Skip to main content
Log in

Changes in enzyme activity of glycogen and hexose metabolism during oocyte maturation in a teleost,Misgurnus fossilis L.

  • Published:
Wilhelm Roux' Archiv für Entwicklungsmechanik der Organismen Aims and scope Submit manuscript

Summary

The oocyte at the end of oogenesis, mature egg and developing embryo of the loachMisgurnus fossilis L.) are characterized by indentical enzyme profiles of the Embden-Meyerhof chain, pentose phosphate cycle and key gluconeogenic enzymes. However, the carbohydrate metabolism in the oocyte differs substantially from that in the embryo.

Oocyte maturation is followed by a complete loss of hexokinase (EC2.7.1.1),2-fold decrease of glycogen synthetase (EC 2.4.1.11) and 10-fold increase of glycogen phosphorylase (EC2.4.1.1) activity. This process is correlated with a gradual decrease of the ATP/(ADP+AMP) ratio from 4∶1 to 2∶1 and increase of the Fructose-6-Phosphate/Fructose-1,6-Diphosphate ratio from 0.27 to 2.0. Thus, oocyte maturation involves a number of changes in control mechanisms resulting in cessation of glycogen accumulation and a transition of carbohydrate metabolism from gluconeogenesis to glycogenolysis.

Zusammenfassung

Die Oozyte und das reife Ei vonMisgurnus fossilis L. besitzen die gleiche Enzymzusammensetzung der Embden-Meyerhof Wege, unterscheiden sich aber wesentlich in den Enzymen des Metabolismus des Glykogens und der Hexosemonophosphate. Beim Reifen der Oozyte erfolgt eine 10fache Zunahme der Aktivität der Phosphorylase (EC 2.4.1.1.), völliger Verlust der Hexokinase (EC 2.7.1.1.) und eine wesentliche Abnahme der Glycogensynthetase (EC 2.4.1.11).

Das Verhältnis ATP/(ADP+AMP)geht von 4∶l auf 2∶-1 zurück, dasjenige von Fructose-6-Phosphat/Fructose-1,6-Diphosphat nimmt von 0,27 auf 2,0 zu.

Änderungen der regulatorischen Mechanismen beim Reifen der Oozyte setzen die Geschwindigkeit der Glykogensynthese und Glukoneogenese scharf herab, unterbinden die Ausnutzung der freien Glukose bei der Glykolyse und sichert eine allmähliche Zunahme der Glykogenolyse während der frühen Entwicklung des Embryos.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Adam, H.: Adenosine diphosphat und Adenosine monophosphat. In: Bergmeyer H. U., Methoden der enzym. Analyse, p. 573–597. Weinheim: Verlag Chemie 1962.

    Google Scholar 

  • Ando, S.: Physiological study on egg formation of the fish. Embryologia (Nagoya)5, 239–246 (1960).

    Google Scholar 

  • Appleman, M., Krebs B. G., Fischer, E.: Purification and properties of inactive liver phosphorylase. Biochemistry5, 2101–2107 (1966).

    Google Scholar 

  • Atkinson, D. E.: Regulation of enzyme activity. Ann. Rev. Biochem.35, 85–123 (1966).

    Google Scholar 

  • Atkinson, D. E., Walton, G. M.: ATP conservation in metabolic regulation J. biol. Chem.242, 3239–3245 (1967).

    Google Scholar 

  • Ballard, F. J.: Adenine nucleotides and adenylate kinase equilibrium in livers of foetal and newborn rats. Biochem. J.117, 231–235 (1970).

    Google Scholar 

  • Beljaeva, V. N., Cherfas, N. B.: On the process of maturation in the ova of Misgurnus fossilis L. Problems of Ichtiology5, 13–29 (1965) [In Russian].

    Google Scholar 

  • Bergmeyer, H. U.: Methoden in der enzym. Analyse, p. 5–70. Weinheim: Verlag Chemie 1962.

    Google Scholar 

  • Burker, J. B.: Preparation and determination of lactic acid. In: Methods of enzymology, vol. 3, p. 241–245 (S. Colowick, N. O. Kaplan). New York: Acad. Press 1957.

    Google Scholar 

  • Criss, W. E., Litwack, C., Morris, H. P., Weinhouse, S.: Cancer Res.30, 370–375 (1970).

    Google Scholar 

  • Czock, R., Eckert, L.: Phosphoglyceratsäure, Phosphopyruvate und Pyruvate. In: Methoden der enzym. Analyse, p. 229–234 (H. U. Bergmeyer). Weinheim: Verlag Chemie 1962.

