Quantitative phosphoproteomic analysis of fertilized egg derived from Tibetan and lowland chickens

Liu, Yaping; Qiu, Ning; Geng, Fang; Sun, Haohao; Wang, Hong; Meng, Yaqi

doi:10.1016/j.ijbiomac.2020.01.211

Cited by 10 publications

(9 citation statements)

References 48 publications

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“…We also detected seven phosphosites (S102, S103, S35, S279, S157, S283, and S480) of VTG2 in the active domain (vitellogenin‐N domain) that contained active sites showing lipid transport activity 37 . The study showed that the higher number of phosphosites found in the active domain might increase the lipid transport activity in DEY 38 . In addition, phosphorylation of phosvitin (major cleaved products of VTG) enhanced the metal‐binding ability and bone‐growth development 49 .…”

Section: Discussionmentioning

confidence: 71%

“…Compared with CEY, only three phosphosites (S269, S279, and S470) (Geng F, 2021, unpublished data) were found in this domain. The higher number of phosphosites found in the active domain might increase the lipid transport activity in DEY 38 . Thus, it could be speculated that DEY phosphoproteins show a stronger binding ability to lipids, metal ions, etc., indicating that they can facilitate the embryonic development process and be more suitable as food‐embedding materials, carrying and transporting lipids and minerals to meet human health needs.…”

Section: Discussionmentioning

confidence: 99%

“…37 The study showed that the higher number of phosphosites found in the active domain might increase the lipid transport activity in DEY. 38 In addition, phosphorylation of phosvitin (major cleaved products of VTG) enhanced the metalbinding ability and bone-growth development. 49 Phosphoproteins were also reported to play a potential role in egg activation and initiation of embryogenesis.…”

Section: Metabolic Process-related Phosphoproteins In Deymentioning

confidence: 99%

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Phosphoproteomic analysis of duck egg yolk provides novel insights into its characteristics and biofunctions

et al. 2021

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BACKGROUND: Although the importance of phosphorylation in the function of proteins is known, investigation of the protein phosphorylation of duck egg yolk (DEY) is still very limited. This study aimed to conduct a detailed phosphoproteomic study of DEY using immobilized metal affinity chromatography and ultra-high liquid chromatography tandem mass spectrometry.RESULTS: A total of 253 phosphorylation sites assigned to 66 phosphoproteins were identified in DEY, of which VTG-1, VTG-2, and fibrinogen alpha chain were found to be the highly phosphorylated proteins in DEY. The biological functions of the identified phosphoproteins were illuminated through gene ontology analysis, which showed that they were mainly involved in binding, catalytic, immune response, and metabolic activity. S-X-E and S-X-S were found to be the most conserved serine motifs of phosphorylation in DEY. The comparison of DEY phosphoproteins with those of chicken egg yolk (CEY) revealed that differences mostly involved molecular functions and biological processes. The comparison also revealed a higher phosphorylation level in DEY proteins.CONCLUSION: The higher phosphorylation level in DEY proteins than that in CEY proteins are supposed to help enhance duck growth performance and biological activities (e.g. antibacterial and antioxidant ability) for better adapting the humid environment the duck lived.

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Section: Discussionmentioning

confidence: 71%

Section: Discussionmentioning

confidence: 99%

Section: Metabolic Process-related Phosphoproteins In Deymentioning

confidence: 99%

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Phosphoproteomic analysis of duck egg yolk provides novel insights into its characteristics and biofunctions

et al. 2021

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“…Peptides were selected for MS/MS, and the fragments were detected at a resolution of 17 500. A data-dependent procedure was applied, which alternated between one MS scan followed by 20 MS/MS scans with a 15 s dynamic exclusion. − …”

Section: Methodsmentioning

confidence: 99%

A Comprehensive Identification of Chicken Egg White Phosphoproteomics Based on a Novel Digestion Approach

Sun

Jin

Sun

et al. 2020

J. Agric. Food Chem.

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There are plenty of phosphoproteins in chicken egg white (CEW), which are of great significance for the biological activity and function of CEW. In this study, phosphorylated proteins in CEW were identified and analyzed based on two digestion strategies (trypsin and trypsin/glutamyl endoproteinase). Besides, the enrichment strategy of immobilized metal affinity chromatography was used, and phosphopeptides were identified by nano liquid chromatography/tandem mass spectrometry. A total of 189 phosphosites mapped onto 166 phosphopeptides corresponding to 96 phosphoproteins were identified. Gene ontology analysis suggested that these phosphoproteins of CEW mainly participated in biological processes such as "cell process", "biological regulation", and "response to stimulus". Moreover, the phosphoproteins of CEW were involved in molecular functions, primarily including "binding" and "catalytic activity". On the basis of the available literature, the research was the first comprehensive identification of chicken egg white phosphoproteins. This study further enriched the identification of phosphoproteins in CEW and laid a foundation for the subsequent study of phosphoproteins.

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“…Moreover, the dephosphorylation process of vitellogenin may be triggered by temperature-regulated phosphatases, allowing for the supply of a lot of phosphate groups for the synthesis of nucleotides and nucleic acids as well as supporting energy metabolism in the developing embryo . In the research by Liu et al, the phosphoproteins of Tibetan chicken eggs possess antibacterial, emulsifying, and antioxidative properties . In the N-glycoproteomic study, a total of 334 unique N -glycopeptides from 153 N -glycoproteins were identified and 82 N -glycopeptides showed some significant changes after 12 days of embryo development.…”

Section: Egg Omics During Embryonic Developmentmentioning

confidence: 99%

Omics as a Window To Unravel the Dynamic Changes of Egg Components during Chicken Embryonic Development

Meng

Qiu

Guyonnet³

et al. 2021

J. Agric. Food Chem.

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Chicken egg, as a completely aseptic and self-sufficient biological entity, contains all of the components required for embryonic development. As such, it constitutes not only an excellent model to study the mechanisms of early embryo nutrition and disease origin but can also be used to develop egg-based products with specific applications. Different omics disciplines, like transcriptomics, proteomics, and metabolomics, represent promising approaches to assess nutritional and functional molecules in eggs under development. However, these individual molecules do not act in isolation during the dynamic embryogenic process (e.g., migration, transportation, and absorption). Unless we integrate the information from all of these omics disciplines, there will remain an unbridged gap in the systematic and holistic assessment of the information from one omics level to the other. This integrative review of the dynamic molecular processes of the different chicken egg components involved in embryo development describes the critical interplay between the egg components and their implications in immunity, hematopoiesis, organ formation, and nutrient transport functions during the embryonic process.

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Quantitative phosphoproteomic analysis of fertilized egg derived from Tibetan and lowland chickens

Cited by 10 publications

References 48 publications

Phosphoproteomic analysis of duck egg yolk provides novel insights into its characteristics and biofunctions

Phosphoproteomic analysis of duck egg yolk provides novel insights into its characteristics and biofunctions

A Comprehensive Identification of Chicken Egg White Phosphoproteomics Based on a Novel Digestion Approach

Omics as a Window To Unravel the Dynamic Changes of Egg Components during Chicken Embryonic Development

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