Abstract
The effects of haloperidol, an antagonist of D2 dopamine receptors, on the functioning of Ca2+, K+, and Cl− ion channels in the membrane of Chara corallina cells and on the functional properties of their cytoskeleton was studied. Haloperidol blocked Ca2+ channels of the plasmalemma. In addition to bringing about a decrease in the amplitude of the calcium current, exposure to haloperidol decelerated the activation and inactivation of calcium channels. The effect of haloperidol was reversible; after it was removed, the characteristics of calcium current were restored. Haloperidol did not affect Ca2+-activated chloride channels. Haloperidol also inhibited microfilament-dependent motion of the cytoplasm. Cytoplasmic streaming was restored after haloperidol was removed from the extracellular solution. These results suggest that the concentration of free Ca2+ ions in the cytoplasm increases in the presence of haloperidol, and that Ca2+ channels of C. corallina plasmalemma possess specific binding sites both for dopamine receptors and for their antagonists.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Abbreviations
- APW:
-
artificial pond water
References
Arteeva, I.V., Egorov, V.V., Gorshkov, A.N., Garmay, Yu.P., Aleinikova, T.D., and Shavlovsky, M.M., Modeling oligomerization and fibrillogenesis of mutant forms of beta 2 microglobulin, Med. Akad. Zh., 2013, vol. 13, no. 4, pp. 92–100.
Biancalana, M. and Koide, S., Molecular mechanism of thioflavin-T binding to amyloid fibrils, Biochim. Biophys. Acta, 2010, vol. 1804, pp. 1405–1412.
Groenning, M., Binding mode of thioflavin T and other molecular probes in the context of amyloid fibrils—current status, J. Chem. Biol., 2010, vol. 3, pp. 1–18.
Klunk, W.E., Pettegrew, J.W., and Abraham, J.D., Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation, J. Histochem. Cytochem., 1989, vol. 37, pp. 1273–1281.
Klunk, W.E., Jacob, R.F., and Mason, R.P., Quantifying amyloid by Congo red spectral shift assay, Meth. Enzymol., 1999, vol. 309, pp. 285–305.
Krebs, M.R.H., Morozova-Roche, L.A., Daniel, K., Robinson, C.V., and Dobson, C.M., Observation of sequence specificity in the seeding of protein amyloid fibrils, Protein Sci., 2004, vol. 13, pp. 1933–1938.
Kuznetsova, I.M., Sulatskaya, A.I., Uversky, V.N., and Turoverov, K.K., Analyzing thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique, PLoS One, 2012, vol. 7, p. e30724.
Lade, H., Govindwar, S., and Paul, D., Mineralization and detoxification of the carcinogenic azo dye Congo Red and real textile effluent by a polyurethane foam immobilized microbial consortium in an upflow column bioreactor, Int. J. Environ. Res. Public Health, 2015, vol. 12, pp. 6894–6918.
Lendel, C., Bertoncini, C.W., Cremades, N., Waudby, C.A., Vendruscolo, M., Dobson, C.M., Schenk, D., Christodoulou, J., and Toth, G., On the mechanism of nonspecific inhibitors of protein aggregation: dissecting the interactions of a-synuclein with Congo red and Lacmoid, Biochemistry, 2009, vol. 48, pp. 8322–8334.
Myers, S.L., Jones, S., Jahn, T.R., Morten, I.J., Tennent, G.A., Hewitt, E.W., and Radford, S.E., A systematic study of the effect of physiological factors on beta2-microglobulin amyloid formation at neutral pH, Biochemistry, 2006, vol. 45, pp. 2311–2321.
Picken, M.M., Amyloidosis—where are we now and where are we heading?, Arch. Pathol. Lab. Med., 2010, vol. 134, pp. 545–551.
Polyakov, D.S. and Shavlovsky, M.M., Molecular basis of beta 2-microglobulin amyloidoses, Med. Akad. Zh., 2014, vol. 14, no. 1, pp. 24–41.
Polyakov, D.S., Grudinina, N.A., Solovyov, K.V., Egorov, V.V., Sirotkin, A.K., Aleynikova, T.D., Totolyan, A.A., and Shavlovsky, M.M., Beta2-microglobulin amyloidosis: fibrillogenesis of natural and recombinant human beta2-microglobulin, Med. Akad. Zh., 2010a, vol. 10, no. 2, pp. 40–49.
Polyakov, D.S., Totolyan, A.A., and Shavlovsky, M.M., Obtaining of natural human beta2-microglobulin, Mol. Med., 2010b, vol. 6, pp. 39–43.
