The Possible Roles of Astrocytes in Energy Metabolism of the Brain

  • Bernd Hamprecht
  • Ralf Dringen
  • Brigitte Pfeiffer
  • Georg Kurz
Part of the Altschul Symposia Series book series (ALSS, volume 2)


In the brain astrocytes are situated in a key position between the microvessels and the other cell types, neurons and oligodendrocytes. If one considers the narrow extracellular space between the brain cells, the conclusion appears inescapable that the nutrients of the brain, such as the quantitatively most important substrates for the generation of energy, glucose and oxygen, must cross the astrocytes to reach their metabolic destination in the neurons and oligodendrocytes. This location also could be the prerequisite for playing a pivotal role in controlling energy metabolism of the brain. However, in saying this one has to add immediately that little is known on such an -anthropomorphically seen — attractive function of astrocytes.


Glial Fibrillary Acidic Protein Malic Enzyme Glycogen Phosphorylase Astroglial Cell Glucosyl Residue 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Carlsson-Skwirut C., Jörnvall H., Holmgren A., Andersson C., Bergman T., Lundquist G., Sjögren B., and Sara V.R., 1986, Isolation and characterization of variant IGF-I as well as IGF-II from adult human brain. FEBS Lett. 201: 46.PubMedCrossRefGoogle Scholar
  2. Carlsson-Skwirut C., Lake M., Hartmanis M., Hall K., and Sara V.R., 1989, A comparison of the biological activity of the recombinant intact and truncated insulin-like growth factor 1 (IGF-1). Biochim. Biophys. Acta 1011: 192.PubMedCrossRefGoogle Scholar
  3. Cataldo A.M. and Broadwell R.D., 1986, Cytochemical identification of cerebral glycogen and glucose-6-phosphatase activity under normal and experimental conditions: neurons and glia. J. Electr. Micros. Tech. 3: 413.CrossRefGoogle Scholar
  4. Coles A.J., 1989, Functions of glial cells in the retina of the honeybee drone. Glia 2: 1PubMedCrossRefGoogle Scholar
  5. David E.S. and Crerar M.M., 1986, Quantitation of muscle glycogen phosporylase mRNA and enzyme amounts in adult rat tissues. Biochim. Biophys. Acta 880: 78.PubMedCrossRefGoogle Scholar
  6. Dringen R. and Hamprecht B., 1990, Modulation of glycogen content in astrocytes. Biol. Chem. Hoppe-Seyler 371: 780.Google Scholar
  7. Dringen R. and Hamprecht B., 1991, Modulation of astrocytic glycogen by hexoses. J. Neurochem. 57, Suppl., S127D.Google Scholar
  8. Dringen R. and Hamprecht B., 1992a, Glucose, insulin and insulin-like growth factor I regulate the glycogen content in astroglia-rich primary cultures. J. Neurochem. 58: 511.PubMedCrossRefGoogle Scholar
  9. Dringen R. and Hamprecht B., 1992b, Investigation on the function of glycogen in astrocytes. Biol. Chem. Hoppe-Seyler, 373: 951.Google Scholar
  10. Dringen R. and Hamprecht B., 1992c, Inhibition by 2-deoxyglucose and 1,5-gluconolactone of glycogen mobilization in astroglia-rich primary cultures. J. Neurochem.,in press.Google Scholar
  11. Edmond J., Robbins R.A., Bergstrom J.D., Cole R.A., and de Vellis J., 1987, Capacity for substrate utilization in oxidative metabolism by neurons, astrocytes, and oligodendrocytes from developing brain in primary culture. J. Neurosci. Res. 18: 551.PubMedCrossRefGoogle Scholar
  12. Friedman D.L. and Lamer J., 1963, Studies on UDPG-a-glucan transglucosylase. III. Interconversion of two forms of muscle UDPG-a-glucan transglucosylase by a phosphorylationdephosphorylation reaction sequence. Biochemistry 2: 669.PubMedCrossRefGoogle Scholar
  13. Geiger A., 1958, Correlation of brain metabolism and function by the use of a brain perfusion method in situ. Physiol. Revs., 38: 1.Google Scholar
  14. Gold A.M., Legrand E., and Sanchez G.R., 1971, Inhibition of muscle phophorylase a by 5gluconolactone. J. Biol. Chem., 246: 5700.PubMedGoogle Scholar
  15. Hamprecht B. and Löffler F., 1985, Primary glial cultures as a model for studying hormone action. Meth. Enzymol., 109: 341.PubMedCrossRefGoogle Scholar
  16. Ignacio P.C., Baldwin B.A., Vijayan V.K., Tait R.C., and Gorin F.A., 1990, Brain isozyme of glycogen phosphorylase: immunohistological localization within the central nervous system. Brain Res., 529: 42.PubMedCrossRefGoogle Scholar
