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Quantitative phosphoproteomics explain cryopreservation-induced reductions in ram sperm motility.
Zang, Shengqin; Yang, Xiaorui; Ye, Jiangfeng; Mo, Xianhong; Zhou, Guangbin; Fang, Yi.
Afiliación
  • Zang S; Key Laboratory of Livestock and Poultry Multi-omics, Ministry of Agriculture and Rural Affairs, College of Animal Science and Technology (Institute of Animal Genetics and Breeding), Sichuan Agricultural University, Chengdu 611130, PR China.
  • Yang X; Key Laboratory of Animal Production, Product Quality and Security, Ministry of Education, College of Animal Science and Technology, Jilin Agricultural University, Jilin, Changchun 130118, China.
  • Ye J; Key Laboratory of Livestock and Poultry Multi-omics, Ministry of Agriculture and Rural Affairs, College of Animal Science and Technology (Institute of Animal Genetics and Breeding), Sichuan Agricultural University, Chengdu 611130, PR China.
  • Mo X; College of Chemistry and Life Science, Chifeng University, Chifeng 024000, PR China.
  • Zhou G; Key Laboratory of Livestock and Poultry Multi-omics, Ministry of Agriculture and Rural Affairs, College of Animal Science and Technology (Institute of Animal Genetics and Breeding), Sichuan Agricultural University, Chengdu 611130, PR China.
  • Fang Y; Key Laboratory of Animal Production, Product Quality and Security, Ministry of Education, College of Animal Science and Technology, Jilin Agricultural University, Jilin, Changchun 130118, China. Electronic address: 17743112414@163.com.
J Proteomics ; 298: 105153, 2024 04 30.
Article en En | MEDLINE | ID: mdl-38438079
ABSTRACT
Sperm cryopreservation decreases motility, probably due to changes in protein phosphorylation. Our objective was to use quantitative phosphoproteomics for systematic comparative analyses of fresh versus frozen-thawed sperm to identify factors causing cryo-injury. Ejaculates were collected (artificial vagina) from six Dorper rams, pooled, extended, and frozen over liquid nitrogen. Overall, 915, 3382, and 6875 phosphorylated proteins, phosphorylated peptides, and phosphorylation sites, respectively, were identified. At least two modified sites were present in 57.94% of the 6875 phosphosites identified, of which AKAP4 protein contained up to 331 modified sites. There were 732 phosphorylated peptides significantly up-regulated and 909 significantly down-regulated in frozen-thawed versus fresh sperm. Moreover, the conserved motif [RxxS] was significantly down-regulated in frozen-thawed sperm. Phosphorylation of sperm-specific proteins, e.g., AKAP3/4, CABYR, FSIP2, GSK3A/B, GPI, and ODF1/2 make them potential biomarkers to assess the quality of frozen-thawed ram sperm. Furthermore, these differentially phosphorylated proteins and modification sites were implicated in cryopreservation-induced changes in sperm energy production, fiber sheath composition, and various biological processes. We concluded that abnormal protein phosphorylation modifications are key regulators of reduced sperm motility. These novel findings implicated specific protein phosphorylation modifications in sperm cryo-injury.

SIGNIFICANCE:

This study used phosphorylated TMT quantitative proteomics to explore regulation of epigenetic modifications in frozen-thawed ram sperm. This experiment demonstrated that ram sperm freezing affects phosphorylation site modifications of proteins, especially those related to functions such as sperm motility and energy production. Furthermore, it is important to link functions of phosphorylated proteins with changes in sperm quality after freezing and thawing, and to clarify intrinsic reasons for sperm quality changes, which is of great importance for elucidating mechanisms of sperm freezing damage. Based on these protein markers and combined with cryoprotectant design theory, it provides a theoretical basis and data reference to study sperm cryoprotectants.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Preservación de Semen / Motilidad Espermática Límite: Animals Idioma: En Revista: J Proteomics Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Preservación de Semen / Motilidad Espermática Límite: Animals Idioma: En Revista: J Proteomics Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos