Redox signaling - Wikipedia, the free encyclopedia

http://en.wikipedia.org/wiki/Redox_signaling

Redox signaling
From Wikipedia, the free encyclopedia

Redox signaling is when free radicals, reactive oxygen species (ROS), and other electronically activated species such as nitric oxide and other oxides of nitrogen act as biological messengers. For example, reactive oxygen species likely play a key role in brocyte activation[1][2] and thus scar formation. Arguably, hydrogen sulde and carbon monoxide are also redox signaling molecules. Similarly, modulation of charge-transfer processes and electronic conduction in macromolecules is also redox signaling. For a review, see Forman[3].

Contents
1 History 2 Electronic conduction in redox signaling 3 Reactive oxygen species as messengers 4 References 5 Further reading 6 External links

History
In a series of papers beginning in 1941,[4] Szent-Gyorgyi proposed that modulation of electronic processes in semiconductive macromolecules plays a key role in biological function and in diseases such as cancer. Hush [5] reviews the history of such molecular electronics. Similarly, the rst modern statement of the ROS are messengers component of redox signaling appears to be that of Proctor,[6] who at a congress of free radical investigators in 1979 generalized the concept to suggest that ....active oxygen metabolites act as specic intermediary transmitter substances for a variety of biological processes including inammation, brosis, and possibly, neurotransmission.. and One explanation for this data is that various active oxygen species ( or such products as hydroperoxides ) may act as specic transmitter substances..... After meeting with signicant early opposition, this was nally published in a 1984 review.[7] The next reference seems to be Bochner and coworkers.[8]

Electronic conduction in redox signaling

Hush [9] credits Mcginness and coworkers .[10] with the rst experimental conrmation of SzentGyorgyis theories concerning semiconductor mechanisms in cellular signaling. Priel and coworkers [11] postulate active electronic mechanisms in modulation of cellular processes by microtubules. Bettinger

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and Bao [12] review recent work on biomaterial-based organic electronic devices. Such may play s role in control of cellular function.

Reactive oxygen species as messengers

The formation of ROS such as hydrogen peroxide[13] underlies much biotic and abiotic stress signaling. For example, as signaling molecules, hydrogen peroxide and other ROS post- translationally modify target proteins by oxidizing thiol groups, thus forming disulde bonds that reversibly alter protein structure and function. Specicity is achieved by localized production, concatenate hormone or calcium signaling, with targeted secondary oxidation occurring via glutaredoxins or thioredoxins.[14] Target proteins containing reduction-oxidation (redox) sensitive thiol groups include i) signal transduction pathway proteins, such as phosphatases[15] and mitogen-activated protein kinases,[16] ii) embryogenesis regulating proteins[17] iii) many transcription factors, iv) RNA-binding proteins that direct DNA methylation, and v) proteins involved in histone acetylation, deacetylation or methylation.[18][19] Similarly, the tyrosine-specic Protein Tyrosine Phosphatases are intracellular activities lacking disulde bonds, but they might sense intracellular redox potential through the conserved cysteine in their active sites [20][21] An intracellular oscillation of oxidant levels has been previously experimentally linked to maintenance of the rate of cell proliferation.[22] As an example, when chelating redox-active iron present in the endosomalysosomal compartment of cultured epithelial cell line HeLa with the iron chelator desferrioxamine, cell proliferation is inhibited.[23] Thioredoxin (Trx) signaling Is also important in Cancer [24], as are other aspects of redox signaling [25]. [26] .

