The University of Southampton
University of Southampton Institutional Repository

Physiological actions of putative neuropeptides in the nematode Ascaris suum

Physiological actions of putative neuropeptides in the nematode Ascaris suum
Physiological actions of putative neuropeptides in the nematode Ascaris suum
Neuropeptide-like immunoreactivity has a widespread distribution in the nematode nervous system (Sithigorngul et al. 1990) and sequences of more than 150 neuropeptides have been predicted from the genomes of C. elegans (Nelson et al. 1998; Nathoo et al. 2001). Here we report a preliminary assessment of the biological activity of six of these on the somatic muscle of the parasitic nematode A. suum. Three of these are encoded by flp (FMRFamide-like peptides) genes and three by nlp (neuropeptide-like precursor) genes. Two of the latter show some sequence similarity to myomodulin, and one to buccalin, molluscan neuropeptides.
The effect of the peptides on the body wall muscle of A. suum was determined using an in vitro preparation of dorsal muscle strips as described by Trim et al. (1997). A 1 cm section of muscle was placed in an organ bath attached to an isometric transducer and perfused with artificial perienteric fluid (composition (mM): NaCl 67, sodium acetate 67, MgCl2 5.6, CaCl2 3, KCl 3, Tris-Cl 5; pH 7.6). The excitatory neuromuscular junction transmitter acetylcholine (ACh; 10 µM) was added for 1 min and then washed out. This elicited a rapid and reversible contraction. This was repeated twice to obtain contractions of reproducible amplitude. Subsequently the neuropeptide was added to the preparation 2 min prior to ACh, and the amplitude of the contraction to ACh in the presence of the peptide was expressed as a percentage of the average amplitude of the three contractions prior to the addition of neuropeptide. None of the neuropeptides had a marked effect on basal muscle tension. However, three had a potent effect on the contraction elicited by ACh, with two acting as inhibitors and one as a potentiator. The results are summarised in Table 1.
In conclusion, all three of the RF-amide neuropeptides had potent effects, and one of the myomodulin-like peptides had a weak inhibitory action. Further studies are in progress to assess the activity of these peptides in C. elegans.
0022-3751
3P-4P
Papaioannou, S.
159597af-6939-4e2a-a491-fd722e2175cf
Holden-Dye, L.
8032bf60-5db6-40cb-b71c-ddda9d212c8e
Walker, R.J.
b6597591-587e-488a-8a54-89156c42ce8d
Papaioannou, S.
159597af-6939-4e2a-a491-fd722e2175cf
Holden-Dye, L.
8032bf60-5db6-40cb-b71c-ddda9d212c8e
Walker, R.J.
b6597591-587e-488a-8a54-89156c42ce8d

Papaioannou, S., Holden-Dye, L. and Walker, R.J. (2002) Physiological actions of putative neuropeptides in the nematode Ascaris suum. Journal of Physiology, 543 (225), 3P-4P.

Record type: Article

Abstract

Neuropeptide-like immunoreactivity has a widespread distribution in the nematode nervous system (Sithigorngul et al. 1990) and sequences of more than 150 neuropeptides have been predicted from the genomes of C. elegans (Nelson et al. 1998; Nathoo et al. 2001). Here we report a preliminary assessment of the biological activity of six of these on the somatic muscle of the parasitic nematode A. suum. Three of these are encoded by flp (FMRFamide-like peptides) genes and three by nlp (neuropeptide-like precursor) genes. Two of the latter show some sequence similarity to myomodulin, and one to buccalin, molluscan neuropeptides.
The effect of the peptides on the body wall muscle of A. suum was determined using an in vitro preparation of dorsal muscle strips as described by Trim et al. (1997). A 1 cm section of muscle was placed in an organ bath attached to an isometric transducer and perfused with artificial perienteric fluid (composition (mM): NaCl 67, sodium acetate 67, MgCl2 5.6, CaCl2 3, KCl 3, Tris-Cl 5; pH 7.6). The excitatory neuromuscular junction transmitter acetylcholine (ACh; 10 µM) was added for 1 min and then washed out. This elicited a rapid and reversible contraction. This was repeated twice to obtain contractions of reproducible amplitude. Subsequently the neuropeptide was added to the preparation 2 min prior to ACh, and the amplitude of the contraction to ACh in the presence of the peptide was expressed as a percentage of the average amplitude of the three contractions prior to the addition of neuropeptide. None of the neuropeptides had a marked effect on basal muscle tension. However, three had a potent effect on the contraction elicited by ACh, with two acting as inhibitors and one as a potentiator. The results are summarised in Table 1.
In conclusion, all three of the RF-amide neuropeptides had potent effects, and one of the myomodulin-like peptides had a weak inhibitory action. Further studies are in progress to assess the activity of these peptides in C. elegans.

This record has no associated files available for download.

More information

Published date: 1 October 2002
Organisations: Biological Sciences

Identifiers

Local EPrints ID: 56092
URI: http://eprints.soton.ac.uk/id/eprint/56092
ISSN: 0022-3751
PURE UUID: a1ed2eca-9525-459f-b0d1-9c1ec8baef02
ORCID for L. Holden-Dye: ORCID iD orcid.org/0000-0002-9704-1217

Catalogue record

Date deposited: 11 Aug 2008
Last modified: 12 Dec 2021 02:34

Export record

Contributors

Author: S. Papaioannou
Author: L. Holden-Dye ORCID iD
Author: R.J. Walker

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×