A critical review on inflammatory bowel diseases risk factors, dietary nutrients regulation and protective pathways based on gut microbiota during recent 5 years.

The treatment of inflammatory bowel diseases (IBDs) has become a worldwide problem. Intestinal flora plays an important role in the development and progression of IBDs. Various risk factors (psychology, living habits, dietary patterns, environment) influence the structure and composition of the gut microbiota and contribute to the susceptibility to IBDs. This review aims to provide a comprehensive overview on risk factors regulating intestinal microenvironment which was contributed to IBDs. Five protective pathways related to intestinal flora were also discussed. We hope to provide systemic and comprehensive insights of IBDs treatment and to offer theoretical guidance for personalized patients with precision nutrition.

Capsaicin: A Novel Approach to the Treatment of Functional Dyspepsia.

Capsaicin, the principal spicy component of red pepper, shows numerous bioactivities these years. Based on the results of past studies, capsaicin may have potential effects on the treatment of functional dyspepsia (FD). However, most studies mainly investigate functional dyspepsia-treatment effects of capsaicin by discussing the relationship between capsaicin and transient receptor potential vanilloid type 1 (TRPV1). In fact, capsaicin may relieve the symptoms of FD in various ways. These effects involve desensitizing C nociceptive fibers, regulating kinds of neurotransmitters, counteracting viruses and inflammation, balancing the gut microbiota, inhibiting the secretion of gastric acid, and reducing oxidative stress damage. A full understanding of these mechanisms will help further development and utilization of capsaicin in food and medical fields.

Unveiling and application of the chicken egg proteome: An overview on a two-decade achievement.

Egg proteins are not only the most complete and ideal form of protein for human or embryo nutrition but also play the vital role in the food industry. Egg proteins are subjected to many potential changes under various conditions, which may further alter the nutritional value, physicochemical-properties, and bioactivities of proteins. Recent advances in our understanding of the proteome of raw egg matrix from different species and dynamic changes occurring during storage and incubation are developing rapidly. This review provides a comprehensive overview of the main characteristics of chicken egg proteome, covering all its components and applications under various conditions, such as markers detection, egg quality evaluation, genetic and biological unknown identification, and embryonic nutritional supplementation, which not only contributes to our in-depth understanding of each constituent functionality of proteome, but also provides information to increase the value to egg industry.

UHPLC-Q-Orbitrap-based untargeted lipidomics reveals the variation of yolk lipids during egg storage.

BACKGROUND: Egg yolk is recognized for its excellent nutritional benefit and economic value; however, egg is a perishable food, potentially losing quality if not handled properly between the time from farm production to consumption. Knowledge of the changes of yolk lipid composition under an extreme storage condition close to vitelline membrane breaking, which results in an inedible condition for shelf-eggs, remains incomplete. Considering the complexity of yolk lipids, the architectural features of yolk lipids at high-temperature storage (30°C for 10 days versus fresh) were classified through lipidomics. RESULTS: This strategy yielded 1508 features within the lipid database coupled with 74 significantly different lipids (P < 0.05, fold change > 1.2 or < 0.83), mainly triglycerides, phospholipids, and sphingolipids. Most of them were decreased after storage; for example, triglycerides were assumed to play a role as a 'buffer' to maintain the system stability during storage by balancing fatty acid saturation, which strongly reduces the egg edible value for humans. Furthermore, phospholipids, especially the highly unsaturated phosphatidylcholine, decreased significantly and were suggested to be the primary cause for the variation in yolk emulsifying properties and flavor. CONCLUSION: Altogether, these results deriving from oxidation and lipolysis reactions enhance our understanding of lipid transformation and the biochemical mechanisms, at the molecular level, of the deteriorative process of the egg yolk. These findings may lay the foundation for identifying processes, including some modifications of the lipid composition of rations fed to laying hens, aiming to improve the long-term shelf-stability of shell eggs and egg products. © 2022 Society of Chemical Industry.

Comparative N-glycoproteomic analysis of Tibetan and lowland chicken fertilized eggs: Implications on proteins biofunction and species evolution.

