Hostname: page-component-76fb5796d-22dnz Total loading time: 0 Render date: 2024-04-25T11:23:45.125Z Has data issue: false hasContentIssue false
  • English
  • Français

Mitochondrial adenosine triphosphatase activity and temperature adaptation in Schistocephalus solidus (Cestoda: Pseudophyllidea)

Published online by Cambridge University Press:  06 April 2009

R. W. Walker  and
J. Barrett
R. W. Walker
Affiliation:
Department of Zoology, University College of Wales, Aberystwyth, Dyfed SY23 3DA
J. Barrett
Affiliation:
Department of Zoology, University College of Wales, Aberystwyth, Dyfed SY23 3DA
Get access Rights & Permissions [Opens in a new window]

Summary

During its life-cycle, the cestode Schistocephalus solidus is parasitic in both an ectotherm (Gasterosteus aculeatus) and an endotherm (Gallus domesticus) host, and so provides an excellent model with which to study temperature adaptation in parasites. A mitochondrial fraction was prepared from the adults and plerocercoids of S. solidus and from their respective hosts; the activities of the mitochondrial adenosine triphosphatase (ATPase) were then measured over the temperature range 1–45 °C. The plerocercoids of S. solidus show evidence of immediate temperature compensation; this would provide a mechanism for withstanding the abrupt temperature change experienced during infection of the final host. Analysis of the Michaelis constant data suggests that variation of Km, a with temperature may be a major factor in this immediate temperature compensation. In response to acclimation at 5 and 19°C, plerocercoid ATPase showed inverse or paradoxical rate compensation, as did the enzyme from the fish host. Acclimation at the two temperatures had no effect on the Q10 or on the linearity of the Arrhenius plots for the plerocercoid mitochondrial ATPase and only a small effect on the Km a. Acclimation of the fish host again had only a small effect on the Km, a of the fish mitochondrial ATPase but, in contrast to the plerocercoid, there was also a significant effect on the Q10 and the Arrhenius plots. Adult S. solidus ATPase showed partial rate compensation and had a biphasic Arrhenius plot, suggesting that after infection there had been a change in the enzyme or its micro-environment. In terms of the effect of temperature on the Q10 amd Km, a and in the biphasic nature of the Arrhenius plot, the mitochondrial ATPase of adult S. solidus showed similarities with the enzyme from its bird host.

Type
Research Article
Information
Parasitology , Volume 87 , Issue 2 , October 1983 , pp. 307 - 326
Copyright
Copyright © Cambridge University Press 1983

