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'''Redox signaling''' is when ], ] (ROS), and other electronically activated species such as ] and other oxides of nitrogen act as biological messengers. For example, ] likely play a key role in fibrocyte activation<ref>{{cite journal|pmid=16297593}}</ref><ref> Vozenin-Brotons MC, Sivan V, Gault N, Renard C, Geffrotin C, Delanian S, '''Redox signaling''' is when ], ] (ROS), and other electronically activated species such as ] and other oxides of nitrogen act as biological messengers. For example, ] likely play a key role in fibrocyte activation<ref>{{cite pmid|16297593}}</ref><ref>{{cite pmid|11134893}}</ref> and thus scar formation. Arguably, ] and ] 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<ref>{{cite pmid|19735727}}</ref>.
Lefaix JL, Martin M. Antifibrotic action of Cu/Zn SOD is mediated by TGF-beta1
repression and phenotypic reversion of myofibroblasts. Free Radic Biol Med. 2001
Jan 1;30(1):30-42. PubMed PMID: 11134893.</ref> and thus scar formation. Arguably, ] and ] 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<ref>], Signal transduction and reactive species. Free Radic. Biol. Med. 47:1237-1238; 2009.</ref>.


==History== ==History==
Line 16: Line 13:
Dekker, Inc., New York. Dekker, Inc., New York.
Szent-Gyorgyi, A., 1978. The Living State and Cancer. Marcel Szent-Gyorgyi, A., 1978. The Living State and Cancer. Marcel
Dekker, Inc., New York.</ref> ] proposed that modulation of electronic processes in semiconductive macromolecules plays a key role in biological function and in diseases such as cancer. Hush <ref>Hush, N.S. An Overview of the First Half-Century of Molecular Electronics. Ann. N.Y. Acad. Sci. 1006:1–20; 2003.</ref> reviews the history of such ]. Dekker, Inc., New York.</ref> ] proposed that modulation of electronic processes in semiconductive macromolecules plays a key role in biological function and in diseases such as cancer. Hush <ref>{{Cite pmid| 14976006}}</ref> reviews the history of such ].


Similarly, the first modern statement of the "ROS are messengers" component of redox signaling appears to be that of ],<ref>{{cite journal |author=Proctor P |title=Electron-transfer factors in psychosis and dyskinesia |journal=Physiol. Chem. Phys. |volume=4 |issue=4 |pages=349–60 |year=1972 |pmid=4680784 |url=http://www.nitrone.com/72rev.htm}}</ref> 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....". After meeting with significant early opposition, this was finally published in a 1984 review.<ref>{{cite journal |author=Proctor P and Reynolds, ES |title=Free Radicals and Disease in Man, |journal=Physiol. Chem. Phys. |volume=16 |issue=3 |pages=175–95 |year=1984 |pmid=6393156 |url=http://www.drproctor.com/rev/84/84rev.htm}}</ref> The next reference seems to be Bochner and coworkers.<ref>{{cite journal |author=Bochner BR, Lee PC, Wilson SW, Cutler CW, ],|title=AppppA and related adenylylated nucleotides are synthesized as a consequence of oxidation stress |journal=Cell |volume=37 |issue=1 |pages=225–32 |year=1984 |month=May |pmid=6373012 |url=http://linkinghub.elsevier.com/retrieve/pii/0092-8674(84)90318-0 |doi=10.1016/0092-8674(84)90318-0}}</ref> Similarly, the first modern statement of the "ROS are messengers" component of redox signaling appears to be that of ],<ref>{{cite pmid|4680784}}</ref> 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....". After meeting with significant early opposition, this was finally published in a 1984 review.<ref>{{cite pmid|6393156}}</ref> The next reference seems to be Bochner and coworkers.<ref>{{cite pmid|6373012}}</ref>


