Virchows Archiv B

, Volume 4, Issue 1, pp 196–207 | Cite as

A biochemical and ultrastructural study of liver, muscle, heart and kidney in type II glycogenosis

  • C. B. Bruni
  • F. M. Paluello


The present study deals with ultrastructural findings and biochemical data from liver, muscle, heart and kidney in a case of type II glycogenosis. A detailed physicochemical and ultrastructural study of the glycogen particles isolated from these tissues has also been performed.

The main findings can be summarized as follows:
  1. 1.

    The data obtained from the ultrastructural study of the cardiac tissue show the glycogen is not within bodies surrounded by a membrane. The shape, size and sedimentation pattern of cardiac glycogen are different from those of the muscle.

  2. 2.

    The glycogen isolated from liver is abnormal with respect to size, distribution of the particles and sedimentation pattern: smaller, lighter particles predominate.

  3. 3.

    Kidney tissue possesses a high acid maltase activity, but in spite of this, numerous lysosomes filled with glycogen are visible. Biochemical data suggest the possibility that several allelic forms of kidney acid maltase exist.



Glycogen Content Sedimentation Pattern Glycogen Storage Disease Sedimentation Coefficient Glucosidase Activity 
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Biochemische und ultrastrukturelle Untersuchungen von Leber, Muskulatur, Herz und Nieren bei Glykogenosis II


In der vorliegenden Studie werden biochemische und elektronenmikroskopische Untersuchungen der Leber, der Muskulatur, des Herzens und der Niere in einem Fall von Glykogenose Typ II vorgelegt.

Folgende Befunde wurden erhoben:
  1. 1.

    Im Herzmuskel liegt das Glykogen nicht in membrangebundener Form vor. Das Herzmuskelglykogen unterscheidet sich in seiner Form, der Größe und dem Sedimentationsverhalten vom Muskelglykogen.

  2. 2.

    Das Leberglykogen ist ebenfalls abnorm hinsichtlich der Größe und der Verteilung der Partikel. Es kommen außerdem mehr kleinere und leichtere Partikel vor.

  3. 3.

    Im Nierengewebe findet man eine hohe Aktivität an saurer Maltase, obwohl zahlreiche Lysosomen Glykogen enthalten. Biochemische Untersuchungen weisen auf die Möglichkeit verschiedener Isoenzyme der sauren Nierenmaltase hin.