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

Ames, B. N. (1966). Assay of inorganic phosphate, total phosphate and phosphatases. In Methods in Enzymology, vol. 8 (ed. Neufeld, E. F. and Ginsberg, V.), pp. 115–18. New York: Academic Press.Google Scholar
Barrett, J. & Fairbairn, D. (1971). Effects of temperature on the kinetics of malate dehydrogenase in the developing eggs and adult muscle of Ascaris lumbricoides (Nematoda). Journal of Experimental Zoology 176, 169–78.CrossRefGoogle ScholarPubMed
Cain, G. D. & Fairbairn, D. (1971). Protocollagen proline hydroxylase and collagen synthesis in developing eggs of Ascaris lumbricoides. Comparative Biochemistry and Physiology 40 B, 165–79.Google ScholarPubMed
Davies, P. S. & Walkey, M. (1966). The effect of body size and temperature upon oxygen consumption of the cestode Schistocephalvs solidus (Müller). Comparative Biochemistry and Physiology 18, 415–25.CrossRefGoogle ScholarPubMed
Dixon, M. & Webb, E. C. (1964). Enzymes. London: Longmans.Google Scholar
Dowd, J. E. & Riggs, D. S. (1965). A comparison of estimates of Michaelis–Menten kinetic constants from various linear transformations. Journal of Biological Chemistry 240, 863–9.CrossRefGoogle ScholarPubMed
Glock, G. E. & McLean, P. (1953). Further studies on the properties and assay of glucose-6-phosphate dehydrogenase and 6-phospho-gluconate dehydrogenase of rat liver. Biochemical Journal 55, 400–8.CrossRefGoogle Scholar
Hazel, J. R. & Prosser, C. L. (1974). Molecular mechanisms of temperature compensation in poikilotherms. Physiological Reviews 54, 620–77.CrossRefGoogle ScholarPubMed
Hochachka, P. W. & Somero, G. N. (1973). Strategies of Biochemical Adaptation. Philadelphia: Saunders.Google Scholar
Johnston, I. A. & Goldspink, G. (1975). Thermodynamic activation parameters of fish myofibrillar ATPase enzyme and evolutionary adaptations to temperature. Nature, London 257, 620–2.CrossRefGoogle ScholarPubMed
Kanungo, M. S. & Prosser, C. L. (1959). Physiological and biochemical adaptation of goldfish to cold and warm temperatures. 1. Standard and active oxygen consumptions of cold- and warm-acclimated goldfish at various temperatures. Journal of Cellular and Comparative Physiology 54, 259–63.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–75.CrossRefGoogle ScholarPubMed
Lyons, J. M. & Raison, J. K. (1970). A temperature-induced transition in mitochondrial oxidation: contrasts between cold and warm blooded animals. Comparative Biochemistry and Physiology 37, 405–11.CrossRefGoogle Scholar
Massey, V. (1953). Studies on fumarase. 3. The effect of temperature. The Biochemical Journal 53, 72–9.CrossRefGoogle Scholar
McCaig, M. L. O.& Hopkins, C. A. (1963). Studies on Schistocephalus solidus. II. Establishment and longevity in the definitive host. Experimental Parasitology 13, 273–83.CrossRefGoogle ScholarPubMed
McMurchie, E. J., Raison, J. K. & Cairncross, K. D. (1973). Temperature-induced phase changes in membrane of heart: a contrast between the thermal response of poikilotherms and homeotherms. Comparative Biochemistry and Physiology 44 B, 1017–26.Google Scholar
Metzger, H. & Düwel, D. (1973). Investigations of metabolism in the liver fluke (Fasciolahepatica) as an aid to the development of new anthelmintics. International Journal of Biochemistry 4, 133–43.CrossRefGoogle Scholar
Precht, H. (1958). Concepts of the temperature adaptation of unchanging reaction systems of cold-blooded animals. In Physiological Adaptation (ed. Prosser, C. L.), pp. 50–78. Washington, D.C.: American Physiological Society.Google Scholar
Pye, V. (1973). Acute temperature change and the oxidation rates of ectotherm mitochondria. In Effects of Temperature on Ectothermic Organisms (ed. Wieser, W.), pp. 83–95. Berlin: Springer-Verlag.CrossRefGoogle Scholar
Rao, K. P. & Bullock, T. H. (1954). Q10 as a function of size and habitat temperature in poikilotherms. American Naturalist 88, 33–44.CrossRefGoogle Scholar
Sizer, I. W. & Josephson, E. S. (1942). Kinetics as a function of temperature of lipase, trypsin, and invertase activity from –70 to 50 °C (–94 to 122 °F). Food Research 7, 201–9.CrossRefGoogle Scholar
Smith, C. L. (1973). The temperature dependence of oxidative phosphorylation and of the activity of various enzyme systems in liver mitochondria from cold- and warm-blooded animals. Comparative Biochemistry and Physiology 46 B, 445–61.Google ScholarPubMed
Smyth, J. D. (1946). Studies on tapeworm physiology. I. The cultivation of Schistocephalus solidus in vitro. Journal of Experimental Biology 23, 47–50.CrossRefGoogle ScholarPubMed
Smyth, J. D. (1969). The Physiology of Cestodes. Edinburgh: Oliver & Boyd.Google Scholar
Somero, G. N. (1969). Enzymic mechanisms of temperature compensation: immediate and evolutionary effects of temperature on enzymes of aquatic poikilotherms. American Naturalist 103, 517–30.CrossRefGoogle Scholar
Vernberg, W. B. (1961). Studies on oxygen consumption in digenetic trematodes. VI. The influence of temperature on larval trematodes. Experimental Parasitology 11, 270–5.CrossRefGoogle ScholarPubMed
Vernberg, W. B. & Hunter, W. S. (1961). Studies on oxygen consumption in digenetic trematodes. V. The influence of temperature on three species of adult trematodes. Experimental Parasitology 11, 34–8.CrossRefGoogle ScholarPubMed
Wilkinson, G. N. (1961). Statistical estimations in enzyme kinetics. The Biochemical Journal 80, 324–32.CrossRefGoogle ScholarPubMed
Wodtke, E. (1976). Discontinuities in the Arrhenius plots of mitochondrial membrane-bound enzyme systems from a poikilotherm: acclimation temperature of carp affects transition temperatures. Journal of Comparative Physiology 110 B, 145–57.CrossRefGoogle Scholar