The characterization and functionality of protein glycosylation among different related species are of common interest. Herein, non-standard quantification and N-glycosylation enrichment technology combined with ultra-high liquid chromatography-tandem mass spectrometry were used to establish detailed N-glycoproteomics of fertilized eggs, and quantitatively compared between Tibetan and lowland chicken. A total of 396N-glycosites from 143 glycoproteins were found. Specifically, compared with lowland chicken egg white, 32N-glycosites of 22 glycoproteins were up-regulated and 57N-glycosites of 25 glycoproteins were down-regulated in Tibetan chicken egg white. Also, 137N-glycosites in 72 glycoproteins showed much higher-degree glycosylation and 36N-glycosites in 15 glycoproteins displayed lower-degree glycosylation in Tibetan chicken egg yolk than those in lowland chicken egg yolk. Through bioinformatic analysis, these varied glycoproteins were highly associated with antifreeze activity, hypoxia adaptation, coagulation cascade, and binding/immunity activities, which may be related to plateau hypoxia and cold stress. PRACTICAL APPLICATIONS: These findings provide a new insight on the role of biological egg N-glycoproteins related to environmental adaptation and evolution, which may be further applied in improving egg processing and human health, by developing biomolecules for food and medical industry.

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

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. © 2021 Society of Chemical Industry.

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

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.

Design, synthesis and antitumor activity evaluation of trifluoromethyl-substituted pyrimidine derivatives.

In order to find efficient new antitumor drugs, a series of novel trifluoromethyl-substituted pyrimidine derivatives were designed and synthesized, and the bioactivity against four human tumor cells (PC-3, MGC-803, MCF-7 and H1975) was evaluated by MTT assay. Compound 17v displayed potent anti-proliferative activity on H1975 (IC50 = 2.27 µΜ), which was better than the positive control 5-FU (IC50 = 9.37 µΜ). Further biological evaluation studies showed that compound 17v induced apoptosis of H1975 cells and arrested the cell cycle at G2/M phase. Furthermore, compound 17v induced H1975 cells apoptosis through increasing the expression of pro-apoptotic proteins Bax and p53 and down-regulating the anti-apoptotic protein Bcl-2. In addition, compound 17v was able to be tightly embedded in the active pocket of EGFR. In summary, these results demonstrated that compound 17v has a potential as a lead compound for further investigation.

Comparative Lipidomics of Chick Yolk Sac during the Embryogenesis Provides Insight into Understanding the Development-Related Lipid Supply.

Yolk sac (YS, include the yolk content) at different chick embryogenesis stages possesses varying lipid distributions, which are nutrition-influencing factors for the health of an early embryo and a later adult. YS lipids can substantially influence embryogenesis metabolism, but a comprehensive understanding of lipid's influence remains unknown. Herein, the effects of embryogenesis on lipid profiling of chick YS were investigated by UHPLC-MS/MS-based lipidomics. A total of 2231 lipid species across 57 subclasses were identified in the YS, and 1011 lipids were significantly different (P < 0.05) at the incubation days of 0, 7, 13, and 18. Specifically, phosphocholine and phosphatidylglycerol in late-stage embryogenesis potentially assist with prehatching gas exchange and infection resistance in the environment after lung respiration. In addition, the accumulated lysophosphatidylcholine at day 18 may induce apoptosis and disturb the membrane structure of YS to enable better absorption by the embryo abdomen. The decreased cardiolipin in late embryogenesis may be due to transportation to the embryo and integration into the mitochondrial membrane to accelerate energy metabolism for the rapidly developing embryo after day 13. Therefore, this study demonstrated the lipid profile alteration of the developing YS, providing theoretical guidance for researching the developmental origins of health and disease.

Comparative N-Glycoproteomic Analysis Provides Novel Insights into the Deterioration Mechanisms in Chicken Egg Vitelline Membrane during High-Temperature Storage.

The weakening of chicken egg vitelline membrane (CEVM) is one of the most important factors influencing egg quality during high-temperature storage. Therefore, a comparative N-glycoproteomic analysis of CEVM after 10 days of storage at 30 °C was performed to explore the roles of protein N-glycosylation in membrane deterioration. In total, 399 N-glycosites corresponding to 198 proteins were identified, of which 46 N-glycosites from 30 proteins were significantly altered. Gene ontology analysis revealed that these differentially N-glycosylated proteins (DGPs) were involved in antibacterial activity, glycosaminoglycan binding, lipid binding, and aminopeptidase activity. Removal of the N-glycans in Mucin-5B may result in a loss of CEVM's mechanical properties. The N-glycosites enriched in the apolipoprotein B ß2 domain in CEVM were significantly changed, which may contribute to lipid composition modifications during storage. Moreover, N-glycosites in several metalloproteases were located within the functional domain or active site region, indicating that the decreased N-glycosylation levels may affect their structural stability, specific substrate binding, or enzyme activity. These findings provide novel insights into the roles of protein N-glycosylation during membrane weakening.