  17. Kao-Jen J. and Wilson J.E., 1980, Localization of hexokinase in neural tissue: electron microscopic studies of rat cerebellar cortex. J. Neurochem., 35: 667.PubMedCrossRefGoogle Scholar
  18. Katoh-Semba R., Keino H., and Kashiwamata S., 1988, A possible contribution by glial cells to neuronal energy production: enzyme-histochemical studies in the developing rat cerebellum. Cell Tissue Res. 252: 133.PubMedCrossRefGoogle Scholar
  19. Kurz G., Wiesinger H., and Hamprecht B., 1992, Purification of cytosolic malic enzyme from bovine brain, generation of monoclonal antibodies, and immunocytochemical localization of the enzyme in glial cells of neural primary cultures. J. Neurochem.,in press.Google Scholar
  20. Lamer J., 1990, Insulin and the stimulation of glycogen synthesis. The road from glycogen structure to glycogen synthase to cyclic AMP-dependent protein kinase to insulin mediators. Adv. Enzymol., 63: 173.Google Scholar
  21. Mayer D., Seelmann-Eggebert G., and Letsch I., 1992, Glycogen phosphorylase isoenzymes from hepatoma 3924A and from a non-tumorigenic liver cell line. Comparison with the liver and brain enzymes. Biochem. J., 282: 665.PubMedGoogle Scholar
  22. Newgard C.B., Hwang P.K., and Fletterick R.J., 1989, The family of glycogen phosphorylases: structure and function. Crit. Rev. Biochem. Mol. Biol., 24: 69.PubMedCrossRefGoogle Scholar
  23. Pfeiffer B., Elmer K., Roggendorf W., and Hamprecht B., 1990, Immunohistochemical demonstration of glycogen phosphorylase in rat brain slices. Histochemistry, 94: 73.PubMedCrossRefGoogle Scholar
  24. Pfeiffer B., Meyermann R., and Hamprecht B., 1992, Immunohistochemical co-localization of glycogen phosphorylase with the astroglial markers glial fibrillary acidic protein and S-100 protein in rat brain sections. Histochemistry 97: 405.PubMedCrossRefGoogle Scholar
  25. Reinhart P.H., Pfeiffer B., Spengler S., and Hamprecht B., 1990, Purification of glycogen phosphorylase from bovine brain and immunocytochemical examination of rat primary cultures using monoclonal antibodies raised against this enzyme. J. Neurochem. 54: 1474.PubMedCrossRefGoogle Scholar
  26. Simurda M. and Wilson J.E., 1980, Localization of hexokinase in neural tissue: immunofluorescence studies on the developing cerebellum and retina of the rat. J. Neurochem., 35: 58.PubMedCrossRefGoogle Scholar
  27. Snyder C.D. and Wilson J.E., 1983, Relative levels of hexokinase in isolated neuronal, astrocytic, and oligodendroglial fractions from rat brain. J. Neurochem., 40: 1178.PubMedCrossRefGoogle Scholar
  28. Tsacopoulos M., Coles J.A., and Van de Werve G., 1987, The supply of metabolic substrate from glia to photoreceptors in the retina of the honeybee drone. J. Physiol. 82: 279.Google Scholar
  29. Tsacopoulos M., Eveqouz-Mercier V., Perrottet P., and Buchner E., 1988, Honeybee retinal glial cells transform glucose and supply the neurons wtih metabolic substrate. Proc. Natl. Acad. Sci. USA, 85: 8727.PubMedCrossRefGoogle Scholar
  30. Tu J., Jacobson G.R., and Graves D.J., 1971, Isotopic effects and inhibition of polysaccharide phosphorylase by 1,5-gluconolactone. Relationship to the catalytic mechanism. Biochemistry, 10: 1229.PubMedCrossRefGoogle Scholar
  31. van Calker D., Muller M., and Hamprecht B., 1978, Adrenergic a-and I3-receptors expressed by the same cell type in primary culture of perinatal mouse brain. J. Neurochem., 30: 713.PubMedCrossRefGoogle Scholar
  32. van Calker D., Muller M., and Hamprecht B., 1980, Regulation by secretin, vasoactive intestinal peptide, and somatostatin of cyclic AMP accumulation in cultured brain cells. Proc. Natl.Acad. Sci. USA 77: 6907.PubMedCrossRefGoogle Scholar
  33. Vicario C., Arizmendi C., Malloch G., Clark J.B., and Medina J.M., 1991, Lactate utilization by isolated cells from early neonatal rat brain. J. Neurochem., 57: 1700.PubMedCrossRefGoogle Scholar
  34. Watanabe H. and Passonneau J.V., 1973, Factors affecting the turnover of cerebral glycogen and limit dextrin in vivo. J. Neurochem. 20: 1543.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Bernd Hamprecht
    • 1
  • Ralf Dringen
    • 1
  • Brigitte Pfeiffer
    • 1
  • Georg Kurz
    • 1
  1. 1.Physiologisch-Chemisches Institut der UniversitätUniversität TübingenTübingenGermany

Personalised recommendations