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  1. Auricchio, F., Bruni, C.B.: Purification of an acid α-1,4-glucosidase by dextran-gel filtration. Biochem. J.105, 35–38 (1967).PubMedGoogle Scholar
  2. ——, Sica, V.: Further purification and characterization of the acid α-1,4-glucosidase. Biochem. J.108, 161–167 (1968).PubMedGoogle Scholar
  3. Baudhuin, P., Hers, H. G., Loeb, H.: Electron microscopic and biochemical study of type II glycogenosis. Lab. Invest.13, 1139–1152 (1964).PubMedGoogle Scholar
  4. Brosemer, R. W., Rutter, W. J.: Liver amylase. I. Cellular distribution and properties. J. biol. Chem.236, 1253–1258 (1961).Google Scholar
  5. Brown, B. I., Zellweger, H.: α-1,4-glucosidase activity in leucocytes from the family of two brothers who lack this enzyme in muscle. Biochem. J.101, 16C-18C (1966).PubMedGoogle Scholar
  6. Bruni, C. B., Auricchio, F., Covelli, I.: Acid α-D-glucosidase-glucohydrolase from cattle liver. Isolation and properties. J. biol. Chem.244, 4735–4742 (1969).PubMedGoogle Scholar
  7. Bueding, E., Orrell, S. A., Sidbury, J.: Studies of storage disease glycogens. In: Control of glycogen metabolism (ed. H. J. Whelan and M. P. Cameron), p. 387–392. London: J. & A. Churchill Ltd. 1964.Google Scholar
  8. Cardiff, R. D.: A histochemical and electron microscopic study of skeletal muscle in a case of Pompe’s disease (Glycogenosis II). Pediatrics37, 249–259 (1966).PubMedGoogle Scholar
  9. Hers, H. G.: Etudes enzymatiques sur fragments hépatiques: application à la classification des glycogenosis. Rev. int. Hépat.9, 35–55 (1959).PubMedGoogle Scholar
  10. — α-glucosidase deficiency in generalized glycogen storage disease (Pompe’s disease). Biochem. J.86, 11–16 (1963).PubMedGoogle Scholar
  11. — Glycogen storage disease. In: Advances in metabolic disorders (ed. R. Levine and R. Luft), vol. I, p. 1–44. New York: Academic Press 1964.Google Scholar
  12. — Hoof, F. van: Enzymes of glycogen degradation in biopsy material. In: Methods in enzymology (ed. E. F. Neufeld and V. Ginsburg), vol. VIII, p. 525–532. New York: Academic Press 1966.Google Scholar
  13. —— Glycogen storage diseases: Type II and type VI glycogenosis. In: Carbohydrate metabolism and its disorders (ed. F. Dickens, P. J. Randle and W. J. Whelan), vol. II, p. 151–168. New York: Academic Press 1968.Google Scholar
  14. Hug, G., Garancis, J. C., Schubert, W. K., Kaplan, S.: Glycogen storage disease, type II, III, VIII and IX. Amer. J. Dis. Child.111, 457–474 (1966).Google Scholar
  15. — Schubert, W. K.: Lysosomes in type II glycogenosis. J. Cell Biol.35, C1-C6 (1967).PubMedCrossRefGoogle Scholar
  16. Illingworth, B., Brown, D. H.: The subcellular distribution of enzymes in type II glycogenosis and the occurence of an oligo-α-1,4-glucan glucohydrolase in human tissues. Biochim. biophys. Acta (Amst.)110, 124–133 (1965).Google Scholar
  17. Karnowsky, M. J.: Simple methods for „staining with lead“ at high pH in electron microscopy. J. biophys. biochem. Cytol.11, 729–732 (1961).Google Scholar
  18. Lejeune, N., Thinès-Sempoux, Hers, H. G.: Tissue fractionation studies. 16. Intracellular distribution and properties of α-glueosidases in rat liver. Biochem. J.86, 16–21 (1963).PubMedGoogle Scholar
  19. Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the Polin phenol reagent. J. biol. Chem.193, 265–275 (1951).PubMedGoogle Scholar
  20. Millonig, G.: The advantage of phosphate buffer for OsO4 solution in fixation. J. appl. Physiol.32, 1637 (1961).Google Scholar
  21. Orrell, S. A., Bueding, E.: Sedimentation characteristics of glycogen. J. Amer. chem. Soc.80, 3800 (1958).CrossRefGoogle Scholar
  22. Seifter, S., Seymour, S., Novic, B., Muntwyler, E.: The estimation of glycogen with the anthrone reagent. Arch. Biochem.25, 191–200 (1950).PubMedGoogle Scholar
  23. Steinitz, K., Rutenberg, A.: Tissue α-glucosidase activity and glycogen content in patients with generalized glycogenosis. Israel J. med. Sci.3, 411–421 (1967).PubMedGoogle Scholar
  24. Torres, H. N., Olavarria, J. M.: Liver α-glucosidases. J. biol. Chem.239, 2427–2434 (1964).PubMedGoogle Scholar
  25. Trump, B. P., Smuekler, E. A., Benditt, E. P.: A method for staining epoxy sections for light microscopy. J. Ultrastruct. Res.5, 343–348 (1961).PubMedCrossRefGoogle Scholar
  26. Watson, M. L.: Staining of tissue sections for electron microscopy with heavy metals. J. biophys. biochem. Cytol.4, 475–478 (1958).PubMedCrossRefGoogle Scholar
  27. Witzleben, C. L.: Renal cortical tubular glycogen localization in glycogenosis type II (Pompe’s disease). Lab. Invest.20, 424–429 (1969).PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1969

Authors and Affiliations

  • C. B. Bruni
    • 1
    • 2
  • F. M. Paluello
    • 1
    • 2
  1. 1.Istituto di Patologia GeneraleUniversità di NapoliNaplesItaly
  2. 2.Istituto di Clinica Medica IIUniversità di RomaRomeItaly

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