Epithelial expression and role of secreted STC1 on asthma airway hyperresponsiveness through calcium channel modulation.

BACKGROUND: Asthma is characterized by airway hyperresponsiveness (AHR), inflammation, and airway remodeling. Airway hyperresponsiveness results from enhanced airway smooth muscle (ASM) contraction potentially under the control of an epithelium-derived relaxing factor (EpDRF). However, relatively rare is known about EpDRF. We aimed to elucidate the role of epithelium-derived stanniocalcin-1 (STC1) on AHR and ASM contraction. METHODS: Stanniocalcin-1 levels in the serum of asthmatic patients and healthy volunteers and in bronchoalveolar lavage fluid (BALF) from ovalbumin (OVA)-challenged mice were measured by ELISA. The effects of exogenous STC1 on AHR and on inflammation were examined in mice. IL-13 modulation of STC1 mRNA and protein levels was studied in human bronchial epithelial cell lines (16HBE). The function of STC1 on Ca2+ influx and ASM contraction was examined ex vivo. RESULTS: Serum STC1 was decreased in asthma (n = 93) compared with healthy volunteers (1071 ± 30.4 vs 1414 ± 75.1 pg/ml, p < 0.0001, n = 23) and correlated with asthma control (p = 0.0270), lung function (FEV1, p = 0.0130), and serum IL-13 levels (p = 0.0009). Treatment of ten asthmatic subjects with inhaled corticosteroids/long-acting beta2-agonists (ICS/LABA) for 1 year enhanced STC1 expression which correlated with improved asthma control (p = 0.022). STC1 was mainly expressed in bronchial epithelium and intranasal administration of recombinant human STC1 (rhSTC1) reduced AHR and inflammation in mice. IL-13 suppressed STC1 release from 16HBE, whereas rhSTC1 blocked store-operated Ca2+ entry (SOCE) by suppressing stromal interaction molecule 1 (STIM1) and further inhibited ASM cell contractility by suppressing Ca2+ -dependent myosin light chain (MLC) phosphorylation. CONCLUSION: Our data indicate that STC1 deficiency in asthmatic airways promotes STIM1 hyperactivity, enhanced ASM contraction, and AHR. STC1 may be a candidate EpDRF.

Quantitative Comparative Proteomic Analysis of Chicken Egg Vitelline Membrane Proteins during High-Temperature Storage.

To explore the thermally induced alterations in chicken egg vitelline membrane (CEVM) protein abundances, a comparative proteomic analysis of CEVM after 10 days of storage at 30 °C was performed. Altogether, 981 proteins were identified, of which 124 protein abundances were decreased and 79 were increased. Bioinformatic analysis suggested that the altered proteins were related to structure (n = 10), mechanical properties (n = 13), chaperone (n = 15), antibacterial (n = 12), and antioxidant (n = 3). Alterations in abundances of structural proteins, possibly resulting from the disintegration of these complexes, were observed in this study, suggesting a loss in fibrous structure. Several proteins involved in mechanical strength (n = 10), elasticity (n = 3), and chaperone were decreased in abundances, which indicated that deficits in these proteins might affect the CEVM mechanical properties. These findings will extend our understanding of CEVM deterioration during high-temperature storage from a proteomic perspective.

Phosphoproteomic analysis of duck egg white and insight into the biological functions of identified phosphoproteins.

Phosphorylation of proteins is one of the most important and pleiotropic modifications. It plays a vital role in controlling protein functions. However, the phosphoproteome of duck egg white (DEW) has not been studied yet. To investigate the role of phosphorylation on DEW proteins, a detailed phosphoproteome analysis of DEW was performed using an immobilized metal affinity chromatography enrichment strategy. A total of 92 phosphosites representing 36 phosphoproteins were identified. [S-x-E] and [T-x-E] were found to be the most overrepresented motifs in DEW. The identified phosphoproteins in DEW were mainly involved in the binding, transport activity, biological regulation, and metabolic processes. Gene ontology analysis was used to elucidate the biological functions of DEW phosphoproteins and compare them with those of chicken egg white (CEW), which showed the differences mostly involved molecular functions and biological processes. PRACTICAL APPLICATIONS: These findings provide fundamental insight into the biological functions of identified phosphoproteins of DEW to better understand the roles of phosphorylated DEW proteins for food industries and human health. Phosphoproteomic study of DEW would be valuable for the food and nutrition industry to exploit the potential of this avian proteins in the processing of health benefit products.

