Aldehyde Dehydrogenase Plays a Pivotal Role in the Maintenance of Stallion Sperm Motility.
Abstract: Although stallion spermatozoa produce significant quantities of reactive oxygen species, a lag between 4-hydroxynonenal (4HNE) adduction and the loss of motility in stallion spermatozoa suggests the presence of a robust aldehyde detoxification mechanism. Because there is a paucity of studies characterizing the role of aldehyde dehydrogenase (ALDH) in sperm functionality, the aim of this study was to ascertain the relationship between 4HNE production and motility and ALDH expression by stallion spermatozoa. PCR analysis revealed the presence of the ALDH1A3, ALDH1B1, and ALDH2 isoforms in these cells. Strong correlations (P < 0.001) were found between ALDH expression and various motility parameters of stallion spermatozoa including the percentage of progressive (r = 0.79) and rapidly motile (r = 0.79) spermatozoa, whereas repeated measurements over 24 h revealed highly significant correlations among progressive motility loss, 4HNE accumulation, and ALDH expression (P ≤ 0.001). ALDH inhibition resulted in a spontaneous increase in 4HNE levels in viable cells (21.1 ± 5.8% vs. 42.6 ± 5.2%; P ≤ 0.05) and a corresponding decrease in total motility (41.7 ± 6.2% vs. 6.4 ± 2.6%; P ≤ 0.001) and progressive motility (17.0 ± 4.1% vs. 0.7 ± 0.4%; P ≤ 0.001) of stallion spermatozoa over 24 h. Similarly, inhibition of ALDH in 4HNE-challenged spermatozoa significantly reduced total motility over 4 h (35.4 ± 9.7% vs. 15.3 ± 5.1%, respectively; P ≤ 0.05). This study contributes valuable information about the role of the ALDH enzymes in the maintenance of stallion sperm functionality, with potential diagnostic and in vitro applications for assisted reproductive technologies.
© 2016 by the Society for the Study of Reproduction, Inc.
Publication Date: 2016-04-20 PubMed ID: 27103446DOI: 10.1095/biolreprod.116.140509Google Scholar: Lookup
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- Journal Article
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Summary
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This research investigates the role of aldehyde dehydrogenase (ALDH) in maintaining the motility of stallion spermatozoa. It reveals that the ALDH enzymes play a crucial role in detoxifying harmful substances and promoting the motility of sperm cells, which could have important implications for reproductive technologies and diagnosis of sperm abnormalities.
Objective of the Study
- The research was conducted to explore the relationship between the production of a harmful compound called 4-hydroxynonenal (4HNE) in sperm cells and the expression of an enzyme group called aldehyde dehydrogenase (ALDH) in stallion spermatozoa. This relationship was sought to understand the factors affecting sperm motility.
Methodology
- By employing PCR analysis, the researchers detected the presence of specific isoforms of the ALDH gene in stallion spermatozoa.
- The correlation between ALDH expression and various sperm motility parameters was studied. Also, changes in motility, 4HNE accumulation, and ALDH expression were measured over 24 hours.
- Furthermore, the effect of ALDH inhibition on 4HNE levels and sperm motility was also examined.
Findings
- The study determined strong correlations between the expression of ALDH enzymes and the percentage of progressively and rapidly motile spermatozoa.
- Researchers observed a significant increase in 4HNE levels within viable cells following ALDH inhibition. Correspondingly, this led to a decrease in both total and progressive motility of stallion spermatozoa.
- Notably, inhibition of ALDH in 4HNE-challenged spermatozoa significantly reduces total motility over a span of 4 hours.
Implications of the Study
- This research provides valuable insights into the critical role of ALDH enzymes in maintaining sperm functionality in stallions.
- The findings might hold diagnostic value in detecting sperm abnormalities and could potentially be applied to assisted reproductive technologies.
Cite This Article
APA
Gibb Z, Lambourne SR, Curry BJ, Hall SE, Aitken RJ.
(2016).
Aldehyde Dehydrogenase Plays a Pivotal Role in the Maintenance of Stallion Sperm Motility.
Biol Reprod, 94(6), 133.
https://doi.org/10.1095/biolreprod.116.140509 Publication
Researcher Affiliations
- Priority Research Centre for Reproductive Science, Discipline of Biological Sciences, Faculty of Science and IT, University of Newcastle, Callaghan, New South Wales, Australia zamira.gibb@newcastle.edu.au.
- Priority Research Centre for Reproductive Science, Discipline of Biological Sciences, Faculty of Science and IT, University of Newcastle, Callaghan, New South Wales, Australia.
- Priority Research Centre for Reproductive Science, Discipline of Biological Sciences, Faculty of Science and IT, University of Newcastle, Callaghan, New South Wales, Australia.
- Priority Research Centre for Reproductive Science, Discipline of Biological Sciences, Faculty of Science and IT, University of Newcastle, Callaghan, New South Wales, Australia.
- Priority Research Centre for Reproductive Science, Discipline of Biological Sciences, Faculty of Science and IT, University of Newcastle, Callaghan, New South Wales, Australia.
MeSH Terms
- Aldehyde Dehydrogenase / metabolism
- Aldehydes / metabolism
- Animals
- Glutathione Transferase / metabolism
- Horses / metabolism
- Isoenzymes
- Lipid Peroxidation
- Male
- Sperm Motility
- Spermatozoa / enzymology
Citations
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