References
1. ^ Emerit, J.; Samuel, D.; Pavio, N. (2006). CuZn super oxide dismutase as a potential antibrotic drug for hepatitis C related brosis. Biomedicine & Pharmacotherapy 60 (1): 14. doi:10.1016/j.biopha.2005.09.002 (http://dx.doi.org/10.1016%2Fj.biopha.2005.09.002) . PMID 16297593 (//www.ncbi.nlm.nih.gov/pubmed/16297593) . 2. ^ Vozenin-Brotons, M. C.; Sivan, V.; Gault, N.; Renard, C.; Geffrotin, C.; Delanian, S.; Lefaix, J. L.; Martin, M. (2001). Antibrotic action of Cu/Zn SOD is mediated by TGF-beta1 repression and phenotypic reversion of myobroblasts. Free radical biology & medicine 30 (1): 3042. doi:10.1016/S0891-5849(00)00431-7 (http://dx.doi.org/10.1016%2FS0891-5849%2800%2900431-7) . PMID 11134893 (//www.ncbi.nlm.nih.gov /pubmed/11134893) . 3. ^ Forman, H. J. (2009). Signal transduction and reactive species. Free Radical Biology and Medicine 47 (9): 12371238. doi:10.1016/j.freeradbiomed.2009.09.002 (http://dx.doi.org /10.1016%2Fj.freeradbiomed.2009.09.002) . PMID 19735727 (//www.ncbi.nlm.nih.gov/pubmed/19735727) . 4. ^ Szent-Gyorgyi, A., 1941b. The study of energy-levels in biochemistry. Nature 148 (3745), 157159. SzentGyorgyi, A., 1957. Bioenergetics. Academic Press, New York. Szent-Gyorgyi, A., 1960. Introduction to a Submolecular Biology. Academic Press, New York. Szent-Gyorgyi, A., 1968. Bioelectronics. Academic Press, New York. Szent-Gyorgyi, A., 1976. Electronic Biology and Cancer. Marcel Dekker, Inc., New York. Szent-Gyorgyi, A., 1978. The Living State and Cancer. Marcel Dekker, Inc., New York.

