Abstract
Follicular fluid (FF) accumulates in the antrum of the ovarian follicle and provides the microenvironment for oocyte development. FF plays an important role in follicle growth and oocyte maturation. The FF provides a unique window to investigate the processes occurring during buffalo follicular development. The observed low quality of buffalo oocytes may arise from the poor follicular microenvironment. Investigating proteins found in buffalo FF (BFF) should provide insight into follicular development processes and provide further understanding of intra-follicular maturation and oocytes quality. Here, a proteomic-based approach was used to analyze the proteome of BFF. SDS-PAGE separation combined with mass spectrometry was used to generate the proteomic dataset. In total, 363 proteins were identified and classified by Gene Ontology terms. The proteins were assigned to 153 pathways, including signaling pathways. To evaluate difference in proteins expressed between BFF with different follicle size (small, <4 mm; and large, >8 mm), a quantitative proteomic analysis based on multi-dimensional liquid chromatography pre-fractionation tandem Orbitrap mass spectrometry identification was performed. Eleven differentially expressed proteins (six downregulated and five upregulated in large BFF) were identified and assigned to a variety of functional processes, including serine protease inhibition, oxidation protection and the complement cascade system. Three differentially expressed proteins, Vimentin, Peroxiredoxin-1 and SERPIND1, were verified by Western blotting, consistent with the quantitative proteomics results. Our datasets offers new information about proteins present in BFF and should facilitate the development of new biomarkers. These differentially expressed proteins illuminate the size-dependent protein changes in follicle microenvironment.
Highlights
Follicles form in the cortex of the mammalian ovary following the recruitment of primordial follicles
Follicles obtained from female buffalo were divided into two groups according to their diameter: (1) small, 8 mm in diameter
A total of 363 proteins were identified from buffalo FF (BFF) using a shotgun proteomic analysis approach
Summary
Follicles form in the cortex of the mammalian ovary following the recruitment of primordial follicles. During the initial period of ovarian follicle development, a cavity termed the antrum is formed that fills with follicular fluid (FF). FF is composed of secretions from the surrounding granulosa cells (GCs) and selective exudates of blood serum, including proteins, metabolites, ionic compounds and regulatory factors. Numerous studies have revealed that key substances are essential for the development of oocyte and granulosa cells [4,5,6]. FF serves as a mediator of communication between the oocyte and GCs. Embryo quality is associated with the presence and concentration of biomarkers in FF [7,8,9]. Understanding the details of FF composition, especially proteins, should provide a comprehensive view of folliculogenesis and aid in the assessment of oocyte quality. Characterizing the mammalian FF proteome has become an active area of research, especially in the last decade
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