Integrated proteomic, phosphoproteomic and N-glycoproteomic analyses of chicken eggshell matrix. (15th November 2020)

• Record Type: Journal Article
• Authors: Yang, Ran; Geng, Fang; Huang, Xiang; Qiu, Ning; Li, Shugang; Teng, Hui; Chen, Lei; Song, Hongbo; Huang, Qun
• Is Part Of: Food chemistry. Volume 330(2020)
• Publication Date: 2020-11-15
• Subjects: Eggshell matrix -- Proteome -- Phosphorylation -- N-Glycoprotein; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2020.127167
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The proteome of chicken eggshell matrix is analyzed, including modified proteins. A total of 112 phosphorylation sites and 297 N -glycosylation sites were identified. A total of 676 matrix proteins were identified, including 251 modified proteins. Eggshell matrix proteins were mainly enriched in regulation of enzyme activity. Abstract: Eggshell matrix (EM) proteins play an important biological role in eggshell mineralization and embryo development. Many studies have demonstrated that some matrix proteins undergo posttranslational modifications, including phosphorylation and glycosylation, which have important regulatory effects on the functional properties of the proteins. Systematic analysis of the proteome, the phosphorylated modified proteome and the glycosylated modified proteome of the chicken EM was performed using a proteomics strategy. A total of 112 phosphorylation sites from 69 phosphoproteins and 297 N -glycosylation sites from 182 N -glycoproteins were identified in the chicken EM. Among all these identified modified proteins, 129 were not identified in the proteome (547 proteins). Therefore, a total of 676 EM proteins were identified in this study. Gene ontology (GO) enrichment analysis indicated that EM proteins and phosphoproteins were mainly enriched in regulation of enzyme activity, while EM N -glycoproteins were enriched in immune response regulation.