D006376:Helminths / Q000737:chemistry*; D007150:Immunohistochemistry / Q000379:methods; D008297:Male; D018613:Microscopy, Confocal; D018485:Muscle Fibers, Skeletal / Q000737:chemistry; D009479:Neuropeptides / Q000032:analysis*; D010986:Platyhelminths / Q000737:chemistry; D018010:Receptors, Invertebrate Peptide
chemical_list: D009479:Neuropeptides; D018010:Receptors, Invertebrate Peptide; C076523:allatostatin