User:Tmetz22/PRDX6

Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene. It is a member of the peroxiredoxin family of antioxidant enzymes. PRDX6 is classified as a 1-Cys peroxiredoxin, as it contains one highly conserved cysteine residue ^[18].  It is present in many mammals, invertebrates, and bacteria, often as part of the immune system ^[17].

Function

The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.

Model organisms

Model organisms have been used in the study of PRDX6 function. A conditional knockout mouse line, called Prdx6^{tm1a(EUCOMM)Wtsi} was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty five tests were carried out on mutant mice but no significant abnormalities were observed.

Immune Function

Peroxiredoxin proteins are part of the innate immune system in aquatic invertebrates ^[17]. The innate immune system is responsible for recognizing pathogens and synthesizing molecules by which to eliminate them ^[17]. When an infection occurs, the synthesis of peroxeridoxins greatly increases, especially in response to bacterial, viral, and fungal pathogens ^[17].

References

1. GRCh38: Ensembl release 89: ENSG00000117592 - Ensembl, May 2017
2. ^ Jump up to:^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000026701 - Ensembl, May 2017
3. ^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^Phelan SA (Mar 2001). "AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant". Antioxid Redox Signal. 1 (4): 571–84. doi:10.1089/ars.1999.1.4-571. PMID 11233154.
6. ^ Jump up to:^{a b}
7. ^"Salmonella infection data for Prdx6". Wellcome Trust Sanger Institute.
8. ^"Citrobacter infection data for Prdx6". Wellcome Trust Sanger Institute.
9. ^ Jump up to:^{a b c}
10. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute
11. ^"International Knockout Mouse Consortium".
12. ^"Mouse Genome Informatics".
13. ^Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
14. ^Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
15. ^Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
16. ^van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
17. Abbas, M. N.; Kausar, S.; Cui, H. The Biological Role of Peroxiredoxins in Innate Immune Responses of Aquatic Invertebrates. Fish & Shellfish Immunology 2019, 89, 91–97.
18. Goo Rhee, S. (2016). Overview on peroxiredoxin. Molecules and Cells, 39(1), 1–5. https://doi.org/10.14348/molcells.2016.2368