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Cold shock, chilling and cryopreservation impact sperm proteasome function
Grace Voss1, Mikayla Crouch1, Michal Zigo2
1School of Veterinary Science, The University of Queensland, Gatton, Australia.
Reproduction (Cambridge, England)
|October 7, 2025
Summary
Sperm preservation alters proteasome function, impacting fertility. Chilling and freezing significantly change proteasome activities, with cryopreservation increasing some activities while oxidative stress decreases all. Further research is needed.
Area of Science:
- Reproductive biology
- Molecular biology
- Biochemistry
Background:
- Sperm preservation methods like cryopreservation can cause sublethal molecular damage, reducing fertility and assisted reproductive technology efficacy.
- Oxidative stress is a key factor in cryopreservation-induced sperm damage, which somatic cells manage via proteasome activity.
- The relationship between sperm proteasome function and cryopreservation-induced oxidative stress remains unexplored.
Purpose of the Study:
- To investigate the impact of cold shock, chilled storage, and cryopreservation on ram sperm proteasome activity.
- To explore the direct effects of oxidative stress on sperm proteasome function.
- To describe novel molecular changes in sperm due to preservation.
Main Methods:
- Ram spermatozoa were subjected to cold shock, chilled storage, or cryopreservation.
- Fresh sperm were exposed to varying levels of hydrogen peroxide (H2O2) to simulate oxidative stress.
- Sperm motility was assessed using computer-assisted sperm analysis.
- Proteasome activities (caspase-like, chymotrypsin-like, trypsin-like) were measured using fluorogenic peptide substrates.
- Proteasome subunit abundance was determined via western blotting.
Main Results:
- Chilled storage significantly decreased caspase-like and chymotrypsin-like proteasome activities, while cryopreservation significantly increased them.
- Trypsin-like activity decreased with cold shock and cryopreservation, and showed a trend of decrease with chilling.
- All measured proteasome activities significantly decreased under induced oxidative stress.
- Cryopreservation led to an apparent increase in proteasome subunit abundance, unlike chilled storage.
Conclusions:
- Sperm proteasome function is demonstrably altered by oxidative stress and common preservation methods (chilling, freezing).
- These alterations represent a new molecular change associated with sperm preservation.
- The functional consequences of these observed changes in sperm proteasome activity on fertility require further investigation.
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