Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase Activity
Abstract Numerous female reproductive abnormalities are caused by uterine smooth muscle (myometrium) disorders. Heavy metals have an adverse effect on the contractility of the uterine smooth muscle. Although zinc is an essential biogenic element for most of the organisms, high doses of this element...
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| Format: | Article |
| Language: | English |
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SpringerOpen
2018-07-01
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| Series: | Nanoscale Research Letters |
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| Online Access: | http://link.springer.com/article/10.1186/s11671-018-2630-2 |
| _version_ | 1797719083139989504 |
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| author | Raisa Labyntsevа Viktoriia Yavorovska Olexander Bevza Andriy Drapaylo Vitaly Kalchenko Sergiy Kosterin |
| author_facet | Raisa Labyntsevа Viktoriia Yavorovska Olexander Bevza Andriy Drapaylo Vitaly Kalchenko Sergiy Kosterin |
| author_sort | Raisa Labyntsevа |
| collection | DOAJ |
| description | Abstract Numerous female reproductive abnormalities are caused by uterine smooth muscle (myometrium) disorders. Heavy metals have an adverse effect on the contractility of the uterine smooth muscle. Although zinc is an essential biogenic element for most of the organisms, high doses of this element are toxic. The study of 0.5−5 mM Zn2+ effect on myosin S1 ATPase activity from the uterus found that 5 mM Zn2+ cations have the most pronounced inhibitory effect. The calculation of the kinetic parameters (K m and V max, ATP) revealed that the apparent maximum velocity of the hydrolysis ATP catalyzed by myosin in the presence of 5 mM Zn2+ decreased by 1.6 times. The value of К m for ATP hydrolysis by myosin S1 in the presence of Zn2+ does not change statistically, although it tends to decrease. It was determined that uterine myosin S1 ATPase activity does not depend on the concentration of Mg2+ in the presence of 5 mM Zn2+. Also, it was demonstrated that tetrahydroxythiacalix[4]arene-tetrasulfosphonate (C-798) and tetrahydroxythiacalix[4]arene-tetraphosphonate (C-800) restored myosin S1 ATPase activity to the control level in the presence of 5 mM Zn2+. One of the most probable mechanisms of restoring the action of these thiacalix[4]arenes protective effect is based on its ability to chelate heavy metal cations from the incubation medium. The molecular docking of C-798 and C-800 into the myosin S1 region showed that these thiacalix[4]arenes could interact with Zn cation bond by myosin amino acid residues near the ATPase active site. Therefore, thiacalix[4]arenes may weaken the interaction between this cation and myosin S1. It was speculated that the obtained results could be used for further research with the aim of using this thiacalix[4]arenes as pharmacological compounds in the case of poisoning with high concentrations of zinc. |
| first_indexed | 2024-03-12T09:00:27Z |
| format | Article |
| id | doaj.art-5160757b3f3b4138a6810381e42d4586 |
| institution | Directory Open Access Journal |
| issn | 1931-7573 1556-276X |
| language | English |
| last_indexed | 2024-03-12T09:00:27Z |
| publishDate | 2018-07-01 |
| publisher | SpringerOpen |
| record_format | Article |
| series | Nanoscale Research Letters |
| spelling | doaj.art-5160757b3f3b4138a6810381e42d45862023-09-02T15:42:48ZengSpringerOpenNanoscale Research Letters1931-75731556-276X2018-07-0113111010.1186/s11671-018-2630-2Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase ActivityRaisa Labyntsevа0Viktoriia Yavorovska1Olexander Bevza2Andriy Drapaylo3Vitaly Kalchenko4Sergiy Kosterin5Palladin Institute of Biochemistry, National Academy of Sciences of UkrainePalladin Institute of Biochemistry, National Academy of Sciences of UkrainePalladin Institute of Biochemistry, National Academy of Sciences of UkraineInstitute of Organic Chemistry, National Academy of Sciences of UkraineInstitute of Organic Chemistry, National Academy of Sciences of UkrainePalladin Institute of Biochemistry, National Academy of Sciences of UkraineAbstract Numerous female reproductive abnormalities are caused by uterine smooth muscle (myometrium) disorders. Heavy metals have an adverse effect on the contractility of the uterine smooth muscle. Although zinc is an essential biogenic element for most of the organisms, high doses of this element are toxic. The study of 0.5−5 mM Zn2+ effect on myosin S1 ATPase activity from the uterus found that 5 mM Zn2+ cations have the most pronounced inhibitory effect. The calculation of the kinetic parameters (K m and V max, ATP) revealed that the apparent maximum velocity of the hydrolysis ATP catalyzed by myosin in the presence of 5 mM Zn2+ decreased by 1.6 times. The value of К m for ATP hydrolysis by myosin S1 in the presence of Zn2+ does not change statistically, although it tends to decrease. It was determined that uterine myosin S1 ATPase activity does not depend on the concentration of Mg2+ in the presence of 5 mM Zn2+. Also, it was demonstrated that tetrahydroxythiacalix[4]arene-tetrasulfosphonate (C-798) and tetrahydroxythiacalix[4]arene-tetraphosphonate (C-800) restored myosin S1 ATPase activity to the control level in the presence of 5 mM Zn2+. One of the most probable mechanisms of restoring the action of these thiacalix[4]arenes protective effect is based on its ability to chelate heavy metal cations from the incubation medium. The molecular docking of C-798 and C-800 into the myosin S1 region showed that these thiacalix[4]arenes could interact with Zn cation bond by myosin amino acid residues near the ATPase active site. Therefore, thiacalix[4]arenes may weaken the interaction between this cation and myosin S1. It was speculated that the obtained results could be used for further research with the aim of using this thiacalix[4]arenes as pharmacological compounds in the case of poisoning with high concentrations of zinc.http://link.springer.com/article/10.1186/s11671-018-2630-2Myosin S1ZnThiacalix[4]arenesATPase activityMolecular dockingSmooth muscle |
| spellingShingle | Raisa Labyntsevа Viktoriia Yavorovska Olexander Bevza Andriy Drapaylo Vitaly Kalchenko Sergiy Kosterin Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase Activity Nanoscale Research Letters Myosin S1 Zn Thiacalix[4]arenes ATPase activity Molecular docking Smooth muscle |
| title | Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase Activity |
| title_full | Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase Activity |
| title_fullStr | Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase Activity |
| title_full_unstemmed | Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase Activity |
| title_short | Thiacalix[4]arenes Remove the Inhibitory Effects of Zn Cations on the Myosin ATPase Activity |
| title_sort | thiacalix 4 arenes remove the inhibitory effects of zn cations on the myosin atpase activity |
| topic | Myosin S1 Zn Thiacalix[4]arenes ATPase activity Molecular docking Smooth muscle |
| url | http://link.springer.com/article/10.1186/s11671-018-2630-2 |
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