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Quantitative proteomic characterization of human sperm cryopreservation: using data-independent acquisition mass spectrometry.


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.

SUBMITTER: Fu L 

PROVIDER: S-EPMC6916233 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Quantitative proteomic characterization of human sperm cryopreservation: using data-independent acquisition mass spectrometry.

Fu Longlong L   An Qi Q   Zhang Kaishu K   Liu Ying Y   Tong Yue Y   Xu Jianfeng J   Zhou Fang F   Wang Xiaowei X   Guo Ying Y   Lu Wenhong W   Liang Xiaowei X   Gu Yiqun Y  

BMC urology 20191216 1


<h4>Background</h4>Human sperm cryopreservation is a simple and effective approach for male fertility preservation.<h4>Methods</h4>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.<h4>Results</h4>A total of 174 significantly differential proteins were identified between fresh and cryoper  ...[more]

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