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Journal of Comparative Physiology B

, Volume 158, Issue 6, pp 771–777 | Cite as

Evidence for glycolytic enzyme binding during anaerobiosis of the foot muscle ofPatella caerulea (L.)

  • A. Lazou
  • B. Michaelidis
  • Is. Beis
Article

Summary

The effect of anaerobiosis and aerobic recovery on the degree of binding of glycolytic enzymes to the particulate fraction of the cell was studied in the foot muscle of the marine molluscP. caerulea, in order to assess the role of glycolytic enzyme binding in the metabolic transition between aerobic and anoxic states. Short periods of anoxia (2 h, 4 h) resulted in an increase in enzyme binding in association with the increased glycolytic rate observed; this was particularly pronounced for phosphorylase, phosphofructokinase, aldolase, pyruvate kinase and lactate dehydrogenase. Decreased enzyme binding was observed after prolonged periods of anoxia. These effects were reversed and control values re-established when animals were returned to aerobic conditions. The results suggest that glycolytic rate could be regulated by changes in the distribution of glycolytic enzymes between free and bound forms inP. caerulea foot muscle. This reversible interaction of glycolytic enzymes with structural proteins may constitute an additional mechanism for metabolic control.

Keywords

Lactate Pyruvate Human Physiology Lactate Dehydrogenase Aerobic Condition 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Abraham S, Fitch WM, Chaikoff IL (1961) Mannose metabolism and the demonstration of mannokinase and phosphomannoisomerase activities in the lactating rat mammary gland. Arch Biochem Biophys 93:278–282Google Scholar
  2. Arnold H, Pette D (1968) Binding of glycolytic enzymes to structure proteins of the muscle. Eur J Biochem 6:163–171Google Scholar
  3. Arnold H, Pette D (1970) Binding of aldolase and triosephosphate dehydrogenase to F-actin and modification of catalytic properties of aldolase. Eur J Biochem 15:360–366Google Scholar
  4. Bergmeyer UH, Bernt E, Möllering H, Pfleiderer G (1974) L-Aspartate and L-Asparagine. In: Bergmeyer HU (ed) Methods of enzymatic analysis, vol 4. Academic Press, New York, pp 1696–1700Google Scholar
  5. Bronstein WW, Knull HR (1981) Interaction of muscle glycolytic enzymes with thin filament proteins. Can J Biochem 59:494–499Google Scholar
  6. Burleigh IG, Schimke RT (1968) On the activities of some enzymes concerned with glycolysis and glycogenolysis in extracts of rabbit skeletal muscles. Biochem Biophys Res Commun 31:831–836Google Scholar
  7. Chapman RG, Hennessey MA, Waltersdorph AM, Hunnekens FM, Cabrio BW (1962) Erythrocyte metabolism. V Levels of glycolytic enzymes and regulation of glycolysis. J Clin Invest 41:1249–1256Google Scholar
  8. Clarke FM, Masters CJ (1972) On the reversible and selective adsorption of aldolase isoenzymes in rat brain. Arch Biochem Biophys 153:258–265Google Scholar
  9. Clarke FM, Masters CJ (1975) On the association of glycolytic enzymes with structural proteins of skeletal muscle. Biochim Biophys Acta 381:37–46Google Scholar
  10. Clarke FM, Shaw FD, Morton DJ (1980) Effect of electrical stimulationpost mortem on bovine muscle on the binding of glycolytic enzymes. Biochem J 186:105–109Google Scholar
  11. Clarke FM, Stephan P, Huxham G, Hamilton D, Morton DJ (1984) Metabolic dependence of glycolytic enzyme binding in rat and sheep heart. Eur J Biochem 138:643–649Google Scholar
  12. Ebberink RHM, Zwaan A de (1980) Control of glycolysis in the posterior adductor muscle of the sea musselMytilus edulis. J Comp Physiol 137:165–171Google Scholar
  13. Ebberink RHM, Zurburg W, Zandee DI (1979) The energy demand of the posterior adductor muscle ofMytilus edulis in catch during exposure to air. Mar Biol Lett 1:23–31Google Scholar
  14. Fields JHA (1983) Alternatives to lactic acid: possible advantages. J Exp Zool 228:445–457Google Scholar
  15. Gäde C (1983) Energy metabolism of arthropods and molluscs during environmental and functional anaerobiosis. J Exp Zool 228:415–429Google Scholar
  16. Hochachka PW, Somero GN (1984) Biochemical adaptation. Princeton University Press, Princeton, NJ, pp 145–181Google Scholar
  17. Hohorst HJ (1965)l-(+) Lactate determination with lactate dehydrogenase and DPN. In: Bergmeyer HU (ed) Methods of enzymatic analysis. Academic Press, New York, pp 266–270Google Scholar
  18. Knull HR (1978) Association of glycolytic enzymes with particulate fractions from nerve endings. Biochim Biophys Acta 522:1–9Google Scholar
  19. Knull HR, Taylor WF, Wells WW (1973) Effects of energy metabolism on in vivo distribution of hexokinase in brain. J Biol Chem 248:5414–5418Google Scholar
  20. Knull HR, Bronstein WW, Desjardin P, Niehaus WG (1980) Interaction of selected brain glycolytic enzymes with an F-actin-tropomyosin complex. J Neurochem 34:222–225Google Scholar
