Ukr.Biochem.J. 2014; Volume 86, Issue 6, Nov-Dec, pp. 154-166
doi: https://doi.org/10.15407/ubj86.06.154
Protective effect of tiacalix[4]arene-tetrasulphonate on heavy metal inhibition of myometrium myosin subfragment-1 ATP-hydrolase activity
R. D. Labyntsevа1, O. V. Bevza1, A. A. Bevza1, A. M. Lulko1,
S. Kharchenko2, V. I. Kalchenko2, S. O. Kosterin1
1Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
е-mail: labyntseva@biochem.kiev.ua; kinet@biochem.kiev.ua;
2Institute of Organic Chemistry, National Academy of Sciences of Ukraine, Kyiv;
е-mail: vik@ioch.kiev.ua
Heavy metals have a negative effect on the contractility of uterine smooth muscles (myometrium), these effects can lead to various pathologies of a women reproductive system. To overcome these effects the methods for correcting the myometrium contractile activity are to be developed. Catalyzed by myosin ATPase ATP hydrolysis is the most important reaction in the molecular mechanism of myometrium contraction. We have found an inhibitory effect of 0.03-0.3 mM Ni2+, Pb2+ and Cd2+ on enzymatic hydrolysis of ATP by myosin subfragment-1 obtained from swine uterine smooth muscles. We have demonstrated that 100 µM thiacalix[4]arene-tetrasulphonate (C-798) recovered to the control level of ATPase activity of myosin subfragment-1 in the presence of heavy metal cations. One of the most probable mechanisms of C-798 corrective activity is based on its ability to chelate heavy metals, thus cations Pb, Cd and Ni can be removed from the incubation medium. Computer simulation has demonstrated that the protective effect of C-798 may also be the result of weakening the interaction of heavy metal ions with amino acid residues of the myosin molecule near the active site of ATP hydrolase. The obtained results can be used for further research aimed at assessing the prospects of thiacalix[4]arene-tetrasulfonate as pharmacological compounds.
Keywords: ATPase activity, docking, heavy metals, myosin subfragment-1, smooth muscle, thiacalix[4]arene, uterus
References:
- Paran’ko NM, Belitskaia EN, Zemliakova TD, Shmatkov GG, Rublevskaia NI, Chub LE, Golovkova TA. Contribution of heavy metals to the development of reproductive disorders. Gig Sanit. 2002 Jan-Feb;(1):28-30. Russian. PubMed
- Serduk AM, Belitskaya EN, Paranko N, Shmatko GG. Heavy metals external environment and their impact on the reproductive function of women. Dnepropetrovsk: ART Press, 2004. 148 p. (In Russian).
- Dorea JG, Donangelo CM. Early (in uterus and infant) exposure to mercury and lead. Clin Nutr. 2006 Jun;25(3):369-76. Review. PubMed, CrossRef
- Bellinger DC, Burger J, Cade TJ, Cory-Slechta DA, Finkelstein M, Hu H, Kosnett M, Landrigan PJ, Lanphear B, Pokras MA, Redig PT, Rideout BA, Silbergeld E, Wright R, Smith DR. Health risks from lead-based ammunition in the environment. Environ Health Perspect. 2013 Jun;121(6):A178-9. PubMed, PubMedCentral, CrossRef
- Bires J, Maracek I, Bartko P, Biresova M, Weissova T. Accumulation of trace elements in sheep and the effects upon qualitative and quantitative ovarian changes. Vet Hum Toxicol. 1995 Aug;37(4):349-56. PubMed
- Vaktskjold A, Talykova LV, Chashchin VP, Odland JØ, Nieboer E. Spontaneous abortions among nickel-exposed female refinery workers. Int J Environ Health Res. 2008 Apr;18(2):99-115. PubMed, CrossRef
- Labyntseva RD, Ulyanenko TV, Kosterіn SA. Effect of heavy metal ions on superprecipitation and ATPase activity of uterine smooth muscle actomyosin activity. Ukr Biokhim Zhurn. 1998 Mar-Apr;70(2):71-7. Russian. PubMed
- Labyntseva RD, Bobrowska OM, Chunikhin OYu, Kosterin SO. Effect of heavy metal cations on ATPase activity of actomyosin complex and myosin subfragment-1 of smooth muscle of the uterus. Ukr Biokhim Zhurn. 2011 Jul-Sep;83(4):84-93. Ukrainian. PubMed
- Gutsche CD. Calixarenes: an introduction, monographs in supramolecular chemistry. Royal Society of Chemistry. Cambridge, 2008. 276 p.
- Morohashi N, Narumi F, Iki N, Hattori T, Miyano S. Thiacalixarenes. Chem Rev. 2006 Dec;106(12):5291-316. PubMed, CrossRef
- Calixarenes for Separations. Eds.: Lumetta GJ, Rogers RD, Gopalan AS. American Chemical Society. – Washington, 2000. 366 p. CrossRef
- Kalchenko VI, Rodik RV, Boyko VI. Calixarenes. Prospects for biomedical applications. J Org Farm Chem. 2005;3(4):13-29. (In Ukrainian).