Modulation of gut microbiota in rats fed whole egg diets by processing duck egg to preserved egg.

Pidan, as the preserved duck egg, is a traditional alkaline-pickled food in China. Previous studies have suggested preserved egg white has an anti-inflammatory effect, though the mechanism of action was unclear. In this work, the difference of peptides distribution in the digestive products was identified from those of duck egg. The effects of preserved egg diet on the modulation of gut microbiota as well as the alteration in fecal metabolites were further investigated. Minor variations of gut microbiota in phylum level were observed between preserved and fresh duck egg diet groups, even though, preserved egg diet intake attributed to increases in the relative abundance of Prevotella and Phascolarctobacterium (p < 0.05), while Ruminococcaceae and Allobaculum were quantitatively decreased (p < 0.05). In terms of metabolites, the contents of acetic acid (p < 0.01) and propionic acid (p < 0.05) were significantly increased in the preserved egg diet group. It was speculated that the preserved egg diet might alter the proportion of short-chain fatty acids (SCFAs) in the gut of rats by modulating specific intestinal bacteria, and subsequently play an active role in anti-inflammatory effects. Compared to the fresh egg group, the bacterial produced SCFAs of preserved egg group were increased in abundance (p < 0.05), which may have potential anti-obesity and anti-inflammatory effects. The results provide a novel insight into the relationship between preserved egg intake, gut microbiota and potential positive effects on host health.

A comparative study of the modulation of the gut microbiota in rats by dietary intervention with different sources of egg-white proteins.

BACKGROUND: Gut microflora dysbiosis has been related closely to a variety of diseases including obesity and inflammatory bowel disease. Proteins and peptides in egg white have been found to alleviate inflammation but the role played by the intestinal flora is still unclear. Using casein as a dietary protein control, we investigated the effects of diets composed of hen egg white, duck egg white, and preserved egg white on gut microbiota in the rat cecum. RESULTS: The gut microbiota in rats were altered after egg-white consumption. The results showed that rats fed with egg white had a similar overall structure of cecal bacterial communities, which was different from those fed with casein. The relative abundance of Akkermansia in the group of rats fed with hen egg white was highest among all groups. Rats fed with duck egg white had significantly higher relative abundance of Proteobacteria and Peptostreptococcaceae, and lower relative abundance of Lachnospiraceae. In addition, the levels of lipopolysaccharide (LPS) and lipopolysaccharide-binding protein (LBP) in rats fed with duck egg white and preserved egg white were lower than the levels in rats fed with hen egg white. CONCLUSION: Our results indicated the possible positive effect on homeostasis of the intestinal flora brought about by the intake of duck egg white. This study provides an insight into the potential positive impact of preserved egg white on health by changing gut microbiota and affecting the antigen load. © 2020 Society of Chemical Industry.

N-glycoproteomic analysis of duck egg yolk proteins: Implications for biofunctions and evolution.

Egg yolk contains multifunctional glycoproteins, which modulate embryogenesis and indicate species-specific adaptation. Here, we conducted an N-glycoproteomic study of duck egg yolk (DEY) and identified 359 N-glycosites corresponding to 113 glycoproteins. The comparison of DEY N-glycoproteins with those of chicken egg yolk (CEY) revealed a higher N-glycosylation level in DEY proteins, suggesting a biological adaption to meet the requirements for embryo development by modulating protein structure and binding ability, including immune response and ligand transport. This variation may be correlated to the strong resistance to the influenza virus disease of duck. A large set of corresponding glycoproteins between DEY and CEY were detected with similar molecular functions, which suggested a relatively lower evolution speed of avian egg yolk proteins than that of egg white proteins.

