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Proteomic analysis of fertilized egg yolk proteins during embryonic development.

ABSTRACT: Egg yolk is an important source of nutrients for embryo development. In this study, the egg yolk protein composition at 0, 10, and 18 D of incubation was analyzed by 2-dimensional gel electrophoresis (2-DE) combined with matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry. A significant difference in the abundance of 42 protein spots representing 12 proteins were identified (P < 0.05). The 2-DE gel image analysis exhibited that the molecular weight (MW) of 29 protein spots was lower than their theoretical value, in which 14 vitellogenin (VTG) fragments were lower than the theoretical value. There were 13 protein spots showed a higher MW including 5 ovotransferrins with MW of 87.2 kDa. The gene ontology enrichment analysis suggested that biological process of the differentially expressed proteins were mainly involved in lipid transport and lipid localization at 10 and 18 D of incubation. The molecular function of the differentially expressed proteins was involved in nutrient reservoir activity, lipid transporter activity, and antigen binding at 10 D of incubation. At 18 D of incubation, the differentially expressed proteins mainly participated in nutrient reservoir activity and substrate-specific transporter activity. The high abundance of VTGs at 10 D of incubation might participate in lipid localization and lipid transportation to facilitate the yolk nutrient transport to embryo. The low expression of ovotransferrins at 10 D of incubation indicated the chondrogenesis of embryo.

SUBMITTER: Zhu W

PROVIDER: S-EPMC7597458 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

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Proteomic analysis of fertilized egg yolk proteins during embryonic development.

Zhu Wenjun W Zhang Junzhi J He Kaiqin K Geng Zhaoyu Z Chen Xingyong X

Poultry science 20200311 5

Egg yolk is an important source of nutrients for embryo development. In this study, the egg yolk protein composition at 0, 10, and 18 D of incubation was analyzed by 2-dimensional gel electrophoresis (2-DE) combined with matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry. A significant difference in the abundance of 42 protein spots representing 12 proteins were identified (P < 0.05). The 2-DE gel image analysis exhibited that the molecular weight (MW) of 29 prot ...[more]

PMID: 32359615

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Project description:The yolk is the principal part of the egg that contains vitamins, minerals, lipids, and proteins which are essential for embryo development and hatching. The egg yolk contains significant amounts of lipoproteins, triacylglycerides, and cholesterol, whose dynamics are indistinct during embryogenesis. The effects of cholesterol on the yolk protein abundance, intensity, and function are ill-defined during embryonic development. Using two-dimensional gel electrophoresis, eggs with respective high and low cholesterol protein abundance were investigated after 0, 2, 6, and 13 days of embryogenesis and further analyzed by matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry. The results revealed that the vitellogenin proteins are the most abundant egg yolk protein that showed proximity and a high degree of variation in isoelectric point and molecular weight. The results demonstrated increased expression of vitellogenin-1 and vitellogenin-3 at two days and vitellogenin-2 protein at 13 days of embryogenesis in both egg types. The ovoinhibitor, immunoglobulin lambda light chain precursor, Ig-gamma (clone-36 chicken), and beta-2-glycoprotein-1 precursor proteins were significantly expressed in high cholesterol eggs while haptoglobin protein PIT-54 and vitelline membrane outer layer proteins intensities were significant in low cholesterol eggs at two days of embryogenesis. The high cholesterol eggs showed a modest increase in egg weight, yolk weight, albumen height, yolk color, and egg strength relative to the low cholesterol eggs. The gene ontology enrichment analysis revealed that the differentially expressed proteins such as vitellogenin proteins were involved in lipid transport and lipid localization biological processes and showed nutrient reservoir activity function. The ovotransferrin regulated the biological processes of plasminogen activation and extracellular matrix disassembly and characterized the anchored component of the plasma membrane. The ovoinhibitor protein was involved in response to mineralocorticoid and corticosterone biological processes whereas the vitellin membrane outer layer protein constituted the extracellular exosome, extracellular organelle, and membrane-bounded vesicle cellular components. Collectively, our study revealed yolk protein abundance, molecular function, cellular components, and biological processes and concluded that yolk protein intensities were significantly altered by cholesterol concentration.

