Comparative proteome analysis of egg yolk plasma proteins during storage

Гао, Дан; Qiu, Ning; Liu, Yaping; Ma, Meihu

doi:10.1002/jsfa.8052

Cited by 31 publications

(31 citation statements)

References 38 publications

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“…Ovalbumin is one of the most abundant proteins in egg yolk plasma ( Mann and Mann, 2008 ). Ovalbumin transports from egg white to yolk during long-time storage ( Gao et al., 2017 ). Only 1 protein spot was identified as ovalbumin with molecular weight of 39.3 kDa at 18 ED in this study.…”

Section: Discussionmentioning

confidence: 99%

“…Ovoinhibitor is a member of the Kazal family of protease inhibitors identified from egg white, which inhibits the activity of trypsin, chymotrypsin, subtilisin, elastase etc., serine proteases ( Oubre et al., 2003 ). Ovoinhibitor protein spots were detected in unfertilized egg white and egg yolk during storage and also in fertilized egg white during incubation ( Qiu et al., 2012 , Wang and Wu, 2014 , Gao et al., 2017 ). In this study, the MW of the identified ovoinhibitors was lower than their theoretical value suggested that the proteins degraded to keep the activity of serine protease which degrade macromolecular nutrients to support the growth and development of chicken embryo.…”

Section: Discussionmentioning

confidence: 99%

“…Using 3 combinatorial peptide ligand libraries, 255 unique proteins were identified in egg yolk plasma ( Farinazzo et al., 2009 ). Using 2-dimensional gel electrophoresis ( 2-DE ) combined with matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry ( MALDI-TOF MS/MS ) to study the changes of egg yolk protein during egg storage, Gao et al. (2017) identified 12 protein spots showed significant abundant changes.…”

Section: Introductionmentioning

confidence: 99%

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Proteomic analysis of fertilized egg yolk proteins during embryonic development

Zhu

Zhang

et al. 2020

Poultry Science

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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.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Proteomic analysis of fertilized egg yolk proteins during embryonic development

Zhu

Zhang

et al. 2020

Poultry Science

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“…Proteomic analysis is a powerful technique for investigating protein expression patterns, and has been used for chicken in several studies (Cao et al, 2012;Zhang et al, 2015;Desai et al, 2016;Gao et al, 2016;Li et al, 2016a,b). Skeletal muscle is an essential component of the animal body and its mass directly correlates with meat production (Güeller and Russell, 2010).…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development

et al. 2017

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Embryonic growth and development of skeletal muscle is a major determinant of muscle mass, and has a significant effect on meat production in chicken. To assess the protein expression profiles during embryonic skeletal muscle development, we performed a proteomics analysis using isobaric tags for relative and absolute quantification (iTRAQ) in leg muscle tissues of female Xinghua chicken at embryonic age (E) 11, E16, and 1-day post hatch (D1). We identified 3,240 proteins in chicken embryonic muscle and 491 of them were differentially expressed (fold change ≥ 1.5 or ≤ 0.666 and p < 0.05). There were 19 up- and 32 down-regulated proteins in E11 vs. E16 group, 238 up- and 227 down-regulated proteins in E11 vs. D1 group, and 13 up- and 5 down-regulated proteins in E16 vs. D1 group. Protein interaction network analyses indicated that these differentially expressed proteins were mainly involved in the pathway of protein synthesis, muscle contraction, and oxidative phosphorylation. Integrative analysis of proteome and our previous transcriptome data found 189 differentially expressed proteins that correlated with their mRNA level. The interactions between these proteins were also involved in muscle contraction and oxidative phosphorylation pathways. The lncRNA-protein interaction network found four proteins DMD, MYL3, TNNI2, and TNNT3 that are all involved in muscle contraction and may be lncRNA regulated. These results provide several candidate genes for further investigation into the molecular mechanisms of chicken embryonic muscle development, and enable us to better understanding their regulation networks and biochemical pathways.

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“…[5] Comparative proteomics offers the possibility to analyze the differential expression patterns of all proteins in the same tissue at specific times and under specific environmental conditions. Several studies of chicken egg yolk proteome [6,7] and comparative proteomics analyses [2,8,9] have profiled its protein patterns in different states. The egg yolk protein profile compared to other poultry species remains unknown.…”

Section: Introductionmentioning

confidence: 99%

Comparative proteomic analysis of chicken, duck, and quail egg yolks

Liu

Qiu

Гао

et al. 2018

International Journal of Food Properties

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A comparative analysis of egg yolk proteome of three major poultry species, namely, chicken, duck, and quail, was carried out with two-dimensional (2D) gel electrophoresis patterns and matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry. Proteins identified from these three poultry species shared high degrees of sequence and structure homology, which might be related to the bird's adaptability under different environmental stresses. Few specific proteins were found in this study. Comparative 2D gel electrophoresis patterns of chicken, duck, and quail revealed that some protein-specific regions on gels could be used for authentic identification of poultry eggs. These findings could provide a fundamental understanding of different poultry egg protein profiles and showed us some new sights in egg yolk nutrients related to certain properties and functions.ARTICLE HISTORY

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Comparative proteome analysis of egg yolk plasma proteins during storage

Cited by 31 publications

References 38 publications

Proteomic analysis of fertilized egg yolk proteins during embryonic development

Proteomic analysis of fertilized egg yolk proteins during embryonic development

Proteomic Analysis of Chicken Skeletal Muscle during Embryonic Development

Comparative proteomic analysis of chicken, duck, and quail egg yolks

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