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

In this study, immobilized metal affinity chromatography and ultra-high liquid chromatography tandem mass spectrometry were used to establish detailed phosphoproteomes of fertilized egg, and further quantitative compared those from Tibetan chicken and lowland chicken. A total of 138 phosphosites from 42 phosphoproteins were identified. Specifically, 103 phosphosites representing 41 phosphoproteins were detected in Tibetan chicken egg, and 125 sites in 40 phosphoproteins were found in lowland chicken egg; 47 phosphosites in 26 phosphoproteins were found in fertilized egg white, while 109 phosphosites in 24 phosphoproteins were identified in fertilized egg yolk. Thirty-one phosphoproteins carrying 83 phosphosites (12 phosphosites from 10 phosphoproteins in egg white and 52 sites from 17 proteins in egg yolk) showed significantly different phosphorylation between Tibetan and lowland chicken eggs, which were mainly involved in binding, catalysis, allergenic and cryoprotectant activities. Besides, several amino acid polymorphisms in ovalbumin and vittelligion-2 were detected, which might alter 3D structures and biofunctions. Our data recorded the egg phosphoprotein abundances and biological activities of two chicken species. These results provide a solid foundation to better understand the egg phosphoprotein characteristics, especially to explore the impacts of cross-species alteration of phosphorylation status on the structure, function and nutritional properties.

Quantitative Comparative Integrated Proteomic and Phosphoproteomic Analysis of Chicken Egg Yolk Proteins under Diverse Storage Temperatures.

To investigate the alterations of egg yolk protein abundances and their phosphorylation status at different storage temperatures, a comparative quantitative study of unfertilized chicken egg yolk after 15 days of storage at 4 and 37 °C was performed. Altogether, 445 proteins were identified in our study, of which the abundances of 154 proteins were significantly changed when comparing high-temperature storage with low-temperature storage, including 42 up-regulated and 112 down-regulated proteins. In the phosphoproteome, we identified a total of 137 phosphorylated sites on 326 peptides corresponding to 51 proteins. The results showed that the degree of phosphorylation for most egg yolk proteins was enhanced during high-temperature storage. Furthermore, GO analysis indicated that these phosphoproteins of egg yolk may be closely related to the binding, catalysis, and transport functions. The results provide further insights into the effect of storage temperature on egg proteome changes and their phosphorylation level. Moreover, this study can provide a theoretical basis for the improvement of egg quality during storage by phosphorylation modification in the food industry.

Comparative proteomic analysis of hen egg yolk plasma proteins during embryonic development.

Avian egg yolk provides essential nutrients and physiological support for the developing embryo. To reveal the dynamics of yolk proteins during the entire period of incubation, we analyzed the alterations of egg yolk plasma proteins at different times during incubation (day 0, 7, 14, and 18). Day 14 (D14) of incubation was considered as the key point on the alteration of egg yolk proteins according to the SDS-PAGE analysis. The two-dimensional electrophoresis-based comparative proteomic analysis was conducted, and 26 spots representing 13 proteins were detected with significant changes in abundance. An accelerating transfer of ovalbumin from egg white into egg yolk was observed at D14 in fertilized eggs but not detected in unfertilized eggs, indicating an unrevealed absorbing pathway for the egg proteins/peptides particularly in fertilized eggs. Meanwhile, the abundance of yolk riboflavin-binding protein constantly decreased after D14, which might meet the need for essential riboflavin during embryo development. PRACTICAL APPLICATIONS: These findings provide fundamental insight into the effects of incubation on egg yolk plasma protein alterations during the entire embryonic development for a better understanding of plasma protein biological functions, especially in nutrient transportations and the formation of embryonic organs.

Integrated Proteomic and N-Glycoproteomic Analyses of Chicken Egg during Embryonic Development.

To better appreciate the alterations of egg proteins and their modifications during embryonic development, a comparative and quantitative study was performed aimed at chicken egg white and yolk proteome and N-glycoproteome after 12 days of incubation using tandem mass tag (TMT)-labeling technology in conjunction with reversed-phase high-performance liquid chromatography (RP-HPLC). A total of 334 unique N-glycosite-containing peptides from 153 N-glycoproteins were identified, of which 82 N-glycosite-containing peptides showed significant changes after 12 days of incubation. The varied proteome was mainly involved with antibacterial, ionic binding, cell proliferation, and embryonic development, while the different degrading and/or absorbing priorities of egg proteins were proposed. This study provides substantial insight into the effects of N-glycoprotein variations on the utilization of egg proteins by chicken embryo during incubation.