Next Article in Journal
Antioxidant Activities, Phenolic Profiles, and Organic Acid Contents of Fruit Vinegars
Next Article in Special Issue
Antioxidants Special Issue: Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family
Previous Article in Journal
Development and Validation of an Analytical Method for Carnosol, Carnosic Acid and Rosmarinic Acid in Food Matrices and Evaluation of the Antioxidant Activity of Rosemary Extract as a Food Additive
Previous Article in Special Issue
Peroxiredoxin6 in Endothelial Signaling
Review

Mouse Models of Genetically Altered Peroxiredoxin 6

1
Institute for Environmental Medicine, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA
2
Peroxitech, Ltd., Philadelphia, PA 19104, USA
Antioxidants 2019, 8(4), 77; https://doi.org/10.3390/antiox8040077
Received: 18 January 2019 / Revised: 7 March 2019 / Accepted: 20 March 2019 / Published: 27 March 2019
(This article belongs to the Special Issue Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family)
Peroxiredoxin 6 (Prdx6) has been shown to have three enzymatic activities: peroxidase, phospholipase A2 (PLA2) and acyl transferase. The peroxidase activity is unusual, as it is capable of reducing phospholipid hydroperoxides (as well as hydrogen peroxide and short chain organic peroxides). Knockout and overexpressing mice have been produced that demonstrate the effect that eliminating or overproducing Prdx6 has on the animals’ physiology. In addition, mutations in various amino acids of Prdx6 have been identified that interfere with different enzymatic functions as well as protein transport. These mutations were originally characterized biochemically; subsequently, several knock-in mouse strains have been produced, each containing one mutation. These mice include the S32T knock-in that affects protein transport, the C47S knock-in that inactivates the peroxidase enzymatic activity, the D140A knock-in that inactivates the PLA2 enzymatic activity and the H26A knock-in that inactivates the peroxidase and blocks binding to phospholipids. This review summarizes the properties of these mice based upon studies conducted with the knockout, overexpressing and knock-in mice and the effect of the genetic changes on the biochemistry and physiology of these mice. The availability of these mice is also briefly discussed. View Full-Text
Keywords: peroxidase; phospholipase A2; lipid peroxidation; phospholipid hydroperoxide; knockout mouse; knock-in mouse; membrane repair peroxidase; phospholipase A2; lipid peroxidation; phospholipid hydroperoxide; knockout mouse; knock-in mouse; membrane repair
MDPI and ACS Style

Feinstein, S.I. Mouse Models of Genetically Altered Peroxiredoxin 6. Antioxidants 2019, 8, 77. https://doi.org/10.3390/antiox8040077

AMA Style

Feinstein SI. Mouse Models of Genetically Altered Peroxiredoxin 6. Antioxidants. 2019; 8(4):77. https://doi.org/10.3390/antiox8040077

Chicago/Turabian Style

Feinstein, Sheldon I. 2019. "Mouse Models of Genetically Altered Peroxiredoxin 6" Antioxidants 8, no. 4: 77. https://doi.org/10.3390/antiox8040077

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop