Quantitative proteomic characterization of human sperm cryopreservation: using data-independent acquisition mass spectrometry
Longlong Fu,
Qi An,
Kaishu Zhang,
Ying Liu,
Yue Tong,
Jianfeng Xu,
Fang Zhou,
Xiaowei Wang,
Ying Guo,
Wenhong Lu,
Xiaowei Liang,
Yiqun Gu
Affiliations
Longlong Fu
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Qi An
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Kaishu Zhang
Department of Reproductive Medicine, The Afliated Hospital of Qingdao University
Ying Liu
Institute of Pediatric Research, Children’s Hospital of Soochow University
Yue Tong
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Jianfeng Xu
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Fang Zhou
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Xiaowei Wang
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Ying Guo
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Wenhong Lu
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Xiaowei Liang
Department of Male Clinical Research/Human sperm bank, National Research Institute for Family Planning & WHO Collaborating Center for Research in Human Reproduction
Yiqun Gu
National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning
Abstract 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.