Longlong Fu1,2, Qi An1,2,3, Kaishu Zhang4, Ying Liu5, Yue Tong1,2,3, Jianfeng Xu1,2, Fang Zhou1,2, Xiaowei Wang1,2, Ying Guo1,2, Wenhong Lu6,7, Xiaowei Liang2, Yiqun Gu8,9,10. 1. National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning, Beijing, 100081, China. 2. Department of Male Clinical Research/Human sperm bank, National Research Institute for Family Planning & WHO Collaborating Center for Research in Human Reproduction, Beijing, 100081, China. 3. Graduate School of Peking Union Medical College, Beijing, 100730, China. 4. Department of Reproductive Medicine, The Afliated Hospital of Qingdao University, Qingdao, Shandong, 266000, People's Republic of China. 5. Institute of Pediatric Research, Children's Hospital of Soochow University, Suzhou, Jiangsu Province, 215025, China. 6. National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning, Beijing, 100081, China. wenhonglu16@163.com. 7. Graduate School of Peking Union Medical College, Beijing, 100730, China. wenhonglu16@163.com. 8. National Health Commission Key Laboratory of Male Reproductive Health, National Research Institute for Family Planning, Beijing, 100081, China. guyq16@163.com. 9. Department of Male Clinical Research/Human sperm bank, National Research Institute for Family Planning & WHO Collaborating Center for Research in Human Reproduction, Beijing, 100081, China. guyq16@163.com. 10. Graduate School of Peking Union Medical College, Beijing, 100730, China. guyq16@163.com.
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.
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.
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