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Reproduction (Cambridge, England)2025; 170(1); e240436; doi: 10.1530/REP-24-0436

Stallion spermatozoa express LDH isoforms A, B, and C, with LDHC playing a crucial role in sustaining sperm viability.

Abstract: Three isoforms of lactate dehydrogenase (LDH) - LDHA (cytoplasmic), LDHB (mitochondrial), and LDHC (flagellar) - have been identified and localized in stallion spermatozoa. Functional inhibition assays indicate that these three isoforms constitute a lactate shuttle of crucial importance for sperm function. Unassigned: Stallion spermatozoa use different energy sources; while oxidative phosphorylation predominates, glycolysis and beta-oxidation of fatty acids are also present. Glycolysis depends on the availability of NAD+ as an electron acceptor. During glycolysis, NAD+ is reduced to NADH. To ensure glycolysis can continue, NAD+ must be regenerated. This regeneration typically occurs when NADH donates its electrons to the electron transport chain (specifically at Complex I), where it is oxidized back to NAD+. If mitochondria are damaged, the regeneration of NAD+ may be compromised, leading to reduced glycolysis and altering sperm metabolism. However, alternative ways to regenerate NAD+ may be present. We hypothesized that aerobic glycolysis is present in the stallion spermatozoa as a backup mechanism to regenerate NAD+. We incubated spermatozoa in two Tyrode's modified media with either 67 mM glucose and 1 mM pyruvate or 67 mM glucose and 10 mM pyruvate. The addition of 10 mM pyruvate improved sperm motility (P < 0.001). Spermatozoa incubated in 67 mM glucose and 1 mM pyruvate for 3 h at 37°C showed a significant decrease in motility (58.1 ± 1.8% vs 81.2 ± 1.8%, P < 0.0001). In contrast, spermatozoa incubated in 67 mM glucose and 10 mM pyruvate retained motility (77.1 ± 1.4%), viability, and mitochondrial membrane potential. We studied the metabolic proteome and metabolome and identified three different isoforms of the enzyme lactate dehydrogenase (LDH), LDHA (cytosolic), LDHB (mitochondrial, with higher affinity for pyruvate), and LDHC (cytosol, motile cilium). Functional experiments using a specific inhibitor of LDHC demonstrated that this isoform may be essential for sperm function. We concluded that activation of aerobic glycolysis in a high-glucose medium improves sperm survival through the regeneration of NAD+.
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Publication Date: 2025-06-05 PubMed ID: 40299647PubMed Central: PMC12150302DOI: 10.1530/REP-24-0436Google 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.

Overview

  • This research investigates how stallion sperm cells utilize different forms of lactate dehydrogenase (LDH) to maintain energy production and sperm viability, particularly focusing on the role of LDHC in regenerating NAD+ to support glycolysis and sperm function.

Background

  • Stallion spermatozoa rely on multiple energy sources including oxidative phosphorylation, glycolysis, and beta-oxidation of fatty acids.
  • Glycolysis requires NAD+ as an electron acceptor; NAD+ is converted to NADH during this process.
  • If mitochondria are damaged, the usual regeneration of NAD+ through the electron transport chain is impaired, potentially reducing glycolysis and affecting sperm metabolism.
  • Researchers hypothesized that aerobic glycolysis might serve as an alternative mechanism for NAD+ regeneration in stallion sperm.

Experimental Design and Methods

  • Spermatozoa were incubated in modified Tyrode’s media with two different pyruvate concentrations: 1 mM and 10 mM, both containing 67 mM glucose.
  • Motility, viability, and mitochondrial membrane potential of sperm were monitored after incubation.
  • Metabolic proteomics and metabolomics were used to identify the LDH isoforms present in sperm cells: LDHA (cytosolic), LDHB (mitochondrial), and LDHC (cytosolic, associated with the motile cilium/flagellum).
  • Functional inhibition experiments specifically targeted LDHC to evaluate its role in sperm function.

Key Findings

  • The presence of 10 mM pyruvate significantly improved sperm motility compared to 1 mM pyruvate, demonstrating better maintenance of motility at higher pyruvate concentrations (77.1% vs 58.1%).
  • Sperm incubated with higher pyruvate maintained viability and mitochondrial membrane potential, indicating healthier metabolic status.
  • All three LDH isoforms (LDHA, LDHB, and LDHC) are expressed in stallion sperm, each localized differently reflecting diverse metabolic roles:
    • LDHA: cytosolic enzyme involved in cytoplasm-based metabolic reactions.
    • LDHB: mitochondrial enzyme with a higher affinity for pyruvate, contributing to mitochondrial metabolism.
    • LDHC: associated with the flagellum, implicated in maintaining sperm motility and viability.
  • Inhibition of LDHC resulted in impaired sperm function, suggesting its essential role in regenerating NAD+ to sustain glycolysis in sperm cells.
  • The data supported the conclusion that aerobic glycolysis, facilitated by these LDH isoforms particularly LDHC, acts as a backup pathway to regenerate NAD+, ensuring continuous ATP production and sperm survival.

Conclusions and Implications

  • Stallion spermatozoa utilize a lactate shuttle system composed of LDHA, LDHB, and LDHC to sustain energy metabolism through both mitochondrial and glycolytic pathways.
  • LDHC is critical for sperm motility and viability by maintaining NAD+ regeneration during aerobic glycolysis.
  • Supplementation with higher pyruvate concentrations enhances sperm survival and function, likely by supporting the aerobic glycolytic pathway.
  • This research provides insight into sperm metabolism which could contribute to improved techniques for sperm preservation, fertilization processes, and treatments for male infertility in horses.

Cite This Article

APA
Becerro-Rey L, Martín-Cano FE, Silva-Rodríguez A, Ortega-Ferrusola C, da Silva-Álvarez E, Ortiz-Placín C, Tapia JA, Gil MC, Peña FJ. (2025). Stallion spermatozoa express LDH isoforms A, B, and C, with LDHC playing a crucial role in sustaining sperm viability. Reproduction, 170(1), e240436. https://doi.org/10.1530/REP-24-0436

Publication

Reproduction (Cambridge, England)
ISSN: 1741-7899
NlmUniqueID: 100966036
Country: England
Language: English
Volume: 170
Issue: 1
PII: e240436

Researcher Affiliations

Becerro-Rey, Laura
    Martín-Cano, Francisco E
      Silva-Rodríguez, Antonio
        Ortega-Ferrusola, Cristina
          da Silva-Álvarez, Eva
            Ortiz-Placín, Cándido
              Tapia, Jose Antonio
                Gil, María Cruz
                  Peña, Fernando J

                    MeSH Terms

                    • Male
                    • Animals
                    • Horses / metabolism
                    • Spermatozoa / enzymology
                    • Spermatozoa / physiology
                    • Spermatozoa / metabolism
                    • L-Lactate Dehydrogenase / metabolism
                    • L-Lactate Dehydrogenase / genetics
                    • Cell Survival
                    • Isoenzymes / metabolism
                    • Glycolysis
                    • Sperm Motility
                    • Mitochondria / enzymology
                    • Mitochondria / metabolism
                    • NAD / metabolism
                    • Lactate Dehydrogenase 5

                    Conflict of Interest Statement

                    The authors declare that there is no conflict of interest that could be perceived as prejudicing the impartiality of the work reported.

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