  21. Liu RS, Anderson S (1980) Activation of rabbit muscle phosphofructokinase phofructokinase by F-actin and reconstituted thin filaments. Biochemistry 19:2684–2688Google Scholar
  22. Livingstone DR, Zwaan A de (1983) Carbohydrate metabolism of gastropods. In: Wilbur KM (ed) The Molusca, vol 1. Academic Press, New York, pp 177–242Google Scholar
  23. Luther MA, Lee JC (1986) The role of phosphorylation in the interaction of rabbit muscle phosphofructokinase with F-actin. J Biol Chem 261:1753–1759Google Scholar
  24. Masters CJ (1977) Metabolic control and the microenvironment. In: Horecker BL, Stadtman ER (eds) Current topics in cellular regulation, vol 12, pp 75–105Google Scholar
  25. Masters CJ (1978) Interactions between soluble enzymes and subcellular structure. Trends Biochem Sci 3:206–208Google Scholar
  26. Masters CJ (1985) Phosphofructokinase, compartmentation and the regulation of glycolysis. Trends Biochem Sci 10:189Google Scholar
  27. Michaelidis B (1984) Study on the energy metabolism in the foot muscle of the sea molluscPatella caerulea (L.). Doctorate thesis, University of Thessaloniki, Thessaloniki, GreeceGoogle Scholar
  28. Michaelidis B, Gaitanaki C, Beis I (in press) Modification of pyruvate kinase from the foot muscle ofP. caerulea (L.) during anaerobiosis. J Exp ZoolGoogle Scholar
  29. Michal G, Beutler HO, Lang G, Guentnes U (1976) Enzymatic determination of succinic acid in foods stuffs. Z. Analyt Chem 279:137–138Google Scholar
  30. Moses F (1978) Compartmentation of glycolysis inEscherichia coli. In: Stere PA, Estabrook RW (eds) Microenvironments and microcompartmentation. Academic Press, New York, pp 169–184Google Scholar
  31. Nemat-Gorgani M, Wilson JE (1980) Ambiquitous behavior — A biological phenomenon of general significance. In: Horecker BL, Stadtman ER (eds) vol 16. Academic Press, New York, pp 45–54Google Scholar
  32. Opie LH, Newsholme EA (1967) The activities of fructose-1,6-disphosphatase, phosphofructokinase and phosphoenolpyruvate carboxykinase in white and red muscle. Biochem J 103:391–399Google Scholar
  33. Plaxton WC, Storey KB (1986) Glycolytic enzyme binding and metabolic control in anaerobiosis. J Comp Physiol B 156:635–640Google Scholar
  34. Ross RE, Hultin HO (1980) A study of binding-solubilization of some glycolytic enzymes in striated muscle in situ. J Cell Physiol 105:409–416Google Scholar
  35. Taylor JF (1955) Aldolase from muscle. In: Colowick SP, Kaplan NO (eds) Methods in enzymology, vol I. Academic Press, New York, pp 310–315Google Scholar
  36. Ureta T (1978) The role of isozymes in metabolism: a model of metabolic pathways as the basis for the biological role of isozymes. In: Horecker BL, Stadtman ER (eds) Current topics in cellular regulation, vol 13. Academic Press, New York, pp 233–258Google Scholar
  37. Walsh TP, Winzor DJ, Clarke FM, Masters CJ, Morton DJ (1980) Binding of aldolase to actin-containing filaments: evidence of interaction with the regulatory proteins of skeletal muscle. Biochem J 186:89–98Google Scholar
  38. Walsh TP, Masters CJ, Morton DJ, Clarke FM (1981) The reversible binding of glycolytic enzymes in ovine skeletal muscles in response to tetanic stimulation. Biochim Biophys Acta 675:29–39Google Scholar
  39. Ward CW, Schofield PJ (1967) Glycolysis inHaemonchus contortus larvae and rat liver. Comp Biochem Physiol 22:33–52Google Scholar
  40. Ward CW, Castro GA, Fairbairn D (1969) Carbon dioxide fixation and phosphoenolpyruvate metabolism inTrichinella spiralis larvae. J Parasitol 55:67–71Google Scholar
  41. Westrin H, Backman L (1983) Association of rabbit muscle glycolytic enzymes with filamentous actin: a counter-current distribution study at high ionic strength. Eur J Biochem 136:407–411Google Scholar
  42. Williamson DH (1974)l-Alanine. Determination with alanine dehydrogenase. In: Bergmeyer HU (ed) Methods of enzymatic analysis. Academic Press, New York, pp 1679–1682Google Scholar
  43. Wilson JE, Reid S, Masters CJ (1982) A comparative study of the binding of aldolase and glyceraldehyde-3-phosphate dehydrogenase to the human erythrocyte membrane. Arch Biochem Biophys 215:610–620Google Scholar
  44. Zwaan A de (1983) Carbohydrate metabolism in bivalves. In: Wilbur KM (ed) The Mollusca, vol 1. Academic Press, New York, pp 137–175Google Scholar
  45. Zwaan A de, Wijsman TCM (1976) Anaerobic metabolism in Bivalvia (Mollusca): characteristics of anaerobic metabolism. Comp Biochem Physiol 54B:313–324Google Scholar

Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • A. Lazou
    • 1
  • B. Michaelidis
    • 1
  • Is. Beis
    • 1
  1. 1.Laboratory of Animal Physiology, Science SchoolUniversity of ThessalonikiThessalonikiGreece

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