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1.
Front Public Health ; 12: 1375379, 2024.
Article in English | MEDLINE | ID: mdl-38737864

ABSTRACT

Background: Inflammation and liver function are associated with cognitive decline and dementia. Little is known about the serum albumin-to-globulin ratio on cognitive function. Objective: The objective of this study was to investigate the association between albumin-to-globulin ratio and cognitive function among the American older people. Methods: The public data available on the US National Health and Nutrition Examination Survey (NHANES) from 2011 to 2014 was used for this cross-sectional study. Participants aged ≥60 years completed the cognitive function assessments, including word learning and recall modules from the Consortium to Establish a Registry for Alzheimer's Disease (CERAD), the animal fluency (AF) test, and the digit symbol substitution test (DSST). A composite cognition score was calculated to evaluate global cognition. The univariate and multivariate linear regression analysis, curve fitting, a threshold effect, along with a subgroup analysis and interaction tests were conducted. Results: Serum albumin-to-globulin ratio (per 0.1 unit) was positively associated DSST score (ß = 0.36, 95% CI: 0.21, 0.51), AF score (ß = 0.1, 95% CI: 0.04, 0.16) and global cognition score (ß = 0.05, 95% CI: 0.02, 0.07), after being fully adjusted, while albumin-to-globulin ratio was not related to CERAD score (ß = 0.05, 95% CI: -0.02, 0.12). A non-linear was observed in the dose-response relationship between albumin-to-globulin ratio and global cognition (P for non-linearity < 0.001). The subgroup analysis was overall stable, yet the interaction test was significant for age on global cognition (P for interaction = 0.036). Conclusion: The findings of this cross-sectional study suggested a positive and non-linear association between albumin-to-globulin ratio and cognitive function in the American older people. Maintaining albumin-to-globulin ratio with an appropriate range may be one of the therapeutic strategies to limit the progression of cognitive decline for the older people.


Subject(s)
Cognition , Nutrition Surveys , Serum Albumin , Humans , Cross-Sectional Studies , Male , Female , Aged , Cognition/physiology , United States , Middle Aged , Serum Albumin/analysis , Cognitive Dysfunction/blood , Aged, 80 and over , Serum Globulins/analysis , Globulins/analysis
2.
J Agric Food Chem ; 72(20): 11694-11705, 2024 May 22.
Article in English | MEDLINE | ID: mdl-38723176

ABSTRACT

The most significant and sensitive antigen protein that causes diarrhea in weaned pigs is soybean 7S globulin. Therefore, identifying the primary target for minimizing intestinal damage brought on by soybean 7S globulin is crucial. MicroRNA (miRNA) is closely related to intestinal epithelium's homeostasis and integrity. However, the change of miRNAs' expression and the function of miRNAs in Soybean 7S globulin injured-IPEC-J2 cells are still unclear. In this study, the miRNAs' expression profile in soybean 7S globulin-treated IPEC-J2 cells was investigated. Fifteen miRNAs were expressed differently. The differentially expressed miRNA target genes are mainly concentrated in signal release, cell connectivity, transcriptional inhibition, and Hedgehog signaling pathway. Notably, we noticed that the most significantly decreased miRNA was ssc-miR-221-5p after soybean 7S globulin treatment. Therefore, we conducted a preliminary study on the mechanisms of ssc-miR-221-5p in soybean 7S globulin-injured IPEC-J2 cells. Our research indicated that ssc-miR-221-5p may inhibit ROS production to alleviate soybean 7S globulin-induced apoptosis and inflammation in IPEC-J2 cells, thus protecting the cellular mechanical barrier, increasing cell proliferation, and improving cell viability. This study provides a theoretical basis for the prevention and control of diarrhea of weaned piglets.