Polyakov, D.S., Grudinina, N.A., Solovyov, K.V., Egorov, V.V., Sirotkin, A.K., Aleinikova, T.D., Totolyan, A.A., and Shavlovsky, M.M., Human recombinant beta2 microglobulin and its fibrillogenesis at low and neutral pH values, Mol. Med., 2011, vol. 2, pp. 36–39.
Rokitansky, C., in Handbuch der speciellen pathologischen Anatomie, Wien: Braumuller und Seidel, 1842, pp. 311–312.
Sereikaite, J. and Bumelis, V.-A., Congo red interaction with a-proteins, Acta Biochimica Polonica, 2006, vol. 53, pp. 87–91.
Shavlovsky, M.M., Molecular and genetic basis of etiopathogenesis of amyloidoses, Med. Akad. Zh., 2010, vol. 10, no. 4, pp. 63–81.
Sipe, J.D., Benson, M.D., Buxbaum, J.N., Ikeda, S., Merlini, G., Saraiva, M.J.M., and Westermark, P., Nomenclature 2014: amyloid fibril proteins and clinical classification of the amyloidosis, Amyloid, 2014, vol. 21, pp. 221–224.
Sladewski, T.E., Shafer, A.M., and Hoag, C.M., The effect of ionic strength on the UV-vis spectrum of Congo red in aqueous solution, Spectrochim. Acta Part A: Mol. Biomol. Spectrosc., 2006, vol. 65, pp. 985–987.
Solovyov, K.V., Gasteva, A.A., Egorov, V.V., Aleinikova, T.D., Sirotkin, A.K., Shvartsman, A.L., and Shavlovsky, M.M., Role of the C-terminal fragment of human transthyretin in abnormal fibrillogenesis, Biochemistry (Moscow), 2006, vol. 71, no. 5, pp. 543–549.
Solovyov, K.V., Polyakov, D.S., Grudinina, N.A., Egorov, V.V., Morozova, I.V., Aleynikova, T.D., and Shavlovsky, M.M., Expression in E. coli and purification of the fibrillogenic fusion proteins TTR-sfGFP and beta2MsfGFP, Prep. Biochem. Biotechnol., 2011, vol. 41, pp. 337–349.
Solovyov, K.V., Kern, A.M., Grudinina, N.A., Aleynikova, T.D., Polyakov, D.S., Morozova, I.V., and Shavlovsky, M.M., Genetic structures and conditions of their expression, which allow receiving native recombinant proteins with high output, Int. J. Biomed., 2012, vol. 2, pp. 45–49.
Stopa, B., Piekarska, B., Konieczny, L., Rybarska, J., Spólnik, P., Zemanek, G., Roterman, I., and Król, M., The structure and protein binding of amyloid-specific dye reagents, Acta Biochimica Polonica, 2003, vol. 50, pp. 1213–1227.
Virchow, R., Ueber den Gang der amyloiden Degeneration, Archiv Path. Anat. Physiol. Klin. Med., 1855, vol. 8, pp. 364–368.
Virchow, R., Ueber eine im Gehirn und Rückenmark des Menschen aufgefundene Substanz mit der chemischen Reaction der Cellulose, Archiv Path. Anat. Physiol. Klin. Med., 1854, vol. 6, pp. 135–138.
Yaneva, Z.L. and Georgieva, N.V., Insights into Congo red adsorption on agro-industrial materials—spectral, equilibrium, kinetic, thermodynamic, dynamic and desorption studies, a review, Int. Rev. Chem. Eng., 2012, vol. 4, pp. 127–146.
Zhou, Q., Xie, C., Gong, W., Xu, N., and Zhou, W., Comments on the method of using maximum absorption wavelength to calculate Congo Red solution concentration published in J. Hazard. Mater., J. Hazard. Mater., 2011, vol. 198, pp. 381–382.
Author information
Authors and Affiliations
Corresponding author
Additional information
Original Russian Text © O.M. Zherelova, A.A. Kataev, V.M. Grischenko, R.Sh. Shtanchaev, 2016, published in Tsitologiya, 2016, Vol. 58, No. 8, pp. 646–654.
Rights and permissions
About this article
Cite this article
Zherelova, O.M., Kataev, A.A., Grischenko, V.M. et al. Haloperidol modulates ion transport in Chara corallina cells. Cell Tiss. Biol. 10, 476–485 (2016). https://doi.org/10.1134/S1990519X16060080
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1134/S1990519X16060080