- Veklich ТО, Kosterin SO, Rodik RV, Cherenok SO, Boyko VI, Kalchenko VI. Effect of calixarene-phosphonic acid on Na+, K+-ATPase activity in plasma membranes of the smooth-muscle cells. Ukr Biokhim Zhurn. 2006 Jan-Feb;78(1):70-78. (In Ukrainian). PubMed
- Cherenok S, Vovk A, Muravyova I, Shivanyuk A, Kukhar V, Lipkowski J, Kalchenko V. Calix[4]arene α-aminophosphonic acids: asymmetric synthesis and enantioselective inhibition of alkaline phosphatases. Org Lett. 2006 Feb 16;8(4):549-52. PubMed, CrossRef
- Phan G, Semili N, Bouvier-Capely C, Landon G, Mekhloufi G, Huang N, Rebière F, Agarande M, Fattal E. Calixarene cleansing formulation for uranium skin contamination. Health Phys. 2013 Oct;105(4):382-9. PubMed, CrossRef
- Nimse SB, Kim T. Biological applications of functionalized calixarenes. Chem Soc Rev. 2013 Jan 7;42(1):366-86. Review. Erratum in: Chem Soc Rev. 2012 Dec 21;41(24):8212. PubMed, CrossRef
- Iki N, Fujimoto T, Miyano SA. A New Water-Soluble Host Molecule Derived from Thiacalixarene. Chem Lett. 1998;27(7):625-6. CrossRef
- Iki N, Morohashi N, Narumi F, Miyano S. High Complexation Ability of Thiacalixarene with Transition Metal Ions. The Effect of Replacing Methylene Bridges of Tetra(p-t-butyl)calyx[4]arenetetrol by Epithio Groups. Bull Chem Soc Jpn. 1998;71(7):1597-1603. CrossRef
- Coleman AW, Perret F, Moussa M, Dupin M, Guo Y, Perron H. Calix[n]arenes as protein sensors. Top Curr Chem. 2007;277:31-88. CrossRef
- Bilyk A, Dunlop JW, Fuller RO, Hall AK, Harrowfield JM, Hosseini MW, Koutsantonis GA, Murray IW, Skelton BW, Stamps RL, White AH. Systematic structural coordination chemistry of p-t-butyltetrathiacalix[4]arene: further complexes of transition-metal ions. Eur J Inorg Chem. 2010 Apr;2010(14) :2106-26. CrossRef
- Weeds AG, Taylor RS. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature. 1975 Sep 4;257(5521):54-6. PubMed, CrossRef
- Chen PS, Toribara TY, Warner H. Microdetermination of phosphorus. Anal Chem. 1956 Nov;28(11):1756-8. CrossRef
- Korostylev PP. Preparation of solutions for chemical analytical work. Moscow: Nauka, 1964. 202 p. (In Russian).
- Cassidy CE, Setzer WN. Cancer-relevant biochemical targets of cytotoxic Lonchocarpus flavonoids: a molecular docking analysis. J Mol Model. 2010 Feb;16(2):311-26. PubMed, CrossRef
- Houdusse A, Kalabokis VN, Himmel D, Szent-Györgyi AG, Cohen C. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Cell. 1999 May 14;97(4):459-70. PubMed, CrossRef
- Li L, Jose J, Xiang Y, Kuhn RJ, Rossmann MG. Structural changes of envelope proteins during alphavirus fusion. Nature. 2010 Dec 2;468(7324):705-8. PubMed, PubMedCentral, CrossRef
- Krieger E, Koraimann G, Vriend G. Increasing the precision of comparative models with YASARA NOVA–a self-parameterizing force field. Proteins. 2002 May 15;47(3):393-402. PubMed, CrossRef
- Morohashi N, Iki N, Sugawara A, Miyano S. Selective oxidation of thiacalix[4]arenes to the sulfinyl or sulfonyl counterparts and their complexation abilities towards metal ions as studied by solvent extraction. Tetrahedron. 2001;57(26):5557-63. CrossRef
- Kofman E, Nankina VP. Some features of actomyosin superprecipitation and its possible mechanisms. By the book.: Biophysical and biochemical methods for investigating of muscle proteins. Leningrad: Leningrad State University, 1978. P. 82-86. (In Russian).
- Bugaenko LT, Ryabykh SM, Bugaenko AL. Almost complete system of average crystallographic ionic radii and its use for determining the ionization potentials. Vestn Mosk Univ. Series 2. Chemistry. 2008;4(6):363-383. (In Russian).
- Burghardt TP, Neff KL, Wieben ED, Ajtai K. Myosin individualized: single nucleotide polymorphisms in energy transduction. BMC Genomics. 2010 Mar 15;11:172. PubMed, PubMedCentral, CrossRef
- Risal D, Gourinath S, Himmel DM, Szent-Györgyi AG, Cohen C. Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding. Proc Natl Acad Sci USA. 2004 Jun 15;101(24):8930-5. PubMed, PubMedCentral, CrossRef
- Mustafina AR, Skripacheva VV, Konovalov AI. Outer-sphere association of calixarenes and other macrocyclic ligands with metal complexes as a basis for designing of molecular devices. Usp Chim. 2007;76(10):979-993. (In Russian).