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5. ^ Hush, N. S. (2003). An overview of the rst half-century of molecular electronics. Annals of the New York Academy of Sciences 1006: 120. doi:10.1196/annals.1292.016 (http://dx.doi.org /10.1196%2Fannals.1292.016) . PMID 14976006 (//www.ncbi.nlm.nih.gov/pubmed/14976006) . 6. ^ Proctor, P. (1972). Electron-transfer factors in psychosis and dyskinesia. Physiological chemistry and physics 4 (4): 349360. PMID 4680784 (//www.ncbi.nlm.nih.gov/pubmed/4680784) . 7. ^ Proctor, P. H.; Reynolds, E. S. (1984). Free radicals and disease in man. Physiological chemistry and physics and medical NMR 16 (3): 175195. PMID 6393156 (//www.ncbi.nlm.nih.gov/pubmed/6393156) . 8. ^ Bochner, B. R.; Lee, P. C.; Wilson, S. W.; Cutler, C. W.; Ames, B. N. (1984). AppppA and related adenylylated nucleotides are synthesized as a consequence of oxidation stress. Cell 37 (1): 225232. doi:10.1016/0092-8674(84)90318-0 (http://dx.doi.org/10.1016%2F0092-8674%2884%2990318-0) . PMID 6373012 (//www.ncbi.nlm.nih.gov/pubmed/6373012) . 9. ^ Hush, N. S. (2003). An overview of the rst half-century of molecular electronics. Annals of the New York Academy of Sciences 1006: 120. doi:10.1196/annals.1292.016 (http://dx.doi.org /10.1196%2Fannals.1292.016) . PMID 14976006 (//www.ncbi.nlm.nih.gov/pubmed/14976006) . 10. ^ McGinness, J.; Corry, P.; Proctor, P. (1974). Amorphous semiconductor switching in melanins. Science 183 (4127): 853855. doi:10.1126/science.183.4127.853 (http://dx.doi.org /10.1126%2Fscience.183.4127.853) . PMID 4359339 (//www.ncbi.nlm.nih.gov/pubmed/4359339) . 11. ^ Priel, A.; Ramos, A. J.; Tuszynski, J. A.; Cantiello, H. F. (2006). A Biopolymer Transistor: Electrical Amplication by Microtubules (//www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez& artid=1471843) . Biophysical Journal 90 (12): 46394643. doi:10.1529/biophysj.105.078915 (http://dx.doi.org/10.1529%2Fbiophysj.105.078915) . PMC 1471843 (//www.ncbi.nlm.nih.gov/pmc/articles /PMC1471843/?tool=pmcentrez) . PMID 16565058 (//www.ncbi.nlm.nih.gov/pubmed/16565058) . //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1471843. 12. ^ Bettinger, C. J.; Bao, Z. (2010). Biomaterials-based organic electronic devices (//www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2895275) . Polymer International 59 (5): 563567. doi:10.1002/pi.2827 (http://dx.doi.org/10.1002%2Fpi.2827) . PMC 2895275 (//www.ncbi.nlm.nih.gov/pmc/articles/PMC2895275/?tool=pmcentrez) . PMID 20607127 (//www.ncbi.nlm.nih.gov/pubmed/20607127) . //www.pubmedcentral.nih.gov /articlerender.fcgi?tool=pmcentrez&artid=2895275. 13. ^ Shlomai, J. (2010). Redox Control of ProteinDNA Interactions: From Molecular Mechanisms to Signicance in Signal Transduction, Gene Expression, and DNA Replication. Antioxidants & Redox Signaling 13 (9): 14291476. doi:10.1089/ars.2009.3029 (http://dx.doi.org/10.1089%2Fars.2009.3029) . PMID 20446770 (//www.ncbi.nlm.nih.gov/pubmed/20446770) . 14. ^ Winterbourn, C. C.; Hampton, M. B. (2008). Thiol chemistry and specicity in redox signaling. Free Radical Biology and Medicine 45 (5): 549561. doi:10.1016/j.freeradbiomed.2008.05.004 (http://dx.doi.org /10.1016%2Fj.freeradbiomed.2008.05.004) . PMID 18544350 (//www.ncbi.nlm.nih.gov/pubmed/18544350) . 15. ^ Tanner, J. J.; Parsons, Z. D.; Cummings, A. H.; Zhou, H.; Gates, K. S. (2011). Redox Regulation of Protein Tyrosine Phosphatases: Structural and Chemical Aspects. Antioxidants & Redox Signaling 15 (1): 7797. doi:10.1089/ars.2010.3611 (http://dx.doi.org/10.1089%2Fars.2010.3611) . PMID 20919935 (//www.ncbi.nlm.nih.gov/pubmed/20919935) . 16. ^ Kovtun, Y.; Chiu, W. L.; Tena, G.; Sheen, J. (2000). Functional analysis of oxidative stress-activated mitogen-activated protein kinase cascade in plants (//www.pubmedcentral.nih.gov /articlerender.fcgi?tool=pmcentrez&artid=16034) . Proceedings of the National Academy of Sciences of the United States of America 97 (6): 29402945. doi:10.1073/pnas.97.6.2940 (http://dx.doi.org /10.1073%2Fpnas.97.6.2940) . PMC 16034 (//www.ncbi.nlm.nih.gov/pmc/articles/PMC16034 /?tool=pmcentrez) . PMID 10717008 (//www.ncbi.nlm.nih.gov/pubmed/10717008) . //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16034. 17. ^ Ufer, C.; Wang, C. C.; Borchert, A.; Heydeck, D.; Kuhn, H. (2010). Redox Control in Mammalian Embryo Development. Antioxidants & Redox Signaling 13 (6): 833875. doi:10.1089/ars.2009.3044 (http://dx.doi.org/10.1089%2Fars.2009.3044) . PMID 20367257 (//www.ncbi.nlm.nih.gov/pubmed /20367257) . 18. ^ Sundar, I. K.; Caito, S.; Yao, H.; Rahman, I. (2010). Oxidative Stress, Thiol Redox Signaling Methods in Epigenetics. Thiol Redox Transitions in Cell Signaling, Part B: Cellular Localization and Signaling. Methods in enzymology. Methods in Enzymology 474: 213244. doi:10.1016/S0076-6879(10)74013-1 (http://dx.doi.org/10.1016%2FS0076-6879%2810%2974013-1) . ISBN 9780123810038. PMID 20609913

