Advertisement

Neuroscience and Behavioral Physiology

, Volume 30, Issue 3, pp 347–355 | Cite as

The effects of the dynamic state of the cytoskeleton on neuronal plasticity

  • T. A. Zapara
  • O. G. Simonova
  • A. A. Zharkikh
  • A. S. Ratushnyak
Article

Abstract

The effects of degrading and stabilizing microtubules and microfilaments on the formation of plastic reactions were studied in isolated nerve cells from the molluskLymnaea stagnalis. Degradation of the cytoskeleton affected the performance, retention, and repeated acquisition of plastic reactions. Stabilization of microtubules led to the appearance of a relationship between the dynamics of the development and retention of plastic reactions and the series of stimulation. Stabilization of microfilaments led to transient plastic reaction, along with long-term reactions. These results show that rearrangements of the cytoskeleton have a key role in the processes of neuronal plasticity.

Key Words

Neuron plasticity cytoskeleton learning 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    L. Sh. Ganelina and T. P. Nekrasova, “Protein kinase C and its role in normal and transformed cells,”Tsitologiya,31, No. 2, 131–147 (1989).Google Scholar
  2. 2.
    D. A. Moshkov,Neuron Adaptation and Ultrastructure [in Russian], Nauka, Moscow (1985).Google Scholar
  3. 3.
    A. S. Ratushnyak, R. A. Zapara, A. A. Zharkikh, and O. A. Tatushnyak, “The effects of changes in dynamic equilibrium in microtubule and microfilament systems on plastic reactions of neurons,”Zh. Vyssh. Nerv. Deyat.,46, No. 2, 355–362 (1995).Google Scholar
  4. 4.
    V. A. Tkachuk, “The role and position of cyclic nucleotides in the neuroendocrine regulation of cells and tissues,”Biol. Nauki,6, 5–17 (1987).PubMedGoogle Scholar
  5. 5.
    Yu. V. Chistyakova and E. V. Parfenova, “Ca protease—an enzyme involved in the metabolism of cytoskeletal proteins in the olfactory pavement of vertebrates,”Tsitologiya,11, 1345–1352 (1989).Google Scholar
  6. 6.
    Ch. Aoki and Ph. Siekevitz, “Ontogenetic changes in the cyclic adenosine-3,5-monophosphate-stimulatable phosphorylation of cat visual cortex proteins, particularly of microtubule-associated protein 2 (MAP2): effects of normal and dark rearing and of the exposure to light,”J. Neurosci.,5, No. 9, 2465–2483 (1985).PubMedGoogle Scholar
  7. 7.
    V. Bennet, K. Gardner, and J. Steiner, “Brain adducin: a protein kinase C substrate that may mediate site-directed assembly at the spectrin-actin junction,”J. Biol. Chem.,263, No. 12, 5860–5869 (1988).Google Scholar
  8. 8.
    M.-F. Carlier, D. Didry, and D. Pantalone, “Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility,”J. Cell. Biol.,136, No. 6, 1307–1322 (1997).PubMedCrossRefGoogle Scholar
  9. 9.
    N. A. Cohen, J. E. Brenman, S. H. Snyder, and D. S. Bredt, “Binding of the inward rectifier K+ channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation,”Neuron,17, No. 4, 759–767 (1996).PubMedCrossRefGoogle Scholar
  10. 10.
    M. R. C. Costa and W. A. Catterall, “Phosphorylation of the α-subunit of the sodium channel by protein kinase C,”Cell. Molec. Neurobiol.,4, No. 3, 291–297 (1984).PubMedCrossRefGoogle Scholar
  11. 11.
    S. A. Deriemer, J. A. Strong, K. A. Albert, P. Greengard, and L. K. Haczmarek, “Enhancement of calcium current inAplysia neurones by phorbol ester and protein kinase C,Nature,313, 313–316 (1985).PubMedCrossRefGoogle Scholar
  12. 12.
    D. A. Ewald, A. Williams, and I. B. Levitan, “Modulation of single Ca-dependent K-channel activity by protein phosphorylation,”Nature,315, No. 6019, 503–505 (1985).PubMedCrossRefGoogle Scholar
