The antioxidant glutathione peroxidase family and spermatozoa: A complex story

  title={The antioxidant glutathione peroxidase family and spermatozoa: A complex story},
  author={Joel R. Drevet},
  journal={Molecular and Cellular Endocrinology},
  • J. Drevet
  • Published 16 May 2006
  • Biology
  • Molecular and Cellular Endocrinology

Mammalian glutathione peroxidases control acquisition and maintenance of spermatozoa integrity.

The importance of the GPx protein family in determining the fertilizing potential of mammalian spermatozoa is underlined in the field of mammalian fertility and infertility as well as in the development of assisted medical procreation technologies and male gamete preservation techniques that are extensively used in human and animal reproduction programs.

Glutathione peroxidases at work on epididymal spermatozoa: an example of the dual effect of reactive oxygen species on mammalian male fertilizing ability.

The roles played by the sperm-associated forms of GPx4, the secreted GPx5 protein, and the epithelial proteins GPx1, GPx3, and cellular GPx2 are reviewed, all functioning in the mammalian epididymis at different stages of the sperm's epidIDymal journey, and in different epididcyis compartments.

Leukocytes and oxidative stress: dilemma for sperm function and male fertility.

  • R. Henkel
  • Biology
    Asian journal of andrology
  • 2011
A proper andrological diagnostic work-up, including the evaluation of ROS levels and the antioxidant capacity of the semen, has to be carried out beforehand, aimed at keeping the fine balance between oxidation and scavenging of vital amounts of ROS.

Role of oxidative stress and antioxidants in domestic and non-domestic cat spermatozoa

Living cells, including spermatozoa, stored under aerobic conditions require oxygen to support their normal metabolism. Excessive levels of metabolites (reactive oxygen species; ROS) can cause cell

Role of Oxidative Stress and Antioxidants in Domestic and Non- Domestic Cat Spermatozoa With special reference to cryopreservation

Living cells, including spermatozoa, stored under aerobic conditions require oxygen to support their normal metabolism. Excessive levels of metabolites (reactive oxygen species; ROS) can cause cell

Role of residual cytoplasm on oxidative status during sperm maturation in dogs.

Induced lipid peroxidation in ram sperm: semen profile, DNA fragmentation and antioxidant status.

An increase in native GPx activity and CAT immunodetection in groups with high susceptibility to induced lipid peroxidation is observed, which may be the main cause of chromatin damage in ram sperm.



Reactive oxygen species and human spermatozoa: physiology and pathology.

This review focuses on the nature and source of the ROS generated by human spermataozoa as well as their operational mechanisms and their effects, which may be detrimental or beneficial.

Antioxidant systems in rat epididymal spermatozoa.

In vitro peroxidation of the two sperm populations by the free radical generator 2,2'-azobis(2-amidinopropane) dihydrochloride revealed that only about 13% of the vitamin E content of the caput epididymidal spermatozoa was consumed, which contrasts with the greater consumption (about 70%) of the Vitamin E content in cauda epididylitezoa.

Levels of antioxidant defenses are decreased in bovine spermatozoa after a cycle of freezing and thawing

It is found that bovine spermatozoa are poorly adapted to metabolize the toxic hydrogen peroxide and the involvement of an oxidative stress during a freeze/thaw cycle is consistent with the hypothesis that ROS generated during such a cycle are detrimental to sperm function.

Analysis of Reactive Oxygen Species Generating Systems in Rat Epididymal Spermatozoa1

Analysis of superoxide anion generation by rat epididymal spermatozoa has revealed a two-component process involving electron leakage from the sperm mitochondria at complexes I and II and a plasma membrane NAD(P)H oxidoreductase.

Reactive oxygen species and sperm physiology.

The fine balance between ROS production and scavenging, as well as the right timing and site for ROS production are of paramount importance for acquisition of fertilizing ability.

Distribution and possible novel role of phospholipid hydroperoxide glutathione peroxidase in rat epididymal spermatozoa.

A role for the enzyme in the maturation of spermatozoa through the metabolism of hydroperoxides and sperm thiol oxidation, in addition to its serving as an antioxidant protector, is suggested.

Cooperative function of antioxidant and redox systems against oxidative stress in male reproductive tissues.

This work overviews the current understanding of the cooperative function of antioxidative and redox systems that are involved in male fertility and suggests that a comprehensive understanding will be required to maintain the physiological functions of male reproductive system.

A critical investigation of NADPH oxidase activity in human spermatozoa.

It is concluded that human spermatozoa do not possess significant NADPH oxidase activity and that the mechanism by which NADPH promotes capacitation must be re-evaluated.

Studies on the origin of redox enzymes in seminal plasma and their relationship with results of in-vitro fertilization.

The findings suggest that the protective enzymes in the seminal plasma are contributed largely by the prostate and little by the epididymis, and that in most cases of IVF, they have no major influence on the outcome.