Pathophysiological Role of S-Nitrosylation and Transnitrosylation Depending on S-Nitrosoglutathione Levels Regulated by S-Nitrosoglutathione Reductase
Nitric oxide (NO) mediates various physiological and pathological processes, including cell proliferation, differentiation, and inflammation. Protein S-nitrosylation (SNO), a NO-mediated reversible protein modification, leads to changes in the activity and function of target proteins. Recent finding...
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| Published in | Biomolecules & therapeutics Vol. 26; no. 6; pp. 533 - 538 |
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| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
Korea (South)
The Korean Society of Applied Pharmacology
01.11.2018
한국응용약물학회 |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1976-9148 2005-4483 |
| DOI | 10.4062/biomolther.2018.179 |
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| Abstract | Nitric oxide (NO) mediates various physiological and pathological processes, including cell proliferation, differentiation, and inflammation. Protein S-nitrosylation (SNO), a NO-mediated reversible protein modification, leads to changes in the activity and function of target proteins. Recent findings on protein-protein transnitrosylation reactions (transfer of an NO group from one protein to another) have unveiled the mechanism of NO modulation of specific signaling pathways. The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. Increasing number of GSNOR-related studies have shown the important role that denitrosylation plays in cellular NO/SNO homeostasis and human pathophysiology. This review introduces recent evidence of GSNO-mediated NO/SNO signaling depending on GSNOR expression or activity. In addition, the applicability of GSNOR as a target for drug therapy will be discussed in this review. |
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| AbstractList | Nitric oxide (NO) mediates various physiological and pathological processes, including cell proliferation, differentiation, and inflammation.
Protein S-nitrosylation (SNO), a NO-mediated reversible protein modification, leads to changes in the activity and function of target proteins. Recent findings on protein-protein transnitrosylation reactions (transfer of an NO group from one protein to another) have unveiled the mechanism of NO modulation of specific signaling pathways. The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling.
Increasing number of GSNOR-related studies have shown the important role that denitrosylation plays in cellular NO/SNO homeostasis and human pathophysiology. This review introduces recent evidence of GSNO-mediated NO/SNO signaling depending on GSNOR expression or activity. In addition, the applicability of GSNOR as a target for drug therapy will be discussed in this review. KCI Citation Count: 11 Nitric oxide (NO) mediates various physiological and pathological processes, including cell proliferation, differentiation, and inflammation. Protein S-nitrosylation (SNO), a NO-mediated reversible protein modification, leads to changes in the activity and function of target proteins. Recent findings on protein-protein transnitrosylation reactions (transfer of an NO group from one protein to another) have unveiled the mechanism of NO modulation of specific signaling pathways. The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. Increasing number of GSNOR-related studies have shown the important role that denitrosylation plays in cellular NO/SNO homeostasis and human pathophysiology. This review introduces recent evidence of GSNO-mediated NO/SNO signaling depending on GSNOR expression or activity. In addition, the applicability of GSNOR as a target for drug therapy will be discussed in this review.Nitric oxide (NO) mediates various physiological and pathological processes, including cell proliferation, differentiation, and inflammation. Protein S-nitrosylation (SNO), a NO-mediated reversible protein