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Updated: Jan 1, 2026
Phosphopeptide Analysis of Rodent Epididymal Spermatozoa
Published on: December 30, 2014
Quantitative proteomic characterization of human sperm cryopreservation: using data-independent acquisition mass
Longlong Fu1,2, Qi An1,2,3, Kaishu Zhang4
1National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning, Beijing, 100081, China.
Background:
Human sperm cryopreservation is a simple and effective approach for male fertility preservation.
Methods:
To identify potential proteomic changes in this process, data-independent acquisition (DIA), a technology with high quantitative accuracy and highly reproducible proteomics, was used to quantitatively characterize the proteomics of human sperm cryopreservation.
Results:
A total of 174 significantly differential proteins were identified between fresh and cryoperservated sperm: 98 proteins decreased and 76 proteins increased in the cryopreservation group. Bioinformatic analysis revealed that metabolic pathways play an important role in cryopreservation, including: propanoate metabolism, glyoxylate and dicarboxylate metabolism, glycolysis/gluconeogenesis, and pyruvate metabolism. Four different proteins involved in glycolysis were identified by Western blotting: GPI, LDHB, ADH5, and PGAM1.
Conclusions:
Our work will provide valuable information for future investigations and pathological studies involving sperm cryopreservation.
