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Physiological effects of platyhelminth RFamide peptides on muscle-strip preparations of Fasciola hepatica (Trematoda: Digenea)

Published online by Cambridge University Press:  06 April 2009

N. J. Marks*
Affiliation:
Animal Health Discovery Research, Pharmacia & Upjohn Inc., Kalamazoo, Michigan, MI 49001, USA
S. Johnson
Affiliation:
Animal Health Discovery Research, Pharmacia & Upjohn Inc., Kalamazoo, Michigan, MI 49001, USA
A. G. Maule
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen’s University of Belfast, Belfast BT7 1NN, Northern Ireland, UK
D. W. Halton
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen’s University of Belfast, Belfast BT7 1NN, Northern Ireland, UK
C. Shaw
Affiliation:
Comparative Neuroendocrinology Research Group, The Queen’s University of Belfast, Belfast BT7 1NN, Northern Ireland, UK
T. G. Geary
Affiliation:
Animal Health Discovery Research, Pharmacia & Upjohn Inc., Kalamazoo, Michigan, MI 49001, USA
S. Moore
Affiliation:
Penninsula Laboratories (Europe) Limited, St Helens, Merseyside WA9 3AJ, UK
D. P. Thompson
Affiliation:
Animal Health Discovery Research, Pharmacia & Upjohn Inc., Kalamazoo, Michigan, MI 49001, USA
*
*Corresponding author. School of Clinical Medicine, Mulhouse Building, The Queen’s University of Belfast, Royal Victoria Hospital Site, Grosvenor Road, Belfast BT12 6BJ, Northern Ireland. Tel: 01232 240503 ext. 2730. Fax: 01232 329899.

Summary

The effects of each of the known platyhelminth neuropeptides were determined on muscle-strip preparations from the liver fluke, Fasciola hepatica. The activity of synthetic replicates of the C-terminal nonapeptide of neuropeptide F (NPF9, Moniezia expansa), and the FMRFamide-related peptides (FaRPs), GNFFRFamide, RYIRFamide, GYIRFamide and YIRFamide, were examined. Muscle-strip activity was recorded from 1 mm segments of muscle prepared from 28 to 32-day-old worms, using a photo-optic transducer system. None of the peptides ( 10 μM) altered baseline tension significantly; however, each of the peptides increased the amplitude and frequency of muscle contraction. The threshold for activity of each of the peptides examined was, respectively, 1 nM (RYIRFamide), 0·3 μM (GYIRFamide and YIRFamide), and 10 μM (GNFFRFamide and NPF9). All of the effects were reversible and repeatable, following wash-out. Muscle-strip integrity was tested following experimentation, using arecoline (10 μM) and high-K+ bathing medium (90 mM K+).

Type
Research Article
Copyright
Copyright © Cambridge University Press 1996

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