Project description:The chicken egg yolk, which is abundant with lipids, proteins, and minerals, is the major nutrient resource for the embryonic development. In fact, the magnitude and type of yolk nutrients are dynamically changed during the chicken embryogenesis to meet the developmental and nutritional requests at different stages. The yolk nutrients are metabolized and absorbed by the yolk sac membrane and then used by the embryo or other extraembryonic tissues. Thus, understanding the metabolites in the yolk helps to unveil the developmental nutritional requirements for the chicken embryo. In this study, we performed ultra high performance liquid chromatography/tandem mass spectrometry (UHPLC-MS/MS) analysis to investigate the change of metabolites in the egg yolk at embryonic (E) 07, E09, E11, E15, E17, and E19. The results showed that 1) the egg yolk metabolites at E07 and E09 were approximately similar, but E09, E11, E15, E17, and E19 were different from each other, indicating the developmental and metabolic change of the egg yolk; and 2) most of the metabolites were annotated in amino acid metabolism pathways from E11 to E15 and E17 to E19. Especially, arginine, lysine, cysteine, and histidine were continuously increased during the embryonic development, probably because of their effects on the growth promotion and oxidative stress amelioration of the embryo. Interestingly, the ferroptosis was found as one of major processes occurred from E15 to E17 and E17 to E19. Owing to the upregulated expression of acyl-CoA synthetase long-chain family member 4 detected in the yolk sac, we assumed that the ferroptosis of the yolk sac was perhaps caused by the accumulation of reactive oxygen species, which was induced by the large amount of polyunsaturated fatty acids and influx of iron in the yolk. Our findings might offer a novel understanding of embryonic nutrition of broilers according to the developmental changes of metabolites in the egg yolk and may provide new ideas to improve the health and nutrition for prehatch broiler chickens.

Project description:Rabbit embryonic stem (rES) cells can be derived from various sources of embryos. However, understanding of the gene expression profile, which distincts embryonic stem (ES) cells from other cell types, is still extremely limited. In this study, we compared the protein profiles of three independent lines of rabbit cells, i.e., fibroblasts, fertilized embryo-derived stem (f-rES) cells, and parthenote-derived ES (p-rES) cells. Proteomic analyses were performed using two-dimensional gel electrophoresis (2-DE) and mass spectrometry. Collectively, the expression levels of 100 out of 284 protein spots differed significantly among these three cell types (p<0.05). Of those differentially expressed spots, 91% were identified in the protein database and represented 63 distinct proteins. Proteins with known identities are mainly localized in the cytoplasmic compartments (48%), nucleus (14%), and cytoskeletal machineries (13%). These proteins were majorly involved in biological functions of energy and metabolic pathways (25%), cell growth and maintenance (25%), signal transduction (14%), and protein metabolisms (10%). When protein expression levels among cell types were compared, six proteins associated with a variety of cellular activities, including structural constituents of the cytoskeleton (tubulins), structural molecule (KRT8), catalytic molecules (?-enolase), receptor complex scaffold (14-3-3 protein sigma), microfilament motor proteins (Myosin-9), and heat shock protein (HSP60), were found highly expressed in p-rES cells. Two proteins related to HSP activity and structural constituent of cytoskeleton in f-rES cells, and one structural molecule activity protein in fibroblasts showed significantly higher expression levels (p<0.05). Marker protein expressions in f-rES and p-rES cells were further confirmed by Western blotting and immunocytochemical staining. This study demonstrated unique proteomic profiles of the three rabbit cell types and revealed some novel proteins differentially expressed between f-rES and p-rES cells. These analyses provide insights into rES cell biology and would invite more in-depth studies toward rES cell applications.

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Proteomic analysis of fertilized egg yolk proteins during embryonic development.

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Proteomic analysis of fertilized egg yolk proteins during embryonic development.

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