Subject(s)
Apoptosis , Globulins , Glycine max , Intestinal Mucosa , MicroRNAs , Soybean Proteins , Animals , MicroRNAs/genetics , MicroRNAs/metabolism , Swine , Cell Line , Glycine max/genetics , Glycine max/chemistry , Glycine max/metabolism , Intestinal Mucosa/metabolism , Soybean Proteins/genetics , Soybean Proteins/metabolism , Globulins/genetics , Globulins/metabolism , Seed Storage Proteins/genetics , Epithelial Cells/metabolism , Cell Proliferation/drug effects , Cell Survival/drug effects , Antigens, Plant
3.
Food Chem ; 453: 139654, 2024 Sep 30.
Article in English | MEDLINE | ID: mdl-38781899

ABSTRACT

As a natural low-calorie sweetener, Mogroside V (Mog-V) has gradually become one of the alternatives to sucrose with superior health attributes. However, Mog-V will bring unpleasant aftertastes when exceeding a threshold concentration. To investigate the possibility of soy protein isolates (SPIs), namely ß-conglycinin (7S), and glycinin (11S) as flavor-improving agents of Mog-V, the binding mechanism between Mog-V and SPIs was explored through multi-spectroscopy, particle size, zeta potential, and computational simulation. The results of the multi-spectroscopic experiments indicated that Mog-V enhanced the fluorescence of 7S/11S protein in a static mode. The binding affinity of 7S-Mog-V was greater compared with 11S-Mog-V. Particle size and zeta potential analysis revealed that the interaction could promote aggregation of 7S/11S protein with different stability. Furthermore, computational simulations further confirmed that Mog-V could interact with the 7S/11S protein in different ways. This research provides a theoretical foundation for the development and application of SPI to improve the flavor of Mog-V, opening a new avenue for further expanding the market demand for Mog-V.


Subject(s)
Soybean Proteins , Sweetening Agents , Soybean Proteins/chemistry , Soybean Proteins/metabolism , Sweetening Agents/chemistry , Sweetening Agents/metabolism , Globulins/chemistry , Globulins/metabolism , Protein Binding , Antigens, Plant/chemistry , Antigens, Plant/metabolism , Computer Simulation , Seed Storage Proteins/chemistry , Seed Storage Proteins/metabolism , Molecular Docking Simulation , Triterpenes
4.
J Agric Food Chem ; 72(15): 8742-8748, 2024 Apr 17.
Article in English | MEDLINE | ID: mdl-38564658

ABSTRACT

Tyrosinase is capable of oxidizing tyrosine residues in proteins, leading to intermolecular protein cross-linking, which could modify the protein network of food and improve the texture of food. To obtain the recombinant tyrosinase with microbial cell factory instead of isolation tyrosinase from the mushroom Agaricus bisporus, a TYR expression cassette was constructed in this study. The expression cassette was electroporated into Trichoderma reesei Rut-C30 and integrated into its genome, resulting in a recombinant strain C30-TYR. After induction with microcrystalline cellulose for 7 days, recombinant tyrosinase could be successfully expressed and secreted by C30-TYR, corresponding to approximately 2.16 g/L tyrosinase in shake-flask cultures. The recombinant TYR was purified by ammonium sulfate precipitation and gel filtration, and the biological activity of purified TYR was 45.6 U/mL. The purified TYR could catalyze the cross-linking of glycinin, and the emulsion stability index of TYR-treated glycinin emulsion was increased by 30.6% compared with the untreated one. The cross-linking of soy glycinin by TYR resulted in altered properties of oil-in-water emulsions compared to emulsions stabilized by native glycinin. Therefore, cross-linking with this recombinant tyrosinase is a feasible approach to improve the properties of protein-stabilized emulsions and gels.


