Inorganic polyphosphate regulates functions of thymocytes via activation of P2X purinoreceptors
Inorganic polyphosphate (polyP) is an ancient polymer, which was proven to be a signalling molecule in the mammalian brain, mediating the communication between astrocytes via activation of P2Y purinoreceptors and modulating the activity of neurons. There is very limited information regarding the abi...
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| Published in | Biochimica et biophysica acta. General subjects Vol. 1868; no. 1; p. 130523 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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| Abstract | Inorganic polyphosphate (polyP) is an ancient polymer, which was proven to be a signalling molecule in the mammalian brain, mediating the communication between astrocytes via activation of P2Y
purinoreceptors and modulating the activity of neurons. There is very limited information regarding the ability of polyP to transmit the information as an agonist of purinoreceptors in other cells and tissues. Here, we show that application of polyP to the suspension of primary thymocytes increases the concentration of intracellular calcium. PolyP evoked calcium signal was dependent on the presence of P2X inhibitors but not P2Y
inhibitor. PolyP dependent increase in intracellular calcium concentration caused mild mitochondrial depolarization, which was dependent on inhibitors of purinoreceptors, extracellular calcium and inhibitor of mitochondrial calcium uniporter but wasn't dependent on cyclosporin A. Application of polyP modulated cell volume regulation machinery of thymocytes in calcium dependent manner. Molecular docking experiments revealed that polyP can potentially bind to several types of P2X receptors with binding energy similar to ATP - natural agonist of P2X purinoreceptors. Further molecular dynamics simulations with P2X
showed that binding of one molecule of polyP dramatically increases permeability of this receptor-channel for water molecules. Thus, in this research we for the first time showed that polyP can interact with P2X receptors in thymocytes and modulate physiological processes. |
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| AbstractList | Inorganic polyphosphate (polyP) is an ancient polymer, which was proven to be a signalling molecule in the mammalian brain, mediating the communication between astrocytes via activation of P2Y
purinoreceptors and modulating the activity of neurons. There is very limited information regarding the ability of polyP to transmit the information as an agonist of purinoreceptors in other cells and tissues. Here, we show that application of polyP to the suspension of primary thymocytes increases the concentration of intracellular calcium. PolyP evoked calcium signal was dependent on the presence of P2X inhibitors but not P2Y
inhibitor. PolyP dependent increase in intracellular calcium concentration caused mild mitochondrial depolarization, which was dependent on inhibitors of purinoreceptors, extracellular calcium and inhibitor of mitochondrial calcium uniporter but wasn't dependent on cyclosporin A. Application of polyP modulated cell volume regulation machinery of thymocytes in calcium dependent manner. Molecular docking experiments revealed that polyP can potentially bind to several types of P2X receptors with binding energy similar to ATP - natural agonist of P2X purinoreceptors. Further molecular dynamics simulations with P2X
showed that binding of one molecule of polyP dramatically increases permeability of this receptor-channel for water molecules. Thus, in this research we for the first time showed that polyP can interact with P2X receptors in thymocytes and modulate physiological processes. Inorganic polyphosphate (polyP) is an ancient polymer, which was proven to be a signalling molecule in the mammalian brain, mediating the communication between astrocytes via activation of P2Y1 purinoreceptors and modulating the activity of neurons. There is very limited information regarding the ability of polyP to transmit the information as an agonist of purinoreceptors in other cells and tissues. Here, we show that application of polyP to the suspension of primary thymocytes increases the concentration of intracellular calcium. PolyP evoked calcium signal was dependent on the presence of P2X inhibitors but not P2Y1 inhibitor. PolyP dependent increase in intracellular calcium concentration caused mild mitochondrial depolarization, which was dependent on inhibitors of purinoreceptors, extracellular calcium and inhibitor of mitochondrial calcium uniporter but wasn't dependent on cyclosporin A. Application of polyP modulated cell volume regulation machinery of thymocytes in calcium dependent manner. Molecular docking experiments revealed that polyP can potentially bind to several types of P2X receptors with binding energy similar to ATP - natural agonist of P2X purinoreceptors. Further molecular dynamics simulations with P2X4 showed that binding of one molecule of polyP dramatically increases permeability of this receptor-channel for water molecules. Thus, in this research we for the first time showed that polyP can interact with P2X receptors in thymocytes and modulate physiological processes. |
| ArticleNumber | 130523 |
| Author | Rustamov, Khondamir R Charishnikova, Oksana S Baev, Artyom Y Makhmudov, Albert R Rakhmatullina, Nigina S H Mirkhodjaev, Ulugbek Z Sabirov, Ravshan Z Nebesnaya, Kamila S Rustamova, Sarvinoz I |
| Author_xml | – sequence: 1 givenname: Kamila S surname: Nebesnaya fullname: Nebesnaya, Kamila S organization: Laboratory of Experimental Biophysics, Centre for Advanced Technologies, Tashkent, Uzbekistan; Department of Biophysics, Faculty of Biology, National University of Uzbekistan, Tashkent, Uzbekistan – sequence: 2 givenname: Albert R surname: Makhmudov fullname: Makhmudov, Albert R organization: Laboratory of Experimental Biophysics, Centre for Advanced Technologies, Tashkent, Uzbekistan – sequence: 3 givenname: Khondamir R surname: Rustamov fullname: Rustamov, Khondamir R organization: Laboratory of Experimental Biophysics, Centre for Advanced Technologies, Tashkent, Uzbekistan; Department of Biophysics, Faculty of Biology, National University of Uzbekistan, Tashkent, Uzbekistan – sequence: 4 givenname: Nigina S H surname: Rakhmatullina fullname: Rakhmatullina, Nigina S H organization: Laboratory of Experimental Biophysics, Centre for Advanced Technologies, Tashkent, Uzbekistan – sequence: 5 givenname: Sarvinoz I surname: Rustamova fullname: Rustamova, Sarvinoz I organization: Institute of Biophysics and Biochemistry, National University of Uzbekistan, Tashkent, Uzbekistan – sequence: 6 givenname: Ulugbek Z surname: Mirkhodjaev fullname: Mirkhodjaev, Ulugbek Z organization: Department of Biophysics, Faculty of Biology, National University of Uzbekistan, Tashkent, Uzbekistan – sequence: 7 givenname: Oksana S surname: Charishnikova fullname: Charishnikova, Oksana S organization: Laboratory of Experimental Biophysics, Centre for Advanced Technologies, Tashkent, Uzbekistan – sequence: 8 givenname: Ravshan Z surname: Sabirov fullname: Sabirov, Ravshan Z organization: Institute of Biophysics and Biochemistry, National University of Uzbekistan, Tashkent, Uzbekistan – sequence: 9 givenname: Artyom Y surname: Baev fullname: Baev, Artyom Y email: baev.a.yu@gmail.com organization: Laboratory of Experimental Biophysics, Centre for Advanced Technologies, Tashkent, Uzbekistan; Department of Biophysics, Faculty of Biology, National University of Uzbekistan, Tashkent, Uzbekistan. Electronic address: baev.a.yu@gmail.com |
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| Keywords | Inorganic polyphosphate Thymocytes Purinoreceptors P2X |
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| Title | Inorganic polyphosphate regulates functions of thymocytes via activation of P2X purinoreceptors |
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