Inhibition of Na(+),K(+)-ATPase and activation of myosin ATPase by calix[4]arene C-107 cause stimulation of isolated smooth muscle contractile activity
The discovery of compounds that might modify myometrial contractility is an important area of researches. In our previous experiments, we found that some representatives of macrocyclic compounds family – calix[4]arenes – can modify the enzymatic and transport activity of membrane-bound cation-trans...
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| Format: | Article |
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National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry
2020-02-01
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| Series: | The Ukrainian Biochemical Journal |
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| Online Access: | http://ukrbiochemjournal.org/wp-content/uploads/2020/02/Veklich_1_20.pdf |
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| author | T. O. Veklich R. D. Labyntseva O. A. Shkrabak O. V. Tsymbalyuk R. V. Rodik V. I. Kalchenko S. O. Kosterin |
| author_facet | T. O. Veklich R. D. Labyntseva O. A. Shkrabak O. V. Tsymbalyuk R. V. Rodik V. I. Kalchenko S. O. Kosterin |
| author_sort | T. O. Veklich |
| collection | DOAJ |
| description | The discovery of compounds that might modify myometrial contractility is an important area of researches. In our previous experiments, we found that some representatives of macrocyclic compounds family – calix[4]arenes – can modify the enzymatic and transport activity of membrane-bound cation-transport ATP hydrolases. The aim of this work was to study and compare the effect of calix[4]arene C-107 on the enzymatic activities of Mg2+-dependent ATPases of the uterine smooth muscle, namely: ouabain-sensitive Na+,K+-ATPase, plasma membrane Ca2+-independent “basal” Mg2+-ATPase, ATPase of the actomyosin complex and myosin subfragment-1, with effect on the contractile activity of the myometrium. It was shown that calix[4]arene C-107 efficiently inhibited myometrium Na+,K+-ATPase (I50 = 54 ± 6 nM) selectively to other ATP-hydrolases of the plasma membrane and simultaneously activated the enzymatic activity of the myosin ATPase of smooth muscles (A50 = 9.6 ± 0.7 μM). Such reciprocal biochemical effects led to the stimulation of the smooth muscle contractile activity that was demonstrated by the tensometric method using different isolated smooth muscles. Calix[4]arene С-107 was shown to stimulate the increase of the tonic component of myometrium contractions induced by oxytocin, as well as contractions of the caecum muscles induced by high-potassium solution or acetylcholine, and to maintain increased tension for a long time. Thus, calix[4]arene C-107 is a prospective compound for enhancing the smooth muscle basal tone and/or contraction in case of hypotonic dysfunctions. |
| first_indexed | 2024-03-09T07:30:12Z |
| format | Article |
| id | doaj.art-6034d4bccfaa413ca139909ac9521a12 |
| institution | Directory Open Access Journal |
| issn | 2409-4943 2413-5003 |
| language | English |
| last_indexed | 2024-03-09T07:30:12Z |
| publishDate | 2020-02-01 |
| publisher | National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry |
| record_format | Article |
| series | The Ukrainian Biochemical Journal |
| spelling | doaj.art-6034d4bccfaa413ca139909ac9521a122023-12-03T06:26:56ZengNational Academy of Sciences of Ukraine, Palladin Institute of BiochemistryThe Ukrainian Biochemical Journal2409-49432413-50032020-02-01921213010.15407/ubj92.01.021Inhibition of Na(+),K(+)-ATPase and activation of myosin ATPase by calix[4]arene C-107 cause stimulation of isolated smooth muscle contractile activityT. O. Veklich0R. D. Labyntseva1O. A. Shkrabak2O. V. Tsymbalyuk3R. V. Rodik4V. I. Kalchenko5S. O. Kosterin6Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, KyivInstitute of High Technologies, Taras Shevchenko National University of Kyiv, UkraineInstitute of Organic Chemistry, National Academy of Sciences of Ukraine, KyivInstitute of Organic Chemistry, National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, KyivThe discovery of compounds that might modify myometrial contractility is an important area of researches. In our previous experiments, we found that some representatives of macrocyclic compounds family – calix[4]arenes – can modify the enzymatic and transport activity of membrane-bound cation-transport ATP hydrolases. The aim of this work was to study and compare the effect of calix[4]arene C-107 on the enzymatic activities of Mg2+-dependent ATPases of the uterine smooth muscle, namely: ouabain-sensitive Na+,K+-ATPase, plasma membrane Ca2+-independent “basal” Mg2+-ATPase, ATPase of the actomyosin complex and myosin subfragment-1, with effect on the contractile activity of the myometrium. It was shown that calix[4]arene C-107 efficiently inhibited myometrium Na+,K+-ATPase (I50 = 54 ± 6 nM) selectively to other ATP-hydrolases of the plasma membrane and simultaneously activated the enzymatic activity of the myosin ATPase of smooth muscles (A50 = 9.6 ± 0.7 μM). Such reciprocal biochemical effects led to the stimulation of the smooth muscle contractile activity that was demonstrated by the tensometric method using different isolated smooth muscles. Calix[4]arene С-107 was shown to stimulate the increase of the tonic component of myometrium contractions induced by oxytocin, as well as contractions of the caecum muscles induced by high-potassium solution or acetylcholine, and to maintain increased tension for a long time. Thus, calix[4]arene C-107 is a prospective compound for enhancing the smooth muscle basal tone and/or contraction in case of hypotonic dysfunctions.http://ukrbiochemjournal.org/wp-content/uploads/2020/02/Veklich_1_20.pdfcalix[4]arenemg(2+)-атраsemyometriummyosin atpasenа(+)_k(+)-атраseplasma membranesmooth muscle cell |
| spellingShingle | T. O. Veklich R. D. Labyntseva O. A. Shkrabak O. V. Tsymbalyuk R. V. Rodik V. I. Kalchenko S. O. Kosterin Inhibition of Na(+),K(+)-ATPase and activation of myosin ATPase by calix[4]arene C-107 cause stimulation of isolated smooth muscle contractile activity The Ukrainian Biochemical Journal calix[4]arene mg(2+)-атраse myometrium myosin atpase nа(+)_k(+)-атраse plasma membrane smooth muscle cell |
| title | Inhibition of Na(+),K(+)-ATPase and activation of myosin ATPase by calix[4]arene C-107 cause stimulation of isolated smooth muscle contractile activity |
| title_full | Inhibition of Na(+),K(+)-ATPase and activation of myosin ATPase by calix[4]arene C-107 cause stimulation of isolated smooth muscle contractile activity |
| title_fullStr | Inhibition of Na(+),K(+)-ATPase and activation of myosin ATPase by calix[4]arene C-107 cause stimulation of isolated smooth muscle contractile activity |
| title_full_unstemmed | Inhibition of Na(+),K(+)-ATPase and activation of myosin ATPase by calix[4]arene C-107 cause stimulation of isolated smooth muscle contractile activity |
| title_short | Inhibition of Na(+),K(+)-ATPase and activation of myosin ATPase by calix[4]arene C-107 cause stimulation of isolated smooth muscle contractile activity |
| title_sort | inhibition of na k atpase and activation of myosin atpase by calix 4 arene c 107 cause stimulation of isolated smooth muscle contractile activity |
| topic | calix[4]arene mg(2+)-атраse myometrium myosin atpase nа(+)_k(+)-атраse plasma membrane smooth muscle cell |
| url | http://ukrbiochemjournal.org/wp-content/uploads/2020/02/Veklich_1_20.pdf |
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