Subject(s)
Cross-Linking Reagents , Gene Expression , Globulins , Hypocreales , Monophenol Monooxygenase , Recombinant Proteins , Soybean Proteins , Monophenol Monooxygenase/biosynthesis , Monophenol Monooxygenase/genetics , Monophenol Monooxygenase/isolation & purification , Monophenol Monooxygenase/metabolism , Cross-Linking Reagents/isolation & purification , Cross-Linking Reagents/metabolism , Hypocreales/classification , Hypocreales/genetics , Hypocreales/growth & development , Hypocreales/metabolism , Globulins/chemistry , Globulins/metabolism , Soybean Proteins/chemistry , Soybean Proteins/metabolism , Electroporation , Cellulose , Ammonium Sulfate , Chromatography, Gel , Fractional Precipitation , Emulsions/chemistry , Emulsions/metabolism , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , Recombinant Proteins/metabolism , Protein Stability , Endoplasmic Reticulum/metabolism , Protein Sorting Signals , Oils/chemistry , Water/chemistry
5.
J Agric Food Chem ; 72(17): 9947-9954, 2024 May 01.
Article in English | MEDLINE | ID: mdl-38647139

ABSTRACT

Glycinin is an important allergenic protein. A1a is the acidic chain of the G1 subunit in glycinin (G1A1a), and it has strong allergenicity. In this study, we used phage display technology to express the protein of G1A1a and its overlapping fragments and an indirect enzyme-linked immunosorbent assay (iELISA) to determine the antigenicity and allergenicity of the expressed protein. After three rounds of screening, it was determined that fragment A1a-2-B-I (151SLENQLDQMPRRFYLAGNQEQEFLKYQQEQG181) is the allergenic domain of G1A1a destroyed by thermal processing. In addition, three overlapping peptides were synthesized from fragments A1a-2-B-I, and a linear epitope was found in this domain through methods including dot blot and iELISA. Peptide 2 (157DQMPRRFYLANGNQE170) showed allergenicity, and after replacing it with alanine, it was found that amino acids D157, Q158, M159, and Y164 were the key amino acids that affected its antigenicity, while Q158, M159, R162, and N168 affected allergenicity.


Subject(s)
Allergens , Globulins , Hot Temperature , Soybean Proteins , Allergens/immunology , Allergens/chemistry , Humans , Globulins/chemistry , Globulins/immunology , Soybean Proteins/chemistry , Soybean Proteins/immunology , Amino Acid Sequence , Food Hypersensitivity/immunology , Epitopes/chemistry , Epitopes/immunology , Protein Domains , Antigens, Plant/immunology , Antigens, Plant/chemistry , Antigens, Plant/genetics , Glycine max/chemistry , Glycine max/immunology , Enzyme-Linked Immunosorbent Assay
6.
Int J Biol Macromol ; 269(Pt 1): 131900, 2024 Jun.
Article in English | MEDLINE | ID: mdl-38677675

ABSTRACT

Liposomes were modified with different proportions of ß-conglycinin (7S) and glycinin (11S) to form Lip-7S and Lip-11S. The morphology, interaction and in vitro simulated digestion of liposomes were studied. The particle size of Lip-7S was smaller than that of Lip-11S. When the values of Lip-7S and Lip-11S were 1:1 and 1:0.75, respectively, the ζ-potential had the maximum absolute value and the dispersion of the system was good. The results of multispectral analysis showed that hydrogen-bond and hydrophobic interaction dominated protein-modified liposomes, the protein structure adsorbed on the surface of liposomes changed, the content of α-helix decreased, and the structure of protein-modified liposomes became denser. The surface hydrophobicity and micropolarity of liposomes decreased with the increase of protein ratio, and tended to be stable after Lip-7S (1:1) and Lip-11S (1:0.75). Differential scanning calorimetry showed that Lip-7S had higher phase transition temperature (≥170.5 °C) and better rigid structure. During simulated digestion, Lip-7S (22.5 %) released less Morin than Lip (40.6 %) and Lip-11S (26.2 %), and effectively delayed the release of FFAs. The environmental stability of liposomes was effectively improved by protein modification, and 7S had better modification effect than 11S. This provides a theoretical basis for 7S and 11S modified liposomes, and also provides a data reference for searching for new materials for stabilization of liposomes.


