About Mechanism of Antihemolitic Action of Chlorpromazine Under Posthypertonic Stress in Erythrocytes

Ekaterina A. Semionova, Elena A. Chabanenko, Natalia V. Orlova, Pavel M. Zubov, Natalia M. Shpakova

Abstract


The research was performed to reveal an antihemolytic effect of chlorpromazine (CPZ) under post-hypertonic stress (PHS) of human erythrocyte depending on the substances present at different stages of experiment (pre-treatment, dehydration, rehydration) as well as the effect of CPZ on the redistribution of phosphatidylserine in erythrocyte membrane bilayer. It has been shown that pre-treatment of erythrocytes with CPZ at a concentration of 180 mmol/l did not lead to antihemolytic effect of the substance under PHS of erythrocytes. It has been established that CPZ under concentration of 100-300 mmol/l did not cause a transbilayer redistribution of phosphatidylserine molecules in erythrocyte membranes. Protective effect of CPZ was implemented following transfer of the cells from the dehydration medium (1.75 mol/l NaCl) into rehydration one (0.15 mol/l NaCl), containing CPZ, i. e.at the moment of stress action. Consequently, the mechanism of antihemolytic action of CPZ under PHS of erythrocytes was associated with the membrane reorganization during an incorporation of the substance molecules into it.

Probl Cryobiol Cryomed 2017; 27(3): 219–229


Keywords


erythrocytes; human; posthypertonic stress; pre-treatment; dehydration; rehydration; chlorpromazine; phosphatidylserine

Full Text:

PDF

References


Ahyayauch H., Bennouna M., Alonso A., Goni F.M. Detergent effects on membranes at subsolubilizing concentrations: transmembrane lipid motion, bilayer permeabilization, and vesicle lysis/reassembly are independent phenomena. Langmuir 2010; 26(10): 7307–7313. CrossRef PubMed

Ahyayaucha H., Gallego M., Casis O., Bennouna M. Changes in erythrocyte morphology induced by imipramine and chlorpromazine. J Physiol Biochem 2006; 62(3): 199–205. CrossRef PubMed

Akel A., Hermle T., Niemoeller O.M. et al. Stimulation of erythrocyte phosphatidylserine exposure by chlorpromazine. Eur J Pharmacol 2006; 532(1): 11–17. CrossRef PubMed

Belous A.M., Bondarenko V.A., Babijchuk L.A. et al. The common mechanism of damage of cell subjected to termal shock, freezing and posthypertonic lysis. Kriobiologiya 1985; (2): 25–32.

Carafoli E., Krebs J. Why Calcium? How Calcium Became the Best Communicator. J Biol Chem 2016; 291(40): 20849–20857. CrossRef PubMed

Dunayevskaya O.N., Pantaler E.R., Shpakova N.M., Bondarenko V.A. Some possible methods of increasing red blood cell stability to the action of cold and osmotic effects after application of cation amphipates. Probl Cryobiol 1995; (1): 21–26.

Enomoto A., Takakuwa Y., Manno S. et al. Regulation of erythrocyte ghost membrane mechanical stability by chlorpromazine. Biochim Biophys Acta 2001; 1512(2): 285–290. CrossRef

Ficarra S., Russo A., Barreca D. et al. Short-term effects of chlorpromazine on oxidative stress in erythrocyte functionality: activation of metabolism and membrane perturbation. Oxid Med Cell Longev 2016; 2016: 10 p. [веб-сайт] https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4992801/ (cited 8.08.2016).

Fuller B.J., Lane N., Benson E.E., editors. Life in the frozen state. Boca Raton, London, New York, Washington, D.C.: CRC Press; 2004.

Gancedo J.M. Biological roles of cAMP: variations on a theme in the different kingdoms of life. Biol Rev Camb Philos Soc 2013; 88(3): 645–668. CrossRef PubMed

Gordienko E.A., Gordienko O.I., Kuleshova L.G., Rozanov L.F. Mechanisms of protecting cells from damage with extra- and intracellular ice In: Goltsev A.N., editor. Current problems of cryobiology and cryomedicine. Kharkiv, 2012. p. 9–44.

Gordienko E.A., Tovstyak V.V. Physics of biological membranes: a tutorial. Кyiv: Nauk Dumka; 2009.

Hagerstrand H., Holmstrom T.H., Bobrowska-Hagerstrand M. et al. Amphiphile-induced phosphatidylserine exposure in human erythrocytes. Mol Membr Biol 1998; 15(2): 89–95. CrossRef PubMed

Iershov S.S., Pysarenko N.A., Orlova N.V., Shpakova N.M. Effect of cationic and anionic amphiphilic compounds on hypertonic cryohemolysis of mammalian red blood cells. Fiziol Zh. 2007; 53(6): 78–84.

Jiang Y.W., Gao G., Chen Z., Wu F.G. Fluorescence studies on the interaction between chlorpromazine and model cell membranes. New J Chem 2017; 41(10): 4048–4057. CrossRef

Kawamura H., Arai M., Togari A. Inhibitory effect of chlorpromazine on RANKL-induced osteoclastogenesis in mouse bone marrow cells. Pharmacol Sci 2011; 117(1): 54–62. CrossRef

Koka S., Lang C., Boini K.M. et al. Influence of chlorpromazine on eryptosis, parasitemia and survival of Plasmodium berghe infected mice. Cell Physiol Biochem 2008; 22(1–4): 261–268.

