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'''Redox signaling''' is when [[free radicals]], [[reactive oxygen species]] (ROS), and other electronically activated species such as [[nitric oxide]] act as messengers in biological systems. Many researchers consider [[hydrogen sulfide]] and [[carbon monoxide]] to also be redox signaling molecules. Modulation of charge-transfer processes and electronic conduction in macromolecules is also generally included in redox signaling <ref>Forman, H.J. Signal transduction and reactive species. Free Radic. Biol. Med. 47:1237-1238; 2009.</ref>.
'''Redox signaling''' is when [[free radicals]], [[reactive oxygen species]] (ROS), and other electronically activated species such as [[nitric oxide]] act as biological messengers. Argubly, [[hydrogen sulfide]] and [[carbon monoxide]] are also redox signaling molecules. Modulation of charge-transfer processes and electronic conduction in macromolecules is also generally included in redox signaling <ref>Forman, H.J. Signal transduction and reactive species. Free Radic. Biol. Med. 47:1237-1238; 2009.</ref>.


=== History ===
=== History ===

Revision as of 21:59, 24 October 2011

Redox signaling is when free radicals, reactive oxygen species (ROS), and other electronically activated species such as nitric oxide act as biological messengers. Argubly, hydrogen sulfide and carbon monoxide are also redox signaling molecules. Modulation of charge-transfer processes and electronic conduction in macromolecules is also generally included in redox signaling [1].

History

The concept of electronically activated species as messengers in both normal metabolism and in pathogenesis goes back to the 19th century. For example, we now know that reactive oxygen species likely play a key role in fibrocyte activation [2] and thus scar formation.

In a series of papers beginning in 1941 [3], Szent-Gyorgyi raised the possibility that modulation of electronic processes in semiconductive macromolecules plays a key role in biological function and in diseases such as cancer. Hush [4] reviews the history of such molecular electronics.

Similarly, the first modern statement of the "ROS are messengers" component of redox signaling appears to be that of Proctor,[5] who at a congress of free radical investigators in 1979 generalized the concept to suggest that " ....active oxygen metabolites act as specific intermediary transmitter substances for a variety of biological processes including inflammation, fibrosis, and possibly, neurotransmission.." and " One explanation for this data is that various active oxygen species ( or such products as hydroperoxides ) may act as specific transmitter substances....". This was formally published in a review in 1984.[6] The next reference seems to be Bochner and coworkers.[7]

Mechanisms

At the hub of much biotic and abiotic stress signaling is the formation of ROS such as hydrogen peroxide[8]. For example, as signaling molecules, hydrogen peroxide and other ROS post- translationally modify target proteins by oxidizing thiol groups, thus forming disulfide bonds that reversibly alter protein structure and function. Specificity is achieved by localized production, concatenate hormone or calcium signaling, with targeted secondary oxidation occurring via glutaredoxins or thioredoxins[9]. Target proteins containing reduction-oxidation (redox) sensitive thiol groups include i) signal transduction pathway proteins, such as phosphatases[10] and mitogen-activated protein kinases[11], ii) embryogenesis regulating proteins[12] iii) many transcription factors, iv) RNA-binding proteins that direct DNA methylation, and v) proteins involved in histone acetylation, deacetylation or methylation[13][14].

Similarly, the tyrosine-specific Protein Tyrosine Phosphatases are intracellular activities lacking disulfide bonds, but they might sense intracellular redox potential through the conserved cysteine in their active sites [15][16] An intracellular oscillation of oxidant levels has been previously experimentally linked to maintenance of the rate of cell proliferation.[17]

As an example, when chelating redox-active iron present in the endosomal/lysosomal compartment of cultured epithelial cell line HeLa with the iron chelator desferrioxamine, cell proliferation is inhibited.[18]

References

  1. ^ Forman, H.J. Signal transduction and reactive species. Free Radic. Biol. Med. 47:1237-1238; 2009.
  2. ^ . PMID 16297593. {{cite journal}}: Cite journal requires |journal= (help); Missing or empty |title= (help)
  3. ^ Szent-Gyorgyi, A., 1941b. The study of energy-levels in biochemistry. Nature 148 (3745), 157–159. Szent-Gyorgyi, 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.
  4. ^ Hush, N.S. An Overview of the First Half-Century of Molecular Electronics. Ann. N.Y. Acad. Sci. 1006:1–20; 2003.
  5. ^ Proctor P (1972). "Electron-transfer factors in psychosis and dyskinesia". Physiol. Chem. Phys. 4 (4): 349–60. PMID 4680784.
  6. ^ http://www.drproctor.com/rev/84/84rev.htm
  7. ^ Bochner BR, Lee PC, Wilson SW, Cutler CW, Ames BN (1984). "AppppA and related adenylylated nucleotides are synthesized as a consequence of oxidation stress". Cell. 37 (1): 225–32. doi:10.1016/0092-8674(84)90318-0. PMID 6373012. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  8. ^ Shlomai 2010. Redox Control of Protein-DNA Ineractions: From Molecular Mechanisms to Significance in Signal Transduction, Gene Expresssion, and DNA Replication. Antioxidants and Redox Signaling 13:1429-1476
  9. ^ Winterbourn C.C., and Hampton M.B. 2008. Thiol chemistry and specificity in redox signaling. Free Radical Biology and Medicine 45: 549-561
  10. ^ 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 15:77-97.
  11. ^ Kovtun Y., Chiu W.L., Tena G., and Sheen J. 2000. Functional analysis of oxidative stress-activated mitogen-activated protein kinase cascade in plants. PNAS 97:2940-2945
  12. ^ Ufer C, Wang CC, Borchert A, Heydeck D, Kuhn H. 2010. Redox control in mammalian embryo development. Antioxidants & Redox Signaling 13: 833-875
  13. ^ Sundar IK, Caito S, Yao H, and Rahman I. 2010. Oxidative stress, thiol redox signaling methods in epigenetics. Methods Enzymol.474:213-44.
  14. ^ Shlomai 2010. Redox Control of Protein-DNA Ineractions: From Molecular Mechanisms to Significance in Signal Transduction, Gene Expresssion, and DNA Replication. Antioxidants and Redox Signaling 13:1429-1476
  15. ^ Tyrosine specific protein phosphatases at PROSITE
  16. ^ Interpro record for Tyrosine specific protein phosphatases
  17. ^ Irani K, Xia Y, Zweier JL; et al. (1997). "Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts". Science. 275 (5306): 1649–52. doi:10.1126/science.275.5306.1649. PMID 9054359. {{cite journal}}: Explicit use of et al. in: |author= (help); Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  18. ^ Doulias PT, Christoforidis S, Brunk UT, 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 Radic. Biol. Med. 35 (7): 719–28. doi:10.1016/S0891-5849(03)00396-4. PMID 14583336. {{cite journal}}: URL–wikilink conflict (help); Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link).

Further reading

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