Hostname: page-component-cd9895bd7-q99xh Total loading time: 0 Render date: 2024-12-25T15:52:14.421Z Has data issue: false hasContentIssue false
  • English
  • Français

A vasoactive intestinal polypeptide-like protein excreted/secreted by Nippostrongylus brasiliensis and its effect on contraction of uninfected rat intestine

Published online by Cambridge University Press:  06 April 2009

N. Foster  and
D. L. Lee
N. Foster
Affiliation:
Department of Pure and Applied Biology, The University of Leeds, Leeds LS2 9JT
D. L. Lee
Affiliation:
Department of Pure and Applied Biology, The University of Leeds, Leeds LS2 9JT
Get access Rights & Permissions [Opens in a new window]

Summary

The 50–30 kDa fraction isolated from the excretory/secretory products (E/S) of the nematode Nippostrongylus brasiliensis significantly decreased the amplitude of contraction of segments of uninfected rat intestine when injected into the lumen of the segments maintained in an organ bath. Dot blot analysis of the fraction suggested that it was similar in immuno-reactivity to porcine vasoactive intestinal polypeptide (VIP). When antiserum to porcine VIP was mixed with N. brasiliensis E/S and the mixtures were injected into the lumen of segments of rat intestine, the inhibitory effect of the E/S on amplitude of contraction decreased. When physiological concentrations of porcine VIP (12·9 pmol/ml) were injected into the lumen of segments of uninfected rat intestine the amplitude of contraction decreased significantly. Western blot analysis of the E/S, using antiserum to porcine VIP, recognized a 30 kDa protein in the E/S and also in whole worm homogenate suggesting that synthesis of the peptide occurs inside the nematode. Peptide histidine isoleucine (PHI)-like immuno-reactivity was detected in a 68 kDa fraction of the E/S and the homogenate but this fraction did not affect the amplitude of contractions of the intestine.

Keywords

biochemical holdfastexcretions/secretionsintestinal motilityNippostrongylusvasoactive intestinal polypeptidepeptide histidine isoleucine.
Type
Research Article
Information
Parasitology , Volume 112 , Issue 1 , January 1996 , pp. 97 - 104
Copyright
Copyright © Cambridge University Press 1996