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(//www.ncbi.nlm.nih.gov/pubmed/20609913) . 19. ^ Shlomai, J. (2010). Redox Control of ProteinDNA Interactions: From Molecular Mechanisms to Signicance in Signal Transduction, Gene Expression, and DNA Replication. Antioxidants & Redox Signaling 13 (9): 14291476. doi:10.1089/ars.2009.3029 (http://dx.doi.org/10.1089%2Fars.2009.3029) . PMID 20446770 (//www.ncbi.nlm.nih.gov/pubmed/20446770) . 20. ^ Tyrosine specic protein phosphatases at PROSITE (http://www.expasy.org/prosite/PDOC00323) . http://www.expasy.org/prosite/PDOC00323 21. ^ Interpro record for Tyrosine specic protein phosphatases (http://www.ebi.ac.uk/interpr DisplayIproEntry?ac=IPR017867) . http://www.ebi.ac.uk/interprDisplayIproEntry?ac=IPR017867 22. ^ Irani, K.; Xia, Y.; Zweier, J. L.; Sollott, S. J.; Der, C. J.; Fearon, E. R.; Sundaresan, M.; Finkel, T. et al (1997). Mitogenic signaling mediated by oxidants in Ras-transformed broblasts. Science 275 (5306): 16491652. doi:10.1126/science.275.5306.1649 (http://dx.doi.org/10.1126%2Fscience.275.5306.1649) . PMID 9054359 (//www.ncbi.nlm.nih.gov/pubmed/9054359) . 23. ^ Doulias, P. T.; Christoforidis, S.; Brunk, U. T.; Galaris, D. (2003). Endosomal and lysosomal effects of desferrioxamine: Protection of HeLa cells from hydrogen peroxide-induced DNA damage and induction of cell-cycle arrest. Free radical biology & medicine 35 (7): 719728. doi:10.1016/S0891-5849(03)00396-4 (http://dx.doi.org/10.1016%2FS0891-5849%2803%2900396-4) . PMID 14583336 (//www.ncbi.nlm.nih.gov /pubmed/14583336) . 24. ^ http://www.mdanderson.org/education-and-research/departments-programs-and-labs/labs/powis-laboratory /current-research/index.html 25. ^ Gupta, S. C.; Hevia, D.; Patchva, S.; Park, B.; Koh, W.; Aggarwal, B. B. (2012). Upsides and Downsides of Reactive Oxygen Species for Cancer: The Roles of Reactive Oxygen Species in Tumorigenesis, Prevention, and Therapy (//www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3324815) . Antioxidants & Redox Signaling 16 (11): 12951322. doi:10.1089/ars.2011.4414 (http://dx.doi.org /10.1089%2Fars.2011.4414) . PMC 3324815 (//www.ncbi.nlm.nih.gov/pmc/articles/PMC3324815 /?tool=pmcentrez) . PMID 22117137 (//www.ncbi.nlm.nih.gov/pubmed/22117137) . //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3324815. 26. ^ Daz, B. A.; Courtneidge, S. A. (2012). Redox signaling at invasive microdomains in cancer cells (//www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3272498) . Free Radical Biology and Medicine 52 (2): 247256. doi:10.1016/j.freeradbiomed.2011.09.016 (http://dx.doi.org /10.1016%2Fj.freeradbiomed.2011.09.016) . PMC 3272498 (//www.ncbi.nlm.nih.gov/pmc/articles /PMC3272498/?tool=pmcentrez) . PMID 22033009 (//www.ncbi.nlm.nih.gov/pubmed/22033009) . //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3272498.

Further reading
Proctor, Peter H. (1989). Free Radicals and Human Disease (http://www.doctorproctor.com /crcpap2.htm) . CRC Handbook of Free Radicals and Antioxidants. 1. pp. 209221. http://www.doctorproctor.com/crcpap2.htm.

External links
http://www.redoxsignaling.com Retrieved from http://en.wikipedia.org/w/index.php?title=Redox_signaling&oldid=494026869 Categories: Signal transduction Free radicals Metabolism This page was last modied on 23 May 2012 at 18:22. Text is available under the Creative Commons Attribution-ShareAlike License; additional terms

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