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Peroxiredoxin

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'''Typical 2-Cys Prx'''<br />
'''Typical 2-Cys Prx'''<br />
* '''Prx 1''' interacts with signaling molecules<ref>PMID:19923889</ref>.
* '''Prx 1''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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* '''Prx 2''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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* '''Prx 2''' is essential for sustaining erythrocyte life span<ref>PMID:18479207</ref>.
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* '''Prx 3''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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* '''Prx 3''' is mitochondria-specific.<ref>PMID:15280382</ref>.
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* '''Prx 4''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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* '''Prx 4''' localizes to the cytoplasm and regulates the activation of NF-κB<ref>PMID:25656995</ref>.
'''Atypical 2-Cys Prx'''<br />
'''Atypical 2-Cys Prx'''<br />
* '''Prx 5''' interacts with signaling molecules<ref>PMID:19923889</ref>.
* '''Prx 5''' interacts with signaling molecules<ref>PMID:19923889</ref>.
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== Relevance ==
== Relevance ==
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Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>.
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Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>. Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>.
== 3D Structures of Peroxiredoxin ==
== 3D Structures of Peroxiredoxin ==

Revision as of 10:35, 21 June 2016

Template:STRUCTURE 1qq2

Contents

Function

Peroxiredoxin (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid byperoxide. The Prxs are divided into typical 2-Cys Prx, atypical 2-Cys Prx and 1-Cys Prx. Prx 5 is expressed in mammalian tissue.

Typical 2-Cys Prx

  • Prx 1 interacts with signaling molecules[1].
  • Prx 2 is essential for sustaining erythrocyte life span[2].
  • Prx 3 is mitochondria-specific.[3].
  • Prx 4 localizes to the cytoplasm and regulates the activation of NF-κB[4].

Atypical 2-Cys Prx

  • Prx 5 interacts with signaling molecules[5].

1-Cys Prx

  • Prx 6 interacts with signaling molecules[6].

Relevance

Prx are over expressed in cancer tissue[7]. Prx 4 mediates osteoclast activation in cancer cells[8].

3D Structures of Peroxiredoxin

Updated on 21-June-2016

References

  1. ↑ Neumann CA, Cao J, Manevich Y. Peroxiredoxin 1 and its role in cell signaling. Cell Cycle. 2009 Dec 15;8(24):4072-8. Epub 2009 Dec 5. PMID:19923889 doi:http://dx.doi.org/10.4161/cc.8.24.10242
  2. ↑ Low FM, Hampton MB, Winterbourn CC. Peroxiredoxin 2 and peroxide metabolism in the erythrocyte. Antioxid Redox Signal. 2008 Sep;10(9):1621-30. doi: 10.1089/ars.2008.2081. PMID:18479207 doi:http://dx.doi.org/10.1089/ars.2008.2081
  3. ↑ Chang TS, Cho CS, Park S, Yu S, Kang SW, Rhee SG. Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria. J Biol Chem. 2004 Oct 1;279(40):41975-84. Epub 2004 Jul 27. PMID:15280382 doi:http://dx.doi.org/10.1074/jbc.M407707200
  4. ↑ Fujii J, Ikeda Y, Kurahashi T, Homma T. Physiological and pathological views of peroxiredoxin 4. Free Radic Biol Med. 2015 Jun;83:373-9. doi: 10.1016/j.freeradbiomed.2015.01.025., Epub 2015 Feb 2. PMID:25656995 doi:http://dx.doi.org/10.1016/j.freeradbiomed.2015.01.025
  5. ↑ Neumann CA, Cao J, Manevich Y. Peroxiredoxin 1 and its role in cell signaling. Cell Cycle. 2009 Dec 15;8(24):4072-8. Epub 2009 Dec 5. PMID:19923889 doi:http://dx.doi.org/10.4161/cc.8.24.10242
  6. ↑ Neumann CA, Cao J, Manevich Y. Peroxiredoxin 1 and its role in cell signaling. Cell Cycle. 2009 Dec 15;8(24):4072-8. Epub 2009 Dec 5. PMID:19923889 doi:http://dx.doi.org/10.4161/cc.8.24.10242
  7. ↑ Noh DY, Ahn SJ, Lee RA, Kim SW, Park IA, Chae HZ. Overexpression of peroxiredoxin in human breast cancer. Anticancer Res. 2001 May-Jun;21(3B):2085-90. PMID:11497302
  8. ↑ Rafiei S, Tiedemann K, Tabaries S, Siegel PM, Komarova SV. Peroxiredoxin 4: a novel secreted mediator of cancer induced osteoclastogenesis. Cancer Lett. 2015 Jun 1;361(2):262-70. doi: 10.1016/j.canlet.2015.03.012. Epub, 2015 Mar 14. PMID:25779674 doi:http://dx.doi.org/10.1016/j.canlet.2015.03.012

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