Subject(s)
Antigens, Plant , Globulins , Liposomes , Seed Storage Proteins , Soybean Proteins , Globulins/chemistry , Seed Storage Proteins/chemistry , Soybean Proteins/chemistry , Liposomes/chemistry , Antigens, Plant/chemistry , Hydrophobic and Hydrophilic Interactions , Digestion , Particle Size , Hydrogen Bonding
7.
J Agric Food Chem ; 72(18): 10627-10639, 2024 May 08.
Article in English | MEDLINE | ID: mdl-38664940

ABSTRACT

Effective reduction of the allergenicity of instant soy milk powder (ISMP) is practically valuable for expanding its applications. This study optimized the enzymolysis technology of ISMP using single-factor experiments and response surface methodology, combined serological analysis, cellular immunological models, bioinformatics tools, and multiple spectroscopy techniques to investigate the effects of alcalase hydrolysis on allergenicity, spatial conformation, and linear epitopes of ISMP. Under the optimal process, special IgE and IgG1 binding abilities and allergenic activity to induce cell degranulation of alcalase-hydrolyzed ISMP were reduced by (64.72 ± 1.76)%, (56.79 ± 3.72)%, and (73.3 ± 1.19)%, respectively (P < 0.05). Moreover, the spatial conformation of instant soy milk powder hydrolysates (ISMPH) changed, including decreased surface hydrophobicity, a weaker peak of amide II band, lower contents of α-helix and ß-sheet, and an enhanced content of random coil. Furthermore, the linear epitopes of major soy allergens, 9 from glycinin and 13 from ß-conglycinin, could be directionally disrupted by alcalase hydrolysis. Overall, the structure-activity mechanism of alcalase hydrolysis to reduce ISMP allergenicity in vitro was preliminarily clarified. It provided a new research direction for the breakthrough in the desensitization of ISMP and a theoretical basis for revealing the potential mechanism of alcalase enzymolysis to reduce the allergenicity of ISMP.


Subject(s)
Allergens , Soy Milk , Subtilisins , Humans , Allergens/chemistry , Allergens/immunology , Allergens/metabolism , Food Hypersensitivity/prevention & control , Food Hypersensitivity/immunology , Globulins/chemistry , Globulins/immunology , Hydrolysis , Immunoglobulin E/immunology , Immunoglobulin G/immunology , Powders/chemistry , Soy Milk/chemistry , Soybean Proteins/chemistry , Soybean Proteins/immunology , Soybean Proteins/metabolism , Structure-Activity Relationship , Subtilisins/metabolism
8.
Plant Physiol Biochem ; 210: 108653, 2024 May.
Article in English | MEDLINE | ID: mdl-38670029

ABSTRACT

Edible plant seeds provide a relatively inexpensive source of protein and make up a large part of nutrients for humans. Plant seeds accumulate storage proteins during seed development. Seed storage proteins act as a reserve of nutrition for seed germination and seedling growth. However, seed storage proteins may be allergenic, and the prevalence of food allergy has increased rapidly in recent years. The 11S globulins account for a significant number of known major food allergens. They are of interest to the public and the agricultural industry because of food safety concerns and the need for crop enhancement. We sought to determine the crystal structure of Cor a 9, the 11 S storage protein of hazelnut and a food allergen. The structure was refined to 1.92 Å, and the R and Rfree for the refined structure are 17.6% and 22.5%, respectively. The structure of Cor a 9 showed a hetero hexamer of an 11S seed storage protein for the first time. The hexamer was two trimers associated back-to-back. Two long alpha helixes at the C-terminal end of the acidic domain of one of the Cor a 9 isoforms lay at the trimer-trimer interface's groove. These data provided much-needed information about the allergenicity of the 11S seed proteins. The information may also facilitate a better understanding of the folding and transportation of 11S seed storage proteins.


Subject(s)
Corylus , Seed Storage Proteins , Corylus/chemistry , Corylus/metabolism , Seed Storage Proteins/chemistry , Seed Storage Proteins/metabolism , Crystallography, X-Ray , Seeds/metabolism , Seeds/chemistry , Plant Proteins/chemistry , Plant Proteins/metabolism , Globulins/chemistry , Globulins/metabolism , Amino Acid Sequence , Protein Multimerization , Models, Molecular
9.
J Agric Food Chem ; 72(14): 8103-8113, 2024 Apr 10.
Article in English | MEDLINE | ID: mdl-38530645

ABSTRACT

The effect of genotype and environment on oat protein composition was analyzed through size exclusion-high-performance liquid chromatography (SE-HPLC) and liquid chromatography-mass spectrometry (LC-MS) to characterize oat protein isolate (OPI) extracted from three genotypes grown at three locations in the Canadian Prairies. SE-HPLC identified four fractions in OPI, including polymeric globulins, avenins, glutelins, and albumins, and smaller proteins. The protein composition was dependent on the environment, rather than the genotype. The proteins identified through LC-MS were grouped into eight categories, including globulins, prolamins/avenins, glutelins, enzymes/albumins, enzyme inhibitors, heat shock proteins, grain softness proteins, and allergenic proteins. Three main globulin protein types were also identified, including the P14812|SSG2-12S seed storage globulin, the Q6UJY8_TRITU-globulin, and the M7ZQM3_TRIUA-Globulin-1 S. Principal component analysis indicated that samples from Manitoba showed a positive association with the M7ZQM3_TRIUA-Globulin-1 S allele and Q6UJY8_TRITU-globulin, while samples from Alberta and Saskatchewan had a negative association with them. The results show that the influence of G × E on oat protein fractions and their relative composition is crucial to understanding genotypes' behavior in response to different environments.


Subject(s)
Globulins , Plant Proteins , Plant Proteins/metabolism , Avena/genetics , Avena/metabolism , Chromatography, High Pressure Liquid , Liquid Chromatography-Mass Spectrometry , Chromatography, Liquid , Tandem Mass Spectrometry , Canada , Glutens/genetics , Prolamins/metabolism , Globulins/metabolism , Albumins
10.
Clin Rheumatol ; 43(4): 1299-1310, 2024 Apr.
Article in English | MEDLINE | ID: mdl-38433147

ABSTRACT

OBJECTIVE: To explore the association of geriatric nutrition risk index (GNRI), a traditional albumin-body weight calculation, with myopenia in patients with rheumatoid arthritis (RA) and compare its ability to identify myopenia with protein indicators. METHODS: This cross-sectional study was carried out based on a Chinese RA cohort. Clinical data and protein indicators (including albumin, globulin, albumin to globulin ratio, prealbumin, hemoglobin) were collected. GNRI was estimated by serum albumin and body weight. Myopenia was indicated as muscle mass loss measured by bioelectric impedance analysis. RESULTS: There were 789 RA patients included with mean age 52.6 ± 12.6 years and 77.6% female. There were 41.3%, 18.0%, 27.5%, 13.2% patients with no (GNRI > 98), low (GNRI 92 to ≤ 98), moderate (GNRI 82 to < 92), and major nutrition-related risk (GNRI < 82). There were 406 (51.5%) RA patients with myopenia, RA patients with major nutrition-related risk had the highest prevalence of myopenia (87.5% vs. 73.3% vs. 50.0% vs. 26.1%). Multivariate logistic analysis showed that compared with no risk, RA patients with low (OR = 3.23, 95% CI: 1.86-5.61), moderate (OR = 9.56, 95% CI: 5.70-16.01), and major nutrition-related risk (OR = 28.91, 95% CI: 13.54-61.71) were associated with higher prevalence of myopenia. Receiver operating characteristic curves showed that GNRI (AUC = 0.79) performed a better identifiable ability toward myopenia than serum albumin (AUC = 0.66) or others indicators (AUC range 0.59 to 0.65), respectively. CONCLUSION: GNRI, an objective and convenient albumin-weight index, may be preferable for identifying myopenia in RA patients. Key Points • We firstly elucidated the association of GNRI with muscle mass loss among RA patients, and compared its ability to identify muscle mass loss with serum albumin or other protein indicators. • Major nutrition-related risk identified by GNRI showed the highest risk of muscle mass loss, GNRI demonstrated a greater ability to identify myopenia in RA patients. which indicated GNRI was an objective and convenient albumin-weight index to identify myopenia in RA patients.


