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 Prdx6tm1a(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].