4.6 Article

Proteomic and phosphoproteomic profiles of Sertoli cells in buffalo

Journal

THERIOGENOLOGY
Volume 170, Issue -, Pages 1-14

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.theriogenology.2021.04.013

Keywords

Proteomic; Phosphoproteomic; Sertoli cell; Spermatogenesis

Funding

  1. National Natural Science Foundation of China [31860643]
  2. Natural Science Foundation of Guangxi [2017GXNSFBA198117]
  3. State Key Laboratory for Conservation and Utilization of Subtropical AgroBioresources [SKLCUSAb201915]

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This study conducted an integrative analysis of the proteome and phosphoproteome of Sertoli cells in buffalo testes to explore their role in spermatogenesis. Multiple proteins were identified, with some being involved in gene expression, cellular localization, and transport processes. The results offer insights into male reproduction and provide a foundation for future research.
Sertoli cells provide nutrients and support for germ cell differentiation and maintain a stable microenvironment for spermatogenesis. Comprehensive identification of Sertoli cellular proteins is important in understanding spermatogenesis. In this study, we performed an integrative analysis of the proteome and phosphoproteome to explore the role of Sertoli cells in spermatogenesis. A total of 2912 and 753 proteins were identified from the proteome and phosphoproteome in Sertoli cells, respectively; 438 proteins were common to the proteome and phosphoproteome. Data are available via ProteomeXchange with identifier PXD024984. In the proteome, ACTG1, ACTB, ACTA2, MYH9 were the most abundant proteins. Gene Ontology (GO) analysis indicated that most of the proteins were involved in the processes of localization, biosynthesis, gene expression, and transport. In addition, some of the proteins related to Sertoli cell functions were also enriched. In the phosphoproteome, most of the proteins were involved in gene expression and the RNA metabolic process; the pathways mainly involved the spliceosome, mitogenactivated protein kinase signaling pathway, focal adhesion, and tight junctions. The pleckstrin homology-like domain is the most highly enriched protein domain in phosphoproteins. Cyclindependent kinases and protein kinases C were found to be highly active kinases in the kinasesubstrate network analysis. Ten proteins most closely related to network stability were found in the analysis of the network interactions of proteins identified jointly in the phosphoproteome and proteome. Through immunohistochemistry and immunofluorescence verification of vimentin, it was found that there were localization differences between phosphorylated and non-phosphorylated vimentin in testicular tissue. This study is the first in-depth proteomic and phosphoproteomic analysis of buffalo testicular Sertoli cells. The results provide insight into the role of Sertoli cells in spermatogenesis and provide clues for further study of male reproduction. (c) 2021 Elsevier Inc. All rights reserved.

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