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Neurophysiology

, Volume 40, Issue 1, pp 6–9 | Cite as

β-amyloid-induced changes in calcium homeostasis in cultured hippocampal neurons of the rat

  • T. Yu. Korol
  • S. V. Korol
  • E. P. Kostyuk
  • P. G. Kostyuk
Article

Abstract

A two-wave technique of calciometry with the use of a fluorescence dye, fura-2/AM, was applied for examination of the effect of a protein, β-amyloid (the main component of senile plaques in Alzheimer’s disease), on calcium homeostasis in cultured neurons of the rat hippocampus; β-amyloid was added to the culture medium. In most neurons, the effect of β-amyloid appeared as a more than twofold increase in the basic calcium concentration, as compared with the control (153.4 ± 11.5 and 71.7 ± 5.4 nM, respectively; P < 0.05). The characteristics of calcium transients induced by application of hyperpotassium solution also changed; the amplitude of these transients decreased, and the duration of a part corresponding to calcium release from the cell (rundown of the transient) increased. The mean amplitude of calcium transients under control conditions was 447.5 ± 20.1 nM, while after incubation in the presence of β-amyloid this index dropped to 278.4 ± 22.6 nM. Under control conditions, the decline phase of calcium transients lasted, on average, 100 ± 6 sec, while after incubation of hippocampal cell cultures in the presence of β-amyloid this phase lasted 250 ± 10 sec. Therefore, an excess of β-amyloid influences significantly calcium homeostasis in the nerve cells by disturbing functions of the calcium-controlling systems, such as voltage-operated calcium channels of the plasma membrane and calcium stores of the mitochondria and endoplasmic reticulum.

Keywords

β-amyloid Alzheimer’s disease hippocampal cell culture voltage-operated calcium channels calcium homeostasis 

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References

  1. 1.
    Alzheimer’s Disease: Advances in Etiology, Pathogenesis and Therapeutics, K. Iqbal, S. S. Sisodia, and B. Winblad (eds.), John Wiley and Sons Ltd., Chichester (2001).Google Scholar
  2. 2.
    L. Hardy, “A hundred years of Alzheimer’s disease research,” Neuron, 52, 3–13 (2006).PubMedCrossRefGoogle Scholar
  3. 3.
    E. Žerovnik, “Amyloid-fibril formation: proposed mechanisms and relevance to conformational disease,” Eur. J. Biochem., 269, 3362–3371 (2002).PubMedCrossRefGoogle Scholar
  4. 4.
    P. M. Rossini, C. Del Percio, P. Pasqualetti, et al., “Conversion from mild cognitive impairment to Alzheimer’s disease is predicted by sources and coherence of brain electroencephalography rhythms,” Neuroscience, 147, 793–803 (2006).CrossRefGoogle Scholar
  5. 5.
    Alzheimer’s Disease: Methods and Protocols, N. M. Hooper (ed.), Humana Press, Totowa (2002).Google Scholar
  6. 6.
    Y. Kashiwaya, T. Takeshima, N. Mori, et al., “D-β-hydroxybutyrate protects neurons in models of Alzheimer’s and Parkinson’s disease,” Proc. Natl. Acad. Sci. USA, 97, No. 10, 5440–5444 (2000).PubMedCrossRefGoogle Scholar
  7. 7.
    B. L. Kelly, R. Vassar, and A. Ferreira, “β-amyloid-induced dynamin 1 depletion in hippocampal neurons: a potential mechanism for early cognitive decline in Alzheimer disease,” J. Biol. Chem., 280, No. 36, 31746–31753 (2005).PubMedCrossRefGoogle Scholar
  8. 8.
    A. Y. Abramov, L. Canevari, and M. R. Duchen, “β-amyloid peptides induce mitochondrial dysfunction and oxidative stress in astrocytes and death of neurons through activation of NADP oxidase,” J. Neurosci., 24, No. 2, 565–575 (2004).PubMedCrossRefGoogle Scholar
  9. 9.
    P. G. Kostyuk, V. L. Zima, S. Magura, et al., Biophysics [in Ukrainian], Oberegy, Kyiv (2001).Google Scholar
  10. 10.
    S. Y. Ivanova, M. V. Storozhuk, I. V. Melnick, and P. G. Kostyuk, “Chronic treatment with ionotropic glutamate receptor antagonist kynurenate affects GABAergic synaptic transmission in rat hippocampal cell cultures,” Neurosci. Lett., 341, No. 1, 61–64 (2003).PubMedCrossRefGoogle Scholar
  11. 11.
    G. Grynkiewicz, M. Poenie, and R. Y. Tsien, “A new generation of Ca2+ indicators with greatly improved fluorescence properties,” J. Biol. Chem., 260, 3440–3450 (1985).PubMedGoogle Scholar
  12. 12.
    C. M. Norris, I. Kadish, E. M. Blalock, et al., “Calcineurin triggers reactive inflammatory processes in astrocytes and is upregulated in aging and Alzheimer’s models,” J. Neurosci., 25, No. 18, 4649–4658 (2005).PubMedCrossRefGoogle Scholar
  13. 13.
    J. P. Spencer, J. T. Brown, J. C. Richardson, et al., “Modulation of hippocampal excitability by 5-HT4 receptor agonists in a transgenic model of Alzheimer’s disease,” J. Neurosci., 129, 49–54 (2004).CrossRefGoogle Scholar
  14. 14.
    W. Fu, H. Luo, S. Partasaraty, and M. P. Mattson, “Catecholamines potentiate amyloid beta peptide neurotoxiticy: involvement of oxidative stress, mitochondrial dysfunction, and perturbed calcium homeostasis,” Neurobiol. Dis., 5, No. 4, 229–243 (1998).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2008

Authors and Affiliations

  • T. Yu. Korol
    • 1
  • S. V. Korol
    • 1
  • E. P. Kostyuk
    • 2
  • P. G. Kostyuk
    • 2
  1. 1.International Center for Molecular PhysiologyNational Academy of Sciences of UkraineKyivUkraine
  2. 2.Bogomolets Institute of PhysiologyNational Academy of Sciences of UkraineKyivUkraine

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