  13. 13.
    J. Farley and S. Auerbach, “Protein kinase C activation induces conductance changes inHermissenda photoreceptors like those seen in associative learning,”Nature,319, No. 6050, 220–223 (1986).PubMedCrossRefGoogle Scholar
  14. 14.
    S. Hameroff and R. Penrose, “Orchestrated reduction of quantum coherence in brain microtubules: A model for consciousness,”Mathemat. Comput. Simulat.,40, No. 3-4, 453–480 (1996).CrossRefGoogle Scholar
  15. 15.
    B. D. Johnson and L. Byerly, “Ca channel Ca2+-dependent inactivation in a mammalian central neuron involves the cytoskeleton,”Pflügers Arch.,429, No. 1, 14–21 (1994).PubMedGoogle Scholar
  16. 16.
    M. Karin and T. Smeal, “Control of transcription factors by signal transduction pathway: the beginning of the end,”TIBS,17, 418–422 (1992).PubMedGoogle Scholar
  17. 17.
    A. Moon and D. G. Drubin, “The ADF/cofilin proteins: stimulus-responsive modulations of actin dynamics,”Mol. Biol. Cell.,6, 1423–1431 (1995).PubMedGoogle Scholar
  18. 18.
    E. J. Neer and D. E. Clapham, “Roles of G protein subunits in trans-membrane signalling,”Nature,333, No. 6169, 129–134 (1988).PubMedCrossRefGoogle Scholar
  19. 19.
    L. S. Perlmutter, C. Gall, M. Baudry, and G. Lynch, “Distribution of calcium-activated and protease calpain in the brain,”J. Comp. Neurol.,296, No. 2, 269–276 (1990).PubMedCrossRefGoogle Scholar
  20. 20.
    R. Prekeris, M. W. Mayhew, J. B. Cooper, and D. M. Terrian, “Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in regulation of synaptic function,”J. Cell. Biol.,132, No. 1-2, 77–90 (1996).PubMedCrossRefGoogle Scholar
  21. 21.
    E. M. Quinlan and S. Halpaint “Emergence of activity-dependent, bidirectional control of microtubule-associated protein MAP2 phosphorylation during postnatal development,”Neurosci.,16, No. 23, 7627–7637 (1996).Google Scholar
  22. 22.
    C. Rosenmund and G. L. Westbrook, “Calcium-induced actin depolymerization reduces NMDA channel activity,”Neuron,10, No. 5, 805–814 (1993).PubMedCrossRefGoogle Scholar
  23. 23.
    Ch. V. Schuster, G. W. Davis, R. D. Fitter, and C. S. Goodman, “Genetic dissection of structural and functional components of synaptic plasticity. II. Fasciclin II controls presynaptic structural plasticity,”Neuron 17, 655–667 (1996).PubMedCrossRefGoogle Scholar
  24. 24.
    P. Vanderklish, T. C. Saido, C. Gall, A. Arai, and G Lynch, “Proteolysis of spectrin by calpain accompanies theta-burst stimulation in cultured hippocampal slices,”Brain Res. Mol. Brain,32, 25–35 (1995).CrossRefGoogle Scholar
  25. 25.
    M. H. Wolf, H. Levine, W. S. May, P. Cuatrecasas, and N. A. Sahyoun, “A model for intracellular translocation of protein kinase C involving synergism between Ca and phorbol esters,”Nature,317, 546–549 (1985).PubMedCrossRefGoogle Scholar
  26. 26.
    C. Wu, V. M. Keivens, T. E. O'Toole, J. A. McDonald, and M. H. Ginsberg, “Integrin activation and cytoskeletal interaction are critical steps in the assembly of a fibronectin matrix,”Cell,83, 715–724 (1995).PubMedCrossRefGoogle Scholar
  27. 27.
    T. N. Yamoah and T. Crow, “Protein kinase and G-protein regulation of Ca currents inHermissenda photoreceptors by 5-HT and GABA,”J. Neurosci.,16, No. 15, 4799–4809 (1996).PubMedGoogle Scholar

Copyright information

© Kluwer Academic/Plenum Publishers 2000

Authors and Affiliations

  • T. A. Zapara
  • O. G. Simonova
  • A. A. Zharkikh
  • A. S. Ratushnyak
    • 1
  1. 1.Construction-Technology Institute of Calculating Technology, Siberian DivisionRussian Academy of SciencesNovosibirskRussia

Personalised recommendations