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Proteomic analysis of boar sperm with differential ability of liquid preservation at 17 °C.
Song, Chenglei; Zhang, Zhe; Wei, Yilin; Dou, Yaqing; Qi, Kunlong; Li, Xiuling; Yang, Feng; Li, Xinjian; Wang, Kejun; Qiao, Ruimin; Han, Xuelei.
Afiliação
  • Song C; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Zhang Z; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Wei Y; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Dou Y; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Qi K; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Li X; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Yang F; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Li X; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Wang K; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Qiao R; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China.
  • Han X; College of Animal Science and Technology, Henan Agricultural University, Zhengzhou, 450046, China. Electronic address: hxl014@126.com.
Theriogenology ; 215: 103-112, 2024 Feb.
Article em En | MEDLINE | ID: mdl-38029685
ABSTRACT
Understanding the liquid preservation ability of boar sperm is pivotal for efficient management and breeding of livestock. Although sperm proteins play an important role in semen quality and freezability, how the levels of protein change in boar sperm with different liquid preservation abilities at 17 °C remains unclear. In this study, two groups of boar sperm with extreme difference in liquid preservation ability, namely the good preservation ability (GPA) and the poor preservation ability (PPA) groups, were selected by evaluating sperm motility parameters on the 7th day of liquid preservation at 17 °C. Quantitative proteomics based on tandem mass tag (TMT) labeling was used, sperm proteomic characteristics from two groups were analyzed, and potentially key proteins related to the fluid preservation ability of sperm were identified. A total of 187 differentially expressed proteins (DEPs) were identified among 2791 quantified proteins, including 85 upregulated, and 102 downregulated proteins. Further, Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analyses of the DEPs revealed that they were enriched in GO terms associated with response to oxidative stress, enzyme activity related to oxidative stress or redox reactions, and several metabolic activities. The significant KEGG pathways included peroxisome, metabolic pathways, selenocompound metabolism, and collection duct acid secretion. In addition, analysis of protein-protein interactions further identified 8 proteins that could be used as biomarker candidates, including GPX5, GLRX, ENO4, QPCT, BBS7, OXSR1, DHRS4 and AP2S1, which may play an essential role in indicating the liquid preservation ability of boar sperm. These findings in this study provide new insights into the underlying molecular mechanisms of the liquid preservation ability of boar sperm. Moreover, the selected candidate proteins can serve as a reference for evaluating sperm quality or preservation ability in boars and their application in related biotechnologies.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Preservação do Sêmen / Análise do Sêmen Limite: Animals Idioma: En Revista: Theriogenology Ano de publicação: 2024 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Preservação do Sêmen / Análise do Sêmen Limite: Animals Idioma: En Revista: Theriogenology Ano de publicação: 2024 Tipo de documento: Article País de afiliação: China