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Anagnostides, A. A., Christofides, N. D., Bloom, S. R. & Chadwick, V. S. (1983). Peptide histidine isoleucine inhibits biliary but not pancreatic secretion in man. Clinical Science 65, 40.CrossRefGoogle Scholar
Bitar, K. N. & Makhlouf, G. M. (1982). Relaxation of isolated gastric smooth muscle cells by vasoactive intestinal peptide. Science 216, 531–3.CrossRefGoogle ScholarPubMed
Brennan, L. J., McLoughlin, T. A., Mutt, V., Tatemoto, K. & Wood, J. R. (1982). Effects of PH1, a newly isolated peptide, on gallbladder function in the guinea pig. Journal of Physiology 329, 71–2.Google Scholar
Castro, G. A., Badiel-aceves, F., Smith, J. W., Dudrick, S. J. & Weibrodt, N. W. (1976). Altered small bowel propulsion associated with parasitism. Gastroenterology 71, 620–5.CrossRefGoogle ScholarPubMed
Christofides, N. D., Yiangou, Y., Piper, P. J.Ghatei, M. A., Tatemoto, K., Polak, J. M. & Bloom, S. R. (1982). Distribution of PHI in the mammalian respiratory tract and some aspects of its pharmacology. Regulatory Peptides 4, 359.CrossRefGoogle Scholar
Costa, M. & Furness, J. B. (1983). The originations, pathways and terminations of neurons with VIP-like immunoreactivity in the guinea pig small intestine. Neuroscience 8, 665–76.CrossRefGoogle ScholarPubMed
Crosthwaite, A. I. P., Huizinga, J. D. & Fox, J. E. (1990). Jejunal circular muscle motility is decreased in nematode infected rat. Gastroenterology 98, 59–65.CrossRefGoogle ScholarPubMed
D'amato, M., De Beurme, F. A. & Lefebvre, R. A. (1988). Comparison of the effect of vasoactive intestinal polypeptide and non-adrenergic non-cholinergic neurone stimulation in the cat gastric fundus. European Journal of Pharmacology 152, 71–82.CrossRefGoogle ScholarPubMed
Foster, N., Deane, E. J. & Lee, D. L. (1994). The effect of homogenates and excretory/secretory products of Nippostrongylus brasiliensis and of acetylcholinesterase on the amplitude and frequency of contraction of uninfected rat intestine in vitro. Parasitology 108, 453–9.CrossRefGoogle ScholarPubMed
Fox, M. T., Gerreli, D., Pitts, S. R. & Jacobs, D. E. (1989). Ostertagia ostertagi infection in the calf: effects of trickle challenge on appetite, digestibility, rate of passage of digesta and liveweight gain. Research in Veterinary Science 47, 294–8.CrossRefGoogle ScholarPubMed
Gregory, P. C., Wenham, G., Poppi, D., Coop, R. L., Mcrae, J. C. & Miller, S. J. (1985). The influence of a chronic subclinical infection of Trichostrongylus colubriformis on gastro-intestinal motility and digesta flow in sheep. Parasitology 91, 381–96.CrossRefGoogle Scholar
Grider, J. R. & Rivier, J. R. (1990). Vasoactive intestinal polypeptide (VIP) as transmitter of inhibitory motor neurones of the gut: evidence from the use of selective VIP antagonists and VIP antiserum. Journal of Pharmacology and Experimental Therapeutics 253, 738–42.Google ScholarPubMed
Izzo, R. S., Scipione, R. A., Pellecchia, C. & Lokchander, R. (1991). Binding and internalization of VIP in rat intestinal epithelium cells. Regulatory Peptides 33, 21–30.CrossRefGoogle Scholar
Konturek, S. J., Schmidt, W. E., Mutt, V., Konturek, J. W. & Creutzfeldt, W. (1987). Valosin stimulates gastric and exocrine pancreatic secretions and inhibits fasting small intestine myoelectric activity in the dog. Gastroenterology 92, 1181–6.CrossRefGoogle ScholarPubMed
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227, 680–5.CrossRefGoogle ScholarPubMed
Lee, D. L. (1970). The fine structure of the excretory system in adult Nippostrongylus brasiliensis (Nematoda) and a suggested function for the ‘excretory glands’. Tissue and Cell 2, 225–31.CrossRefGoogle Scholar
Nishizawa, M., Hayakawa, Y., Yanaihara, N. & Okamoto, H. (1985). Nucleotide sequence divergence and functional constraint in VIP mRNA evolution between human and rat. FEBS Letters 183, 55–9.CrossRefGoogle ScholarPubMed
Ogilvie, B. M. & Jones, V. E. (1971). Nippostrongylus brasiliensis: a review of immunity and the host-parasite relationship in the rat. Experimental Parasitology 29, 138–77.CrossRefGoogle ScholarPubMed
Racusen, L. C. & Binder, H. J. (1977). Adrenergic interaction with ion transport across colonic mucosa: role of both alpha and beta adrenergic agonist. In Mechanisms of Intestinal Secretion (ed. Binder, H.), pp. 201–15. New York: A. R. Liss.Google Scholar
Savin, K. W., Dopheideide, T. A. A., Frenkel, M. J., Wagland, B. M., Warwick, N. G. & Ward, C. W. (1990). Characterization, cloning and host-protective activity of a 30 kilodalton glycoprotein secreted by the parasitic stages of Trichostrongylus colubriformis. Molecular and Biochemical Parasitology 41, 167–76.CrossRefGoogle ScholarPubMed
Sithigorngul, P., Stretton, A. O. W. & Cowden, C. (1990). Neuropeptide diversity in Ascaris: an immunocytochemical study. Journal of Comparative Neurology 294, 362–76.CrossRefGoogle ScholarPubMed
Symons, L. E. A. (1966). Digestion and absorption of maltose in rats infected with the nematode Nippostrongylus brasiliensis. Experimental Parasitology 18, 12–24.CrossRefGoogle ScholarPubMed
Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences, USA 76, 4350–4.CrossRefGoogle ScholarPubMed
Voller, A. (1980). Heterogeneous enzyme-immunoassays and their applications. In Enzyme Assays (ed. Maggio, E. T.), pp. 181–96. Boca Raton, Florida: CRC Press.Google Scholar
Wood, J. R., Brennan, L. J., McLoughlin, T. A., Tatemoto, K. & Mutt, V. (1982). Comparison of the effects of natural and synthetic PHI on gallbladder fluid transport. Regulatory Peptides 4 383CrossRefGoogle Scholar