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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2016.1
- 수록면
- 65 - 71 (7page)
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A challenge in the redox field is the elucidation of the molecular mechanisms, by which H2O2 mediates signal transduction in cells. This is relevant since redox pathways are disturbed in some pathologies. The transcription factor OxyR is the H2O2 sensor in bacteria, whereas Cys-based peroxidases are involved in the perception of this oxidant in eukaryotic cells. Three possible mechanisms may be involved in H2O2 signaling that are not mutually exclusive. In the simplest pathway, H2O2 signals through direct oxidation of the signaling protein, such as a phosphatase or a transcription factor. Although signaling proteins are frequently observed in the oxidized state in biological systems, in most cases their direct oxidation by H2O2 is too slow (101 M-1 s-1 range) to outcompete Cys-based peroxidases and glutathione. In some particular cellular compartments (such as vicinity of NADPH oxidases), it is possible that a signaling protein faces extremely high H2O2 concentrations, making the direct oxidation feasible. Alternatively, high H2O2 levels can hyperoxidize peroxiredoxins leading to local building up of H2O2 that then could oxidize a signaling protein (floodgate hypothesis). In a second model, H2O2 oxidizes Cys-based peroxidases that then through thiol-disulfide reshuffling would transmit the oxidized equivalents to the signaling protein. The third model of signaling is centered on the reducing substrate of Cys-based peroxidases that in most cases is thioredoxin. Is this model, peroxiredoxins would signal by modulating the thioredoxin redox status. More kinetic data is required to allow the identification of the complex network of thiol switches.
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참고문헌 (81)
참고문헌 신청
Abbasi, A. / 2014 / Circulating peroxiredoxin 4 and type 2 diabetes risk : the Prevention of Renal and Vascular Endstage Disease(PREVEND)study / Diabetologia 57:1842~1849
Ahsan, M. K. / 2009 / Redox regulation of cell survival by the thioredoxin superfamily : an implication of redox gene therapy in the heart Antioxid / Redox Signal 11:2741~2758
Aslund, F. / 1999 / Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status / Proc. Natl. Acad. Sci. USA 96:6161~6165
Berndt, C. / 2007 / Thiol-based mechanisms of the thioredoxin and glutaredoxin systems : implications for diseases in the cardiovascular system / Am. J. Physiol. Heart Circ. Physiol 292:1227~1236
Biteau, B. / 2003 / ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin / Nature 425:980~984
Ahsan, M. K. / 2009 / Redox regulation of cell survival by the thioredoxin superfamily : an implication of redox gene therapy in the heart Antioxid / Redox Signal 11:2741~2758
Aslund, F. / 1999 / Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status / Proc. Natl. Acad. Sci. USA 96:6161~6165
Berndt, C. / 2007 / Thiol-based mechanisms of the thioredoxin and glutaredoxin systems : implications for diseases in the cardiovascular system / Am. J. Physiol. Heart Circ. Physiol 292:1227~1236
Biteau, B. / 2003 / ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin / Nature 425:980~984
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