modification, leads to changes in the activity and function of target proteins. Recent findings on protein-protein transnitrosylation reactions (transfer of an NO group from one protein to another) have unveiled the mechanism of NO modulation of specific signaling pathways. The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. Increasing number of GSNOR-related studies have shown the important role that denitrosylation plays in cellular NO/SNO homeostasis and human pathophysiology. This review introduces recent evidence of GSNO-mediated NO/SNO signaling depending on GSNOR expression or activity. In addition, the applicability of GSNOR as a target for drug therapy will be discussed in this review. Nitric oxide (NO) mediates various physiological and pathological processes, including cell proliferation, differentiation, and inflammation. Protein S-nitrosylation (SNO), a NO-mediated reversible protein modification, leads to changes in the activity and function of target proteins. Recent findings on protein-protein transnitrosylation reactions (transfer of an NO group from one protein to another) have unveiled the mechanism of NO modulation of specific signaling pathways. The intracellular level of S-nitrosoglutathione (GSNO), a major reactive NO species, is controlled by GSNO reductase (GSNOR), a major regulator of NO/SNO signaling. Increasing number of GSNOR-related studies have shown the important role that denitrosylation plays in cellular NO/SNO homeostasis and human pathophysiology. This review introduces recent evidence of GSNO-mediated NO/SNO signaling depending on GSNOR expression or activity. In addition, the applicability of GSNOR as a target for drug therapy will be discussed in this review. |
| Author | Choi, Min Sik |
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| Cites_doi | 10.2174/1389557053175399 10.1164/rccm.200901-0158OC 10.1073/pnas.0804852105 10.1016/j.cbpa.2010.10.012 10.1074/jbc.M807125200 10.1016/S0301-4622(02)00092-3 10.1016/j.cbi.2011.01.028 10.4062/biomolther.2010.18.4.351 10.4062/biomolther.2011.19.4.419 10.1016/j.neuron.2005.03.028 10.1089/ars.2013.5696 10.1126/science.1093891 10.4062/biomolther.2013.029 10.1038/364626a0 10.1177/1074248415626300 10.1016/j.bmcl.2012.01.047 10.1016/j.neuron.2006.11.023 10.1016/j.yexmp.2009.03.001 10.1038/35054560 10.3109/10715762.2014.906743 10.1074/mcp.M110.000034 10.1073/pnas.1113319109 10.1073/pnas.1105172108 10.1038/nchembio720 10.1016/S0009-8981(03)00046-9 10.1038/nature04782 10.1038/71090 10.1126/science.1073634 10.1016/j.celrep.2013.12.007 10.1016/S0022-3476(99)70101-0 10.1074/jbc.273.14.7828 10.1021/bi201785u 10.1016/0378-1119(92)90135-C 10.1016/j.molcel.2010.07.002 10.1089/ars.2012.4590 10.1016/S0166-2236(02)02245-2 10.1016/j.niox.2014.07.002 10.1073/pnas.0607260103 10.1016/j.niox.2010.09.007 10.1126/science.1108228 10.1016/j.ymeth.2013.04.016 10.1016/S0092-8674(04)00131-X 10.1165/rcmb.2006-0289SM 10.1164/ajrccm.165.7.2105032 10.1371/journal.pone.0014007 10.1073/pnas.0404161101 10.1016/j.ymeth.2013.04.018 10.1126/stke.2001.86.pl1 10.1007/s11064-013-1053-9 10.1038/ncb2114 10.1038/nrm1569 10.1002/ejhf.100 10.2337/diabetes.54.4.959 10.1073/pnas.1220185110 10.1074/jbc.M109.019919 10.1126/scitranslmed.3000328 10.1089/ars.2015.6548 10.4049/jimmunol.1000080 10.1523/JNEUROSCI.4751-13.2014 10.4062/biomolther.2014.101 10.1021/acs.biochem.5b01373 10.1074/mcp.M111.013441 10.1006/bbrc.2001.4935 10.1161/JAHA.115.001974 10.1073/pnas.0908540107 10.1126/science.1158265 10.1038/ncb1268 10.1152/ajpcell.00198.2013 10.1074/jbc.R111.285742 10.1007/978-1-4615-8356-1_5 10.1038/35068596 10.1038/nn.2334 10.1016/j.molmed.2009.06.007 10.1016/j.cca.2008.05.001 10.1073/pnas.0901043106 10.1089/ars.2012.4716 10.1073/pnas.89.1.444 |
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| Title | Pathophysiological Role of S-Nitrosylation and Transnitrosylation Depending on S-Nitrosoglutathione Levels Regulated by S-Nitrosoglutathione Reductase |
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