Lieber M.R., Steck T.L. Dynamics of the holes in human erythrocyte membrane ghosts. J Biol Chem 1982; 257(19): 11660–11666.

Lubker C., Seifert R. Effects of 39 Compounds on CalmodulinRegulated Adenylyl Cyclases AC1 and Bacillus anthracis Edema Factor. PLoS One 2015; 10(5): e0124017.

Martins P.T., Velazquez-Campoy A., Vaz W.L. et al. Kinetics and thermodynamics of chlorpromazine interaction with lipid bilayers: effect of charge and cholesterol. J Am Chem Soc 2012; 134(9): 4184–4195. CrossRef PubMed

Muldrew K. The salting-in hypothesis of post-hypertonic lysis. Cryobiology 2008; 57(3): 251–256. CrossRef PubMed

Nussio M.R., Sykes M.J., Miners J.O., Shapter J.G. Kinetics membrane disruption due to drug interactions of chlorpromazine hydrochloride. Langmuir 2009; 25(2): 1086–1090. CrossRef PubMed

Olejnik O.A., Ramazanov V.V., Bondarenko V.A. Posthypertonic lysis of modified erythrocytes in citrate medium. Probl Cryobiol 2003; (1): 21-29.

Reinhart W.H., Lubszky S., Thony S., Schulzki T. Interaction of injectable neurotropic drugs with the red cell membrane. Toxicol In Vitro 2014; 28(7): 1274–1279. CrossRef PubMed

Roy A., Ye J., Deng F., Wang Q.J. Protein kinase D signaling in cancer: A friend or foe? Biochim Biophys Acta 2017; 1868(1): 283–294.

Rudenko S.V. Erythrocyte morphological states, phases, transitions and trajectories. Biochim Biophys Acta 2010; 1798(9): 1767–1778. CrossRef PubMed

Semionova E.A., Iershova N.A., Orlova N.V., Shpakova N.M. Hypotonic lysis of mammalian erythrocytes in chlorpromazine presence. EESJ 2016 (2): 7–17.

Semionova E.A., Yershova N.A., Yershov S.S., Orlova N.V., Shpakova N.M. Peculiarities of posthypertonic lysis in erythrocytes of several mammals. Probl Cryobiol Cryomed 2016; 26(1): 73–83. CrossRef

Semionova Y.A., Zemlyanskikh N.G., Orlova N.V., Shpakova N.M. Antihemolytic efficiency of chlorpromazine under posthypertonic shock and glycerol removal from erythrocytes after thawing. Probl Cryobiol Cryomed 2017; 27(1): 51–60. CrossRef

Shpakova N.M., Bondarenko V.A. The effect of chlorpromazine on the temperature and osmotic sensitivity of erythrocytes. Biokhimiia (Moscow, Russia) 1991; 56(12): 2125–2130.

Shpakova N.M., Ershov S.S., Nipot O.E. To the question about possible correlation between release of К+ions and development of hemolytic damage of mammalian erythrocytes under hypertonic cryohemolysis. Animal Biology 2008;10(1–2): 164–170.

Shpakova N.M., Pantaler E.R., Bondarenko V.A. Antihemolytic effect of chlorpromazine on erythrocytes in hyperosmotic and cold shock. Biokhimiia (Moscow, Russia) 1995; 60(10): 1624–1631.

Song C., Holmsen H., Nerdal W. Existence of lipid microdomains in bilayer of dipalmitoyl phosphatidylcholine (DPPC) and 1-stearoyl-2-docosahexenoyl phosphatidylserine (SDPS) and their perturbation by chlorpromazine: a 13C and 31P solid-state NMR study. Biophys Chem 2006;120(3): 178–187. CrossRef PubMed

Suwalsky M., Villena F., Sotomayor C.P. et al. Human cells and cell membrane molecular models are affected in vitro by chlorpromazine. Biophys Chem 2008; 135(1–3): 7–13.

Takemoto-Kimura S., Suzuki K., Horigane S.I. et al.. Calmodulin kinases: essential regulators in health and disease. J Neurochem 2017; 141(6): 808–818. CrossRef PubMed

Tsymbal L.V., Orlova N.V., Shpakova N.M. Modification of the structure-functional state of erythrocyte membranes by chlorpromazine. Biochemistry (Moscow) Supplement. Series A: Membrane and Cell Biology 2005; 22(4): 327–335.

van Genderen H.O., Kenis H., Hofstra L. Extracellular annexin A5: functions of phosphatidylserine-binding and two-dimensional crystallization. Biochim Biophys Acta 2008; 1783(6): 953–963. CrossRef PubMed




DOI: https://doi.org/10.15407%2Fcryo27.03.219

Refbacks

  • There are currently no refbacks.


Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.

 

Institute for Problems of Cryobiology and Cryomedicine

23, Pereyaslavskaya str., Kharkov, Ukraine

Tel. +38057 373 4143; Fax +38057 373 5952

e-mail: journal@cryo.org.ua