title: Parasitic peptides! The structure and function of neuropeptides in parasitic worms.
abstract: Parasitic worms come from two very different phyla-Platyhelminthes (flatworms) and Nematoda (roundworms). Although both phyla possess nervous systems with highly developed peptidergic components, there are key differences in the structure and action of native neuropeptides in the two groups. For example, the most abundant neuropeptide known in platyhelminths is the pancreatic polypeptide-like neuropeptide F, whereas the most prevalent neuropeptides in nematodes are FMRFamide-related peptides (FaRPs), which are also present in platyhelminths. With respect to neuropeptide diversity, platyhelminth species possess only one or two distinct FaRPs, whereas nematodes have upwards of 50 unique FaRPs. FaRP bioactivity in platyhelminths appears to be restricted to myoexcitation, whereas both excitatory and inhibitory effects have been reported in nematodes. Recently interest has focused on the peptidergic signaling systems of both phyla because elucidation of these systems will do much to clarify the basic biology of the worms and because the peptidergic systems hold the promise of yielding novel targets for a new generation of antiparasitic drugs.
authors.affiliation: Department of Pharmacology and Toxicology, Michigan State University, East Lansing 48824, USA. dayt@pilot.msu.edu
authors.forename: T A
authors.initials: TA
authors.lastname: Day
authors.forename: A G
authors.initials: AG
authors.lastname: Maule
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006376:Helminths / Q000737:chemistry*; D008969:Molecular Sequence Data; D009348:Nematoda / Q000737:chemistry*; D009479:Neuropeptides / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
chemical_list: D009479:Neuropeptides