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Cryopreservation Induces Acetylation of Metabolism-Related Proteins in Boar Sperm

Cryodamage affects the normal physiological functions and survivability of boar sperm during cryopreservation. Lysine acetylation is thought to be an important regulatory mechanism in sperm functions. However, little is known about protein acetylation and its effects on cryotolerance or cryodamage i...

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Autores principales: Ali, Malik Ahsan, Qin, Ziyue, Dou, Shan, Huang, Anqi, Wang, Yihan, Yuan, Xiang, Zhang, Yan, Ni, Qingyong, Azmat, Rameesha, Zeng, Changjun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10341673/
https://www.ncbi.nlm.nih.gov/pubmed/37446160
http://dx.doi.org/10.3390/ijms241310983
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author Ali, Malik Ahsan
Qin, Ziyue
Dou, Shan
Huang, Anqi
Wang, Yihan
Yuan, Xiang
Zhang, Yan
Ni, Qingyong
Azmat, Rameesha
Zeng, Changjun
author_facet Ali, Malik Ahsan
Qin, Ziyue
Dou, Shan
Huang, Anqi
Wang, Yihan
Yuan, Xiang
Zhang, Yan
Ni, Qingyong
Azmat, Rameesha
Zeng, Changjun
author_sort Ali, Malik Ahsan
collection PubMed
description Cryodamage affects the normal physiological functions and survivability of boar sperm during cryopreservation. Lysine acetylation is thought to be an important regulatory mechanism in sperm functions. However, little is known about protein acetylation and its effects on cryotolerance or cryodamage in boar sperm. In this study, the characterization and protein acetylation dynamics of boar sperm during cryopreservation were determined using liquid chromatography–mass spectrometry (LC-MS). A total of 1440 proteins were identified out of 4705 modified proteins, and 2764 quantifiable sites were elucidated. Among the differentially modified sites, 1252 were found to be upregulated compared to 172 downregulated sites in fresh and frozen sperms. Gene ontology indicated that these differentially modified proteins are involved in metabolic processes and catalytic and antioxidant activities, which are involved in pyruvate metabolism, phosphorylation and lysine degradation. In addition, the present study demonstrated that the mRNA and protein expressions of SIRT5, IDH2, MDH2 and LDHC, associated with sperm quality parameters, are downregulated after cryopreservation. In conclusion, cryopreservation induces the acetylation and deacetylation of energy metabolism-related proteins, which may contribute to the post-thawed boar sperm quality parameters.
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spelling pubmed-103416732023-07-14 Cryopreservation Induces Acetylation of Metabolism-Related Proteins in Boar Sperm Ali, Malik Ahsan Qin, Ziyue Dou, Shan Huang, Anqi Wang, Yihan Yuan, Xiang Zhang, Yan Ni, Qingyong Azmat, Rameesha Zeng, Changjun Int J Mol Sci Article Cryodamage affects the normal physiological functions and survivability of boar sperm during cryopreservation. Lysine acetylation is thought to be an important regulatory mechanism in sperm functions. However, little is known about protein acetylation and its effects on cryotolerance or cryodamage in boar sperm. In this study, the characterization and protein acetylation dynamics of boar sperm during cryopreservation were determined using liquid chromatography–mass spectrometry (LC-MS). A total of 1440 proteins were identified out of 4705 modified proteins, and 2764 quantifiable sites were elucidated. Among the differentially modified sites, 1252 were found to be upregulated compared to 172 downregulated sites in fresh and frozen sperms. Gene ontology indicated that these differentially modified proteins are involved in metabolic processes and catalytic and antioxidant activities, which are involved in pyruvate metabolism, phosphorylation and lysine degradation. In addition, the present study demonstrated that the mRNA and protein expressions of SIRT5, IDH2, MDH2 and LDHC, associated with sperm quality parameters, are downregulated after cryopreservation. In conclusion, cryopreservation induces the acetylation and deacetylation of energy metabolism-related proteins, which may contribute to the post-thawed boar sperm quality parameters. MDPI 2023-07-01 /pmc/articles/PMC10341673/ /pubmed/37446160 http://dx.doi.org/10.3390/ijms241310983 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ali, Malik Ahsan
Qin, Ziyue
Dou, Shan
Huang, Anqi
Wang, Yihan
Yuan, Xiang
Zhang, Yan
Ni, Qingyong
Azmat, Rameesha
Zeng, Changjun
Cryopreservation Induces Acetylation of Metabolism-Related Proteins in Boar Sperm
title Cryopreservation Induces Acetylation of Metabolism-Related Proteins in Boar Sperm
title_full Cryopreservation Induces Acetylation of Metabolism-Related Proteins in Boar Sperm
title_fullStr Cryopreservation Induces Acetylation of Metabolism-Related Proteins in Boar Sperm
title_full_unstemmed Cryopreservation Induces Acetylation of Metabolism-Related Proteins in Boar Sperm
title_short Cryopreservation Induces Acetylation of Metabolism-Related Proteins in Boar Sperm
title_sort cryopreservation induces acetylation of metabolism-related proteins in boar sperm
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10341673/
https://www.ncbi.nlm.nih.gov/pubmed/37446160
http://dx.doi.org/10.3390/ijms241310983
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