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Home / Equine Research Bank / Antioxidants (Basel) / Specific Activity of Superoxide Dismutase in Stallion Semina...
Antioxidants (Basel, Switzerland)2019; 8(11); 539; doi: 10.3390/antiox8110539

Specific Activity of Superoxide Dismutase in Stallion Seminal Plasma Is Related to Sperm Cryotolerance.

Abstract: While the removal of seminal plasma is a routine practice prior to equine sperm cryopreservation, this fluid contains the main source of antioxidant enzymes able to scavenge these reactive oxygen species. Therefore, stallion seminal plasma components may have an impact on ejaculate freezability. Against this background, this study was designed to investigate whether the activities of the main stallion seminal plasma antioxidant enzymes are related to sperm cryotolerance. With this purpose, 16 ejaculates were collected from 14 healthy stallions, and each ejaculate was split into two aliquots. The first one was used to evaluate the activities of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPX), and glutathione reductase (GSR) in seminal plasma. The second aliquot was extended and then processed for cryopreservation. Sperm motility and viability were evaluated before and after cryopreservation, and ejaculates were classified as of good (GFE) or poor freezability (PFE) based on total motile and viable spermatozoa at post-thaw. We observed that, while the specific activities of CAT, GPX, and GSR were similar between GFE and PFE, that of SOD was significantly ( < 0.05) higher in GFE than in PFE. We can thus conclude that, in stallions, the specific activity of SOD in the seminal plasma of a given ejaculate might be related to its freezability.
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Publication Date: 2019-11-09 PubMed ID: 31717586PubMed Central: PMC6912747DOI: 10.3390/antiox8110539Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The study assesses the effect of antioxidant enzymes in stallion seminal plasma on sperm cryotolerance, specifically focusing on superoxide dismutase (SOD). The research found that higher SOD activity may indicate better sperm freezability.

Objective and Methodology

  • The main objective of this study was to identify the relationship between the activity levels of primary antioxidant enzymes in stallion seminal plasma and the freezability (cryotolerance) of sperm.
  • 16 ejaculates were taken from 14 healthy stallions and each ejaculate was used for two main purposes.
  • One aliquot of the ejaculate was used to evaluate the activity of specific antioxidant enzymes including superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPX), and glutathione reductase (GSR).
  • The second aliquot was prepared and processed for freezing to examine the sperm’s cryotolerance.
  • Sperm mobility and viability were checked before and after freezing and were grouped as either good (GFE) or poor freezability (PFE) based on total moveable and viable spermatozoa post-thaw.

Findings

  • The findings indicate that while the activities of CAT, GPX, and GSR enzymes did not show a significant difference between GFE and PFE, SOD activity was significantly higher in ejaculates with good freezability compared to poor freezability.
  • The research thus concludes that in stallions, the activity of SOD in a given ejaculate’s seminal plasma might be closely related to its freezing tolerance.

Implications

  • The study’s findings could play a crucial role in enhancing our understanding of equine sperm cryopreservation.
  • Given that seminal plasma is typically removed before equine sperm cryopreservation, this study supports the idea that the presence and activity level of antioxidant enzymes, particularly SOD in seminal plasma, could impact how well sperm can be cryopreserved.

Cite This Article

APA
Papas M, Catalán J, Fernandez-Fuertes B, Arroyo L, Bassols A, Miró J, Yeste M. (2019). Specific Activity of Superoxide Dismutase in Stallion Seminal Plasma Is Related to Sperm Cryotolerance. Antioxidants (Basel), 8(11), 539. https://doi.org/10.3390/antiox8110539

Publication

Antioxidants (Basel, Switzerland)
ISSN: 2076-3921
NlmUniqueID: 101668981
Country: Switzerland
Language: English
Volume: 8
Issue: 11
PII: 539

Researcher Affiliations

Papas, Marion
  • Equine Reproduction Service, Department of Animal Medicine and Surgery, Faculty of Veterinary Sciences, Autonomous University of Barcelona, E-08193 Bellaterra, Spain.
Catalán, Jaime
  • Equine Reproduction Service, Department of Animal Medicine and Surgery, Faculty of Veterinary Sciences, Autonomous University of Barcelona, E-08193 Bellaterra, Spain.
Fernandez-Fuertes, Beatriz
  • Biotechnology of Animal and Human Reproduction (TechnoSperm), Unit of Cell Biology, Department of Biology, Institute of Food and Agricultural Technology, Faculty of Sciences, University of Girona, E-17003 Girona, Spain.
Arroyo, Laura
  • Department of Biochemistry and Molecular Biology, Faculty of Veterinary Sciences, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain.
Bassols, Anna
  • Department of Biochemistry and Molecular Biology, Faculty of Veterinary Sciences, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain.
Miró, Jordi
  • Equine Reproduction Service, Department of Animal Medicine and Surgery, Faculty of Veterinary Sciences, Autonomous University of Barcelona, E-08193 Bellaterra, Spain.
Yeste, Marc
  • Biotechnology of Animal and Human Reproduction (TechnoSperm), Unit of Cell Biology, Department of Biology, Institute of Food and Agricultural Technology, Faculty of Sciences, University of Girona, E-17003 Girona, Spain.

Grant Funding

  • H2020-MSCA-IF-79212 / European Commission
  • RYC-2014-15581 / Ministerio de Ciencia, Innovaciu00f3n y Universidades
  • AGL2017-88329-R / Ministerio de Ciencia, Innovaciu00f3n y Universidades
  • SGR-2017-1229 / Agu00e8ncia de Gestiu00f3 d'Ajuts Universitaris i de Recerca

Conflict of Interest Statement

The authors declare no conflict of interest.

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Citations

This article has been cited 13 times.
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