Hui Peng Similar Datasets
Project description:A greater understanding of the proteins involved in reproduction can benefit animal production. New advances in proteomics are having a major impact on our understanding of how spermatozoa acquire their capacity for fertilization [1]. Sperm proteomics aims at the identification of the proteins that compose the sperm cell and the study of their function [2]. The sperm cell is one of the most highly differentiated cells and is composed of a head with a highly compacted chromatin structure and a large flagellum with midpiece that contains the required machinery for movement and therefore to deliver the paternal genetic and epigenetic content to the oocyte [3]. By being so highly differentiated, spermatozoa are advantageous cells to study proteomics of specific compartments such as the membrane, which basically is the area of major importance for its role in interacting with the surroundings and the oocyte [4]. The fusion of a sperm and an oocyte is a sophisticated process that must be preceded by suitable changes in the sperm's membrane composition [5]. Recent studies of spermatozoa from the proteomic point of view have allowed the identification of different proteins in spermatozoa that are responsible for the regulation of normal/defective sperm functions [6]. While several techniques are available in proteomics, LC-MS based analysis of complex protein/peptide mixtures has turned out to be a mainstream analytical technique for quantitative proteomics [7]. Using this method, detailed proteomic data are now available for human [8], macaque [9,10], mouse [11], rat [12], bull [13-15], stallion [16], fruit fly [17], Caenorhabditis elegans [18], carp [19], rainbow trout [20], mussel [21], ram [22], honeybee [23] and rooster [24] sperm membrane proteins. Rabbit (Oryctolagus cuniculus) is an important mammalian species worldwide, being at the same time of commercial interest and a research model animal. European rabbit meat production is approximately 500 thousand tons, corresponding to a 30% share of world production [25]. Besides, rabbits account for the seventh highest number of animals slaughtered per year in the European Union-27, with 347,603 × 1000 head in 2014 [26]. In a previous work, we identified and quantified rabbit seminal plasma proteins between two different genotypes [27], concluding the clear effect of genotype in the abundance of certain seminal plasma proteins. However, it is unknown at present whether these differences also exist at sperm proteome level. Therefore, the aim of the present study was to characterise rabbit sperm membrane proteins through NanoLC-MS/MS analysis focusing on the influence of the genetic origin.
2019-02-15 | PXD007989 | Pride
Project description:The data in this study were obtained from proteomics and phosphoproteomics analyses of bull sperm during the cryopreservation process, with or without the addition of melatonin. The experiment employed TMT-10 plex labeling technology to analyze the proteome and phosphoproteome of three groups: before sperm cryopreservation, after cryopreservation without melatonin, and after cryopreservation with melatonin.
| PXD057125 |
Project description:Cryoinjury and protein changes are a consequence of cryopreservation and may have a negative impact on sperm quality regarding motility, viability and fertilizing ability. However, potential proteomic changes in rabbit semen throughout the cryopreservation process have never been investigated previously. The aim of the present study was to compare the whole proteome of fresh and cryopreserved rabbit spermatozoa. Comparative analysis and identification of proteins were performed using 2-dimensional difference in-gel electrophoresis (2D-DIGE) coupled with matrix-assisted laser desorption/ionization mass (MALDI TOF/TOF) spectrometry. We found that 108 proteins differed in abundance in spermatozoa between fresh and frozen semen. Most of these proteins was involved in pathways related to energy metabolism and protein quality control under stress conditions, reproductive processes and mechanisms of cell death/survival regulation, resulting in a significant decrease of motility and viability of post-thawing rabbit sperm and its potential fertilizing ability.
2022-10-14 | PXD034832 | Pride
Project description:In this study, we conducted a comprehensive quantitative phosphoproteomic analysis of mouse epididymal sperm from different regions (caput, corpus, and cauda) to unveil the dynamics of protein phosphorylation during sperm maturation. And we performed phosphoproteomic analysis of ALK inhibitor 2 compound 18-treated and control sperm to gain further insights into the potential mechanisms by which TSSK2 regulates sperm motility.
2024-10-17 | PXD049067 | Pride
Project description:Purpose: Sperm-borne RNA are particularly sensitive to degradation and methodology-induced bias, thus necessitating the use of a consistent, effective RNA extraction protocol for inter-species comparisons. To this end, we established SpermBase, an RNA expression database consisting of small and large RNA expression data obtained using consistent methodologies. Methods: Total RNA was extracted from total sperm and sperm head samples using an RNA extraction protocol that required only slight, species-specific alterations at the lysis stage. Total RNA was subjected to either RNA-Seq (large RNA) or sncRNA-Seq (small RNA). Results: By using a consistent methodology, we were able to perform a cross-species analysis on the conserved features of large and small sperm-borne RNAs. We identified conserved features in both populations of RNAs in the four mammalian species (i.e., mouse, rabbit, rat, and human) surveyed. Conclusions: Our study demonstrates an effective, near-universal approach to the study of sperm-borne RNAs, and identifies conserved characteristics in the large and small RNA populations of mammalian sperm.
2016-05-07 | GSE81216 | GEO
Project description:Cryoinjury and protein changes are a consequence of cryopreservation and may have a negative impact on sperm quality regarding motility, viability and fertilizing ability. However, potential proteomic changes in rabbit semen throughout the cryopreservation process have never been investigated previously. The aim of the present study was to compare the whole proteome of fresh and cryopreserved rabbit extracellular fluid of semen. Comparative analysis and identification of proteins were performed using 2-dimensional difference in-gel electrophoresis (2D-DIGE) coupled with matrix-assisted laser desorption/ionization mass (MALDI TOF/TOF) spectrometry. We found that 28 proteins differed in abundance between fresh and frozen extracellular fluid.
2022-10-13 | PXD034853 | Pride
Project description:Seminal plasma contributes to the safe environment for sperm maturation, sperm viability and fertilization in mammals (Kumar 2013). Moreover, seminal plasma is a promising source for the study of potential reproductive biomarkers, because it is a complex mixture of secretions from testis, epididymis and male accessory sex glands (González-Cadavid et al. 2014). The protein composition of mammalian seminal plasma varies among species, and has important effects on sperm function (Mortarino et al. 1998). In rabbits, seminal plasma has a positive effect in maintaining sperm motility and viability during in vitro storage (Castellini et al. 2000). To study proteins on a large scale, the application of a proteomic approach is mandatory (Dietrich 2014). Rabbit seminal plasma proteome has been proved different between rabbit genetic line A (maternal) and R (growth) (Viudes-de-Castro et al. (2004), Safaa et al. (2008), Casares-Crespo 2016) and between seasons (Casares-Crespo 2016). In these previous studies a traditional 1 dimension polyacrylamide gel was done, identifying only major proteins visible after Coomassie Colloidal Blue staining and obtaining the relative quantity of these protein bands. On the contrary, new approaches such as liquid chromatography in-gel or in-solution digestion coupled with mass spectrometric analysis are a powerful, yet relatively uncomplicated strategy to identify and characterize proteins. Mass spectrometry-based proteomics has become the tool of choice for identifying and quantifying the proteome of an organism (Karpievitch 2010). Therefore, the present study was conducted to describe the seminal plasma proteome of rabbits, compare the differentially expressed seminal plasma proteins between genetic lines A and R and study the effect of season in rabbit seminal plasma proteome.
2018-01-04 | PXD006308 | Pride
Project description:Our objective was to use quantitative phosphoproteomics for systematic comparative analyses of fresh versus frozen-thawed sperm to identify factors causing cryo-injury.
2023-12-28 | PXD048166 |