    Google Scholar 

  • Hohorst, H. J.: Glukose-6-Phosphat und Eructose-6-Phosphat. In: Methoden der enzym. Analyse, p. 131–133 (H. U. Bergmeyer). Weinheim: Verlag Chemie 1962.

    Google Scholar 

  • Lamprecht, W., Trautschold, I.: Adenosine triphosphat. In: Methoden der enzym. Analyse, p. 543–549 (H. U. Bergmeyer). Weinheim: Verlag Chemie 1962.

    Google Scholar 

  • Leloir, L., Goldemberg, S. H.: Synthesis of glycogen from uridine diphosphoglucose in liver. J. biol. Chem.235, 919–923 (1960).

    Google Scholar 

  • Lowry, O. H., Rosenbrough, M., Farr, A.: Protein measurement with the Polin phenol reagent. J. biol. Chem.193, 265–278 (1951).

    Google Scholar 

  • Mac Blair, D.: Magnesium, potassium ions and adenylate kinase equilibrium. Europ. J. Biochem.13, 384–388 (1970).

    Google Scholar 

  • Masui, J.: Relative roles of the pituitary follicle cells and progesterone in the oocyte maturation in Rana pipiens. J. exp. Zool.166, 365–376 (1967).

    Google Scholar 

  • Milman, L. S., Yurowitzky, Yu. G.: The control of glycolysis in early embryogenesis. Biochim. biophys. Acta (Amst.)148, 362–371 (1967).

    Google Scholar 

  • Milman, L. S., Yurowitzky, Yu, G.: Control of enzyme activity of glycolysis in early embryogenesis. Uspechi biol. Himii (Progress in biol. Chemistry, in Russian)13, 159–176 (1972).

    Google Scholar 

  • Siebert, G.: Isocitrate. In: Methoden der enzym. Analyse, S. 318–320 (H. U. Bergmayer). Weinheim: Verlag Chemie 1962.

    Google Scholar 

  • Somogyi, M.: Preparation of glycogen. In: Methods in enzymology, vol. 3, p. 3–5 (S. Colowick and N. O. Kaplan). New York: Acad. Press 1957.

    Google Scholar 

  • Stern, J. H.: Assay of trycarboxylic acids. In: Methos in enzymology, vol. 3, p. 425–429 (S. Colowick, N. O. Kaplan). New York: Acad. Press 1957.

    Google Scholar 

  • Ströminger, J.: The enzymic determination of uridine diphosphoglucose. J. biol. Chem.224, 79–90 (1957).

    Google Scholar 

  • Sutherland, E. W., Wosilait W. D.: Liver phosphorylase, preparation and properties. J. biol. Chem.218, 459–478 (1956).

    Google Scholar 

  • Weidemann, M. S., Hems, D. A., Krebs, H. A.: Effect of adenine nucleotides on renal metabolism. Nephron6, 282–296 (1969).

    Google Scholar 

  • Wettermark, G., Brolin, S., Borglund, E.: Determination of hexokinase activity. Analyt. Biochem.22, 211–217 (1968).

    Google Scholar 

  • Williamson, J. R.: Effect of fatty acids and glucagon on the control of gluconeogenesis in rat liver. Advanc. Enzyme Regul.5, 229–256 (1967).

    Google Scholar 

  • Williamson, J. R., Scholz, B., Browning, E. T.: Control mechanisms of gluconeogenesis and ketogenesis. J. biol. Chem.244, 4607–4616 (1969).

    Google Scholar 

  • Yurowitzky, Yu. G., Milman, L. S.: Pecularities of the glycolysis in loach oogenesis. Ontogenez3, 405–414 (1972) [In Russian].

    Google Scholar 

  • Yurowitzky, Yu. G., Milman, L. S.: Co-ordinative changes in the enzyme activity in oogenesis of loach (Misgurnus fossilis). FEBS Letters14, 105–106 (1971a). Biokhimia36, 1130–1135 (1971b) [In Russian].

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yurowitzky, Y.G., Milman, L.S. Changes in enzyme activity of glycogen and hexose metabolism during oocyte maturation in a teleost,Misgurnus fossilis L.. W. Roux' Archiv f. Entwicklungsmechanik 171, 48–54 (1972). https://doi.org/10.1007/BF00584413

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00584413

Keywords

Navigation