ArticleCell communication and signaling : CCS2025
PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress.
Article in Cell communication and signaling : CCS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Comparative proteomic characterization of seminal plasma and sperm proteins associated with reproductive function in the Indo-Pacific bottlenose dolphin (Tursiops aduncus).Veterinary world · 2026Article
- Reactive Oxygen Species-Induced Damage in Cryopreserved Bovine Sperm: Mitigation Strategies.Veterinary medicine and science · 2026Review
- Single-cell analysis reveals cellular heterogeneity and molecular features during postnatal pig testis development.BMC genomics · 2025Article
- Mechanisms and etiology of male health disorders: hormones, cancer, and fertility.Cell communication and signaling : CCS · 2025Article
- Exploring the effect of skim milk on the membrane stability of frozen-thawed Inner Mongolia cashmere goat sperm based on proteomics.Frontiers in cell and developmental biology · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
Cryopreservation of bull sperm, crucial for breeding and assisted reproduction, often reduces sperm quality due to oxidative stress. This study examines how oxidative stress during cryopreservation affects peroxiredoxin 5 (PRDX5) and peroxiredoxin 6 (PRDX6) proteins, leading to their translocation and oligomerization in bull sperm. Increased reactive oxygen species (ROS) and nitric oxide (NO) levels were linked to reduced mitochondrial potential, higher DNA fragmentation, and increased membrane fluidity, prompting PRDX5 to move intracellularly and PRDX6 to the cell membrane. Under cryopreservation, these proteins formed high molecular weight oligomers, that may shift from peroxidase to chaperone roles. Their interaction with Toll-like receptor 4 (TLR4) may be key to their intracellular transport. On the other hand, the presence of PRDX5 and PRDX6 in exosomal vesicles suggested a potential mechanism for their transport into sperm cells. Using Imaging Flow Cytometry and various PAGE techniques, the study detected PRDX5 and PRDX6 in different sperm locations and analyzed their oligomer formation. These findings highlight the adaptive roles of PRDX5 and PRDX6 in protecting sperm cells, offering insights that could improve cryopreservation protocols in animal breeding and human reproductive medicine, and advance our understanding of the oxidative stress response in sperm cells.
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