==Electronic conduction in redox signaling== ==Electronic conduction in redox signaling==
Hush <ref>Hush, N.S. An Overview of the First Half-Century of Molecular Electronics. Ann. N.Y. Acad. Sci. 1006:1–20; 2003.</ref> credits ] and coworkers .<ref>{{cite journal | doi = 10.1126/science.183.4127.853 | url = http://www.organicmetals.com/amorphous.htm | author = McGinness, J.E., Corry, P.M., and Proctor, P. | title = Amorphous semiconductor switching in melanins| journal = Science | volume = 183 | issue = 4127 |pages = 853–855 | year = 1974 | pmid = 4359339}}</ref> with the first experimental confirmation of Szent-Gyorgyi's theories concerning semiconductor mechanisms in cellular signaling. Priel and coworkers <ref>Priel A, Ramos AJ, Tuszynski JA, Cantiello HF. A biopolymer transistor: electrical amplification by microtubules. Biophys J. 2006 Jun 15;90(12):4639-43. Epub 2006 Mar 24. PMID 16565058; {{PMC|1471843}}.</ref> postulate active electronic mechanisms in modulation of cellular processes by microtubules. Bettinger and Bao <ref>Bettinger CJ, Bao Z. Biomaterials-Based Organic Electronic Devices. Polym Int. 2010 May 1;59(5):563-567. PMID 20607127; {{PMC|2895275}}</ref> review recent work on biomaterial-based organic electronic devices. Such may play s role in control of cellular function. Hush <ref>{{cite pmid| 14976006}}</ref> credits ] and coworkers .<ref>{{cite pmid|4359339}}</ref> with the first experimental confirmation of Szent-Gyorgyi's theories concerning semiconductor mechanisms in cellular signaling. Priel and coworkers <ref>{{cite pmid|16565058}}</ref> postulate active electronic mechanisms in modulation of cellular processes by microtubules. Bettinger and Bao <ref>{{cite pmid|20607127}}</ref> review recent work on biomaterial-based organic electronic devices. Such may play s role in control of cellular function.


==Reactive oxygen species as messengers== ==Reactive oxygen species as messengers==
The formation of ROS such as ]<ref>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</ref> underlies much biotic and abiotic stress signaling. For example, as signaling molecules, hydrogen peroxide and other ROS post- translationally modify target proteins by oxidizing ] ], thus forming ] that reversibly alter protein structure and function. Specificity is achieved by localized production, concatenate ] or ], with targeted secondary oxidation occurring via ]s or ]s.<ref>Winterbourn C.C., and Hampton M.B. 2008. Thiol chemistry and specificity in redox signaling. Free Radical Biology and Medicine 45: 549-561</ref> Target proteins containing reduction-oxidation (redox) sensitive thiol groups include i) signal transduction pathway proteins, such as ]s<ref>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.</ref> and ]s,<ref>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</ref> ii) embryogenesis regulating proteins<ref>Ufer C, Wang CC, Borchert A, Heydeck D, Kuhn H. 2010. Redox control in mammalian embryo development. Antioxidants & Redox Signaling 13: 833-875</ref> iii) many ]s, iv) ]s that direct ], and v) proteins involved in ] ], deacetylation or ].<ref>Sundar IK, Caito S, Yao H, and Rahman I. 2010. Oxidative stress, thiol redox signaling methods in epigenetics. Methods Enzymol.474:213-44.</ref><ref>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</ref> The formation of ROS such as ]<ref>{{Cite pmid| 20446770}}</ref> underlies much biotic and abiotic stress signaling. For example, as signaling molecules, hydrogen peroxide and other ROS post- translationally modify target proteins by oxidizing ] ], thus forming ] that reversibly alter protein structure and function. Specificity is achieved by localized production, concatenate ] or ], with targeted secondary oxidation occurring via ]s or ]s.<ref>{{Cite pmid|18544350}}</ref> Target proteins containing reduction-oxidation (redox) sensitive thiol groups include i) signal transduction pathway proteins, such as ]s<ref>{{Cite pmid| 20919935}}</ref> and ]s,<ref>{{cite pmid| 10717008}}</ref> ii) embryogenesis regulating proteins<ref>{{Cite pmid| 20367257}}</ref> iii) many ]s, iv) ]s that direct ], and v) proteins involved in ] ], deacetylation or ].<ref>{{Cite pmid| 20609913}}</ref><ref>{{cite pmid|20446770}}</ref>


Similarly, the tyrosine-specific ] are intracellular activities lacking disulfide bonds, but they might sense intracellular redox potential through the conserved cysteine in their active sites <ref>{{citation |title=Tyrosine specific protein phosphatases at PROSITE |url=http://www.expasy.org/prosite/PDOC00323}}</ref><ref>{{citation |title=Interpro record for Tyrosine specific protein phosphatases |url=http://www.ebi.ac.uk/interpro/DisplayIproEntry?ac=IPR017867}}</ref> Similarly, the tyrosine-specific ] are intracellular activities lacking disulfide bonds, but they might sense intracellular redox potential through the conserved cysteine in their active sites <ref>{{citation |title=Tyrosine specific protein phosphatases at PROSITE |url=http://www.expasy.org/prosite/PDOC00323}}</ref><ref>{{citation |title=Interpro record for Tyrosine specific protein phosphatases |url=http://www.ebi.ac.uk/interpro/DisplayIproEntry?ac=IPR017867}}</ref>
An intracellular oscillation of oxidant levels has been previously experimentally linked to maintenance of the rate of cell proliferation.<ref>{{cite journal |author=Irani K, Xia Y, Zweier JL, ''et al.'' |title=Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts |journal=Science |volume=275 |issue=5306 |pages=1649–52 |year=1997 |month=March |pmid=9054359 |url=http://www.sciencemag.org/cgi/pmidlookup?view=long&pmid=9054359 |doi=10.1126/science.275.5306.1649}}</ref> An intracellular oscillation of oxidant levels has been previously experimentally linked to maintenance of the rate of cell proliferation.<ref>{{cite pmid|9054359}}</ref>


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.<ref>{{cite journal |author=Doulias PT, Christoforidis S, Brunk UT, Galaris D |title=Endosomal and lysosomal effects of desferrioxamine: protection of ] cells from hydrogen peroxide-induced DNA damage and induction of cell-cycle arrest |journal=Free Radic. Biol. Med. |volume=35 |issue=7 |pages=719–28 |year=2003 |month=October |pmid=14583336 |url=http://linkinghub.elsevier.com/retrieve/pii/S0891584903003964 |doi=10.1016/S0891-5849(03)00396-4}}.</ref> 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.<ref>{{cite pmid|14583336}}</ref>


] (Trx) signaling Is also important in Cancer , as are other aspects of redox signaling <ref>Gupta SC, Hevia D, Patchva S, Park B, Koh W, Aggarwal BB., Upsides and Downsides of Reactive Oxygen Species for Cancer: The Roles of Reactive Oxygen Species in Tumorigenesis, Prevention, and Therapy. Antioxid Redox Signal. 2012 Jan 16. http://www.ncbi.nlm.nih.gov/pubmed/22117137</ref>. <ref>Díaz B, Courtneidge SA. Redox signaling at invasive microdomains in cancer cells. Free Radic Biol Med. 2012 Jan 15;52(2):247-56. http://www.ncbi.nlm.nih.gov/pubmed/22033009</ref>. ] (Trx) signaling Is also important in Cancer , as are other aspects of redox signaling <ref>{{cite pmid| 22117137}}</ref>. <ref>{{cite pmid| 22033009}}</ref>.


==References== ==References==
{{reflist}} {{Reflist}}


==Further reading== ==Further reading==

Revision as of 18:13, 23 May 2012

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 fibrocyte activation and thus scar formation. Arguably, hydrogen sulfide 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.

History

In a series of papers beginning in 1941, 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 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, 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....". After meeting with significant early opposition, this was finally published in a 1984 review. The next reference seems to be Bochner and coworkers.

Electronic conduction in redox signaling

Hush credits Mcginness and coworkers . with the first experimental confirmation of Szent-Gyorgyi's theories concerning semiconductor mechanisms in cellular signaling. Priel and coworkers postulate active electronic mechanisms in modulation of cellular processes by microtubules. Bettinger and Bao 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 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 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. Target proteins containing reduction-oxidation (redox) sensitive thiol groups include i) signal transduction pathway proteins, such as phosphatases and mitogen-activated protein kinases, ii) embryogenesis regulating proteins iii) many transcription factors, iv) RNA-binding proteins that direct DNA methylation, and v) proteins involved in histone acetylation, deacetylation or methylation.

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 An intracellular oscillation of oxidant levels has been previously experimentally linked to maintenance of the rate of cell proliferation.

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.

Thioredoxin (Trx) signaling Is also important in Cancer , as are other aspects of redox signaling . .

References

  1. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 16297593, please use {{cite journal}} with |pmid=16297593 instead.
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  4. 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.
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  20. Tyrosine specific protein phosphatases at PROSITE
  21. Interpro record for Tyrosine specific protein phosphatases
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Further reading

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