Properties of Calcium-Activated Chloride Currents in Rat Purkinje Cerebellum Neurons

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V.L. Zamoyski
E.V. Bovina
V.V. Grigoriev

Abstract

The presence of calcium-activated chloride current was shown using on freshly isolated rat Purkinje cerebellum neiurones and the pacth-clamp method in the whole-cell configuration. Chloride currents appeared in sodium-free external solution and reversibly disappeared in chloride-free or calcium-free external solution. Replacing of K+ ions (120 mM) to Cs+ ions in micropipette (120 mM) show the chloride currents even with 140 mM Na+ in external solution. This current was blocked to 80–100% by nifluminic acid (25–100 μM). It was found out that well known blockers of potassium channels tetraethylammonium (TEA) and 4-aminopyridine (4-AP) also effectively blocked chloride channels. The IC50 values for TEA and 4-AP were 130 μM, and 110 μM respectively. The action of TEA was reversible, while 4-AP at concentration 100 μM and above irreversibly blocked chloride channels.

Article Details

How to Cite
Zamoyski, V., Bovina, E., & Grigoriev, V. (2018). Properties of Calcium-Activated Chloride Currents in Rat Purkinje Cerebellum Neurons. Biomedical Chemistry: Research and Methods, 1(3), e00034. https://doi.org/10.18097/BMCRM00034
Section
EXPERIMENTAL RESEARCH

References

  1. Pedemonte, N. Galietta, L. J. V. (2014). Structure and Function of Tmem16 Proteins (Anoctamins). Physiological Reviews, 94(2): p. 419-459. DOI
  2. Huang, F., Rock, J. R., Harfe, B. D., Cheng, T., Huang, X. Z., Jan, Y. N., Jan, L. Y. (2009). Studies on expression and function of the TMEM16A calcium-activated chloride channel. Proceedings of the National Academy of Sciences of the United States of America, 106(50): p. 21413-21418. DOI
  3. Kaneda, M., Nakamura, H., Akaike, N. (1988). Mechanical and Enzymatic Isolation of Mammalian Cns Neurons. Neuroscience Research, 5(4): p. 299-315. DOI
  4. Hamill, O. P., Marty, A., Neher, E., Sakmann, B., Sigworth, F. J. (1981). Improved Patch-Clamp Techniques for High-Resolution Current Recording from Cells and Cell-Free Membrane Patches. Pflugers Archiv-European Journal of Physiology, 391(2): p. 85-100. DOI
  5. Ferrera, L., Caputo, A., Galietta, L. J. V. (2010). TMEM16A Protein: A New Identity for Ca2+-Dependent Cl- Channels. Physiology, 25(6): p. 357-363. DOI
  6. Arroyo, J. P., Kahle, K. T., Gamba, G. (2013). The SLC12 family of electroneutral cation-coupled chloride cotransporters. Molecular Aspects of Medicine, 34(2-3): p. 288-298. DOI
  7. Kaila, K., Price, T. J., Payne, J. A., Puskarjov, M., Voipio, J. (2014). Cation-chloride cotransporters in neuronal development, plasticity and disease. Nature Reviews Neuroscience, 15(10): p. 637-654. DOI
  8. Huang, W. C., Xiao, S. H., Huang, F., Harfe, B. D., Jan, Y. N., Jan, L. Y. (2012). Calcium-Activated Chloride Channels (CaCCs) Regulate Action Potential and Synaptic Response in Hippocampal Neurons. Neuron, 74(1): p. 179-192. DOI
  9. Sanchez, D. Y. Blatz, A. L. (1994). Block of Neuronal Fast Chloride Channels by Internal Tetraethylammonium Ions. Journal of General Physiology, 104(1): p. 173-190. DOI