Misplaced Pages

Redox signaling: Difference between revisions

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
Browse history interactively← Previous editNext edit →Content deleted Content addedVisualWikitext
Revision as of 08:48, 26 October 2012 edit98.202.20.79 (talk) Removed phrase, "and other oxides of nitrogen" for brevity and redundancy← Previous edit Revision as of 08:49, 26 October 2012 edit undo98.202.20.79 (talk) Corrected punctuationNext edit →
Line 1: Line 1:
'''Redox signaling''' is simply biochemical communication within the cells and body by ], ] (ROS), and other electrochemically active species such as ] acting as biological messengers. Arguably, ]<ref>Jerzy Bełtowski and Anna Jamroz-Wiśniewska, Modulation of H2S Metabolism by Statins: A New Aspect of Cardiovascular Pharmacology . Antioxidants & Redox Signaling. July 1, 2012, 17(1): 81-94. doi:10.1089/ars.2011.4358.</ref> 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>. There appear to be a large number of redox signaling molecules, and they are involved in many different processes. Some redox signaling molecules are as simple as ] while others are much more complex chemicals and organic compounds. Redox signaling molecules are produced in every cell of living things. During the biological processes of life, including such essential processes as breathing oxygen, oxidative free radicals and other harmful compounds are generated and redox signaling is activated. Essentially Redox signaling is one of the means by which the body controls certain potentially harmful chemicals, compounds, processes and injuries. For example, ] likely play a key role in fibrocyte activation<ref>{{cite pmid|16297593}}</ref><ref>{{cite pmid|11134893}}</ref> and thus scar formation. These molecules act as messengers or triggers and are produced on demand, within the cells, as the cells need them. Redox signaling molecules are universally present in living tissue in response to cellular stresses and injury. Since redox signaling is produced in the cells on an as needed basis, there currently is no evidence of any beneficial effect from attempts to supply the body with external sources of these compounds. '''Redox signaling''' is simply biochemical communication within the cells and body by ], ] (ROS), and other electrochemically active species such as ], acting as biological messengers. Arguably, ]<ref>Jerzy Bełtowski and Anna Jamroz-Wiśniewska, Modulation of H2S Metabolism by Statins: A New Aspect of Cardiovascular Pharmacology . Antioxidants & Redox Signaling. July 1, 2012, 17(1): 81-94. doi:10.1089/ars.2011.4358.</ref> 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>. There appear to be a large number of redox signaling molecules, and they are involved in many different processes. Some redox signaling molecules are as simple as ] while others are much more complex chemicals and organic compounds. Redox signaling molecules are produced in every cell of living things. During the biological processes of life, including such essential processes as breathing oxygen, oxidative free radicals and other harmful compounds are generated and redox signaling is activated. Essentially Redox signaling is one of the means by which the body controls certain potentially harmful chemicals, compounds, processes and injuries. For example, ] likely play a key role in fibrocyte activation<ref>{{cite pmid|16297593}}</ref><ref>{{cite pmid|11134893}}</ref> and thus scar formation. These molecules act as messengers or triggers and are produced on demand, within the cells, as the cells need them. Redox signaling molecules are universally present in living tissue in response to cellular stresses and injury. Since redox signaling is produced in the cells on an as needed basis, there currently is no evidence of any beneficial effect from attempts to supply the body with external sources of these compounds.


==History== ==History==

Revision as of 08:49, 26 October 2012

Redox signaling is simply biochemical communication within the cells and body by free radicals, reactive oxygen species (ROS), and other electrochemically active species such as nitric oxide, acting as biological messengers. 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.. There appear to be a large number of redox signaling molecules, and they are involved in many different processes. Some redox signaling molecules are as simple as hydrogen peroxide while others are much more complex chemicals and organic compounds. Redox signaling molecules are produced in every cell of living things. During the biological processes of life, including such essential processes as breathing oxygen, oxidative free radicals and other harmful compounds are generated and redox signaling is activated. Essentially Redox signaling is one of the means by which the body controls certain potentially harmful chemicals, compounds, processes and injuries. For example, reactive oxygen species likely play a key role in fibrocyte activation and thus scar formation. These molecules act as messengers or triggers and are produced on demand, within the cells, as the cells need them. Redox signaling molecules are universally present in living tissue in response to cellular stresses and injury. Since redox signaling is produced in the cells on an as needed basis, there currently is no evidence of any beneficial effect from attempts to supply the body with external sources of these compounds.

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,. At a 1979 congress of free radical investigators he further generalized this 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 global concept was published in a 1984 review. The next reference seems to be Bochner and coworkers., reporting increased synthesis of "alarmome" adenylylated nucleotides as a specific response to oxidative stress in bacteria.

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 electrochemical mechanisms in modulation of cellular processes by microtubules. Bettinger and Bao review recent work on biomaterial-based organic electronic devices. Such may play a 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 experimentally linked to maintenance of the rate of cell proliferation.

As an example, when chelating redox-active iron is 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. Jerzy Bełtowski and Anna Jamroz-Wiśniewska, Modulation of H2S Metabolism by Statins: A New Aspect of Cardiovascular Pharmacology . Antioxidants & Redox Signaling. July 1, 2012, 17(1): 81-94. doi:10.1089/ars.2011.4358.
  2. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 19735727, please use {{cite journal}} with |pmid=19735727 instead.
  3. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 16297593, please use {{cite journal}} with |pmid=16297593 instead.
  4. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 11134893, please use {{cite journal}} with |pmid=11134893 instead.
  5. 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.
  6. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 14976006, please use {{cite journal}} with |pmid= 14976006 instead.
  7. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 4680784, please use {{cite journal}} with |pmid=4680784 instead.
  8. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 6393156, please use {{cite journal}} with |pmid=6393156 instead.
  9. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 6373012, please use {{cite journal}} with |pmid=6373012 instead.
  10. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 14976006, please use {{cite journal}} with |pmid= 14976006 instead.
  11. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 4359339, please use {{cite journal}} with |pmid=4359339 instead.
  12. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 16565058, please use {{cite journal}} with |pmid=16565058 instead.
  13. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 20607127, please use {{cite journal}} with |pmid=20607127 instead.
  14. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 20446770, please use {{cite journal}} with |pmid= 20446770 instead.
  15. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 18544350, please use {{cite journal}} with |pmid=18544350 instead.
  16. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 20919935, please use {{cite journal}} with |pmid= 20919935 instead.
  17. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 10717008, please use {{cite journal}} with |pmid= 10717008 instead.
  18. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 20367257, please use {{cite journal}} with |pmid= 20367257 instead.
  19. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 20609913, please use {{cite journal}} with |pmid= 20609913 instead.
  20. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 20446770, please use {{cite journal}} with |pmid=20446770 instead.
  21. "Tyrosine specific protein phosphatases at PROSITE"Template:Inconsistent citations{{cite web}}: CS1 maint: postscript (link)
  22. "Interpro record for Tyrosine specific protein phosphatases"Template:Inconsistent citations{{cite web}}: CS1 maint: postscript (link)
  23. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 9054359, please use {{cite journal}} with |pmid=9054359 instead.
  24. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 14583336, please use {{cite journal}} with |pmid=14583336 instead.
  25. http://www.mdanderson.org/education-and-research/departments-programs-and-labs/labs/powis-laboratory/current-research/index.html
  26. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 22117137, please use {{cite journal}} with |pmid= 22117137 instead.
  27. Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 22033009, please use {{cite journal}} with |pmid= 22033009 instead.

Further reading

External links

Categories: