Protective role of testis-specific peroxiredoxin 4 against cellular oxidative stress

  title={Protective role of testis-specific peroxiredoxin 4 against cellular oxidative stress},
  author={Eisuke Tasaki and S Matsumoto and Hisashi Tada and Toshihiro Kurahashi and Xuhong Zhang and Junichi Fujii and Toshihiko Utsumi and Yoshihito Iuchi},
  journal={Journal of Clinical Biochemistry and Nutrition},
  pages={156 - 161}
Peroxiredoxin (PRDX), a newly discovered antioxidant enzyme, has an important role in hydrogen peroxide reduction. Among six PRDX genes (PRDX1–6) in mammals, PRDX4 gene is alternatively spliced to produce the somatic cell form (PRDX4) and the testis specific form (PRDX4t). In our previous study, PRDX4 knockout mice displayed testicular atrophy with an increase in cell death due to oxidative stress. However, the antioxidant function of PRDX4t is unknown. In this study, we demonstrate that PRDX4t… 
Testis-specific peroxiredoxin 4 variant is not absolutely required for spermatogenesis and fertility in mice
It is concluded that the disruption of the function of PRDX4t in the spermatogenic process appears to be compensated by other factors including GPX4, which plays an essential role in the disulfide bond formation during sperMatogenesis.
Mutual interaction between oxidative stress and endoplasmic reticulum stress in the pathogenesis of diseases specifically focusing on non-alcoholic fatty liver disease
Protecting the ER by eliminating excessive ROS via the administration of antioxidants or by enhancing lipid-metabolizing capacity via the activation of peroxisome proliferator-activated receptors represent promising therapeutics for NAFLD.
TXNRD3 supports male fertility via the redox control of spermatogenesis
The results show that TXNRD3 plays a critical role in male reproduction via the thiol redox control of spermatogenesis via theThioredoxin/glutathione reductase evolved by gene duplication within the Txnrd family.


Peroxiredoxin 4 knockout results in elevated spermatogenic cell death via oxidative stress.
The results suggest that the presence of Prx4, most likely the membrane-bound form, is important for spermatogenesis, but not an absolute requisite.
Peroxiredoxin 6 as an antioxidant enzyme: Protection of lung alveolar epithelial type II cells from H2O2‐induced oxidative stress
Prdx6 has been shown previously to reduce phospholipid hydroperoxides and it is postulated that this activity is a major mechanism for the effectiveness of Prdx6 as an antioxidant enzyme in mouse AEC II.
Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells.
A characterization of Prx IV in human cells demonstrating that it is actually retained within the ER (endoplasmic reticulum) and oligomeric interactions are stabilized by additional non-catalytic disulfide bonds, indicative of a primary role other than peroxide elimination.
Physiological and pathological views of peroxiredoxin 4.
Circumstantial evidence, together with deduced functions from the systemic form, suggests that there are potential roles for testicular PRDX4 in the reproductive processes such as the regulation of hormonal signals and the oxidative packaging of sperm chromatin.
1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage
The results indicate that 1-cysPrx can scavenge peroxides but in addition can reduce peroxidized membrane phospholipids, thereby playing an important role in cellular defense against oxidant stress.
Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein
  • J. Fujii, Y. Ikeda
  • Biology, Medicine
    Redox report : communications in free radical research
  • 2002
A comparative study of the divergence would lead to a better understanding of the biological significance of the Prx family, and suggest that individual members serve divergent functions which are associated with various biological processes such as the detoxification of oxidants, cell proliferation, differentiation and gene expression.
Structure, mechanism and regulation of peroxiredoxins.
Using crystal structures, a detailed catalytic cycle has been derived for typical 2-Cys Prxs, including a model for the redox-regulated oligomeric state proposed to control enzyme activity.
Identification and Characterization of Alternatively Transcribed Form of Peroxiredoxin IV Gene That Is Specifically Expressed in Spermatids of Postpubertal Mouse Testis*
It is suggested that Prx IV-L functions as an H2O2 sensor that mediates protein thiol oxidation required for the maturation of spermatozoa in placental mammals.
Inactivation of Peroxiredoxin I by Phosphorylation Allows Localized H2O2 Accumulation for Cell Signaling
It is shown that PrxI associated with membranes is transiently phosphorylated on tyrosine-194 and thereby inactivated both in cells stimulated via growth factor or immune receptors in vitro and in those at the margin of healing cutaneous wounds in mice.
Free radicals in the physiological control of cell function.
  • W. Dröge
  • Biology, Medicine
    Physiological reviews
  • 2002
There is growing evidence that aging involves, in addition, progressive changes in free radical-mediated regulatory processes that result in altered gene expression.