Subject(s)
Arthritis, Rheumatoid , Globulins , Humans , Female , Aged , Adult , Middle Aged , Male , Nutrition Assessment , Cross-Sectional Studies , Nutritional Status , Arthritis, Rheumatoid/complications , Muscular Atrophy , Serum Albumin , Body Weight , Muscles , Risk Factors
11.
Prev Vet Med ; 226: 106167, 2024 May.
Article in English | MEDLINE | ID: mdl-38461703

ABSTRACT

Feline immunodeficiency virus (FIV) and feline leukemia virus (FeLV) are retroviruses of great importance for domestic cats with a worldwide distribution. A retrospective study was conducted to determine the epidemiological and clinicopathological aspects of the infection by FIV and FeLV in cats from the Brazilian semiarid region. Cats treated between 2011 and 2021 at the teaching veterinary hospital of the Federal Rural University of the Semi-Arid Region that were submitted to a point-of-care (POC) test to detect anti-FIV IgG antibodies and FeLV antigen were enrolled in the study. Overall, 454 cats were selected, of which 30.2% [95% CI = 26.0% - 34.3%] were FIV-positive, 1.1% [95% CI = 0.9% - 1.2%] were FeLV-positive, and 0.7% [95% CI = 0.1% - 1.3%] were coinfected by both retroviruses. No statistical association was found between the studied retroviruses (P = 0.144). Multivariable analysis detected significant associations between FIV infection and male sex [OR = 5.7, 95% CI = 3.0-10.7, P < 0.0001), age between 19 and 78 months [OR = 5.2, 95% CI = 2.2-12.1, P < 0.0001], age greater than 78 months [OR = 12.8, 95% CI = 5.1-31.9, P < 0.0001], crossbreed [OR = 4.1, 95% CI = 1.2-13.4, P = 0.021], the presence of oral disease [OR = 2.1, 95% CI = 1.3-3.4, P = 0.004], reduced red blood cell (RBC) count [OR = 3.7, 95% CI = 1.9-7.2, P < 0.0001], and an albumin:globulin (A:G) ratio lower than 0.6 [OR = 3.4, 95% CI = 1.6-7.1, P = 0.001]. No statistical analyses were performed for FeLV infection due to the low number of positive animals. In the quantitative analyses of hematological parameters, FIV-positive cats presented lower values for RBC, hemoglobin, hematocrit, lymphocytes, and platelets compared to the negative animals. In the biochemical profile, cats infected with FIV showed higher creatinine, urea, total protein, and globulin values, while lower values for albumin and A:G ratio were observed (P < 0.05). The findings of this study characterized the prevalence, clinicopathological findings, and risk factors associated with FIV and FeLV in cats from the Brazilian semiarid region. They may help support veterinary practitioners in diagnosing feline retroviruses. The FIV prevalence observed is among the highest reported in Brazil, demonstrating the need for prevention and control strategies for this retrovirus.


Subject(s)
Cat Diseases , Feline Acquired Immunodeficiency Syndrome , Globulins , Immunodeficiency Virus, Feline , Leukemia, Feline , Cats , Animals , Male , Leukemia Virus, Feline , Brazil/epidemiology , Retrospective Studies , Leukemia, Feline/epidemiology , Albumins , Feline Acquired Immunodeficiency Syndrome/epidemiology , Cat Diseases/epidemiology
12.
Molecules ; 29(6)2024 Mar 08.
Article in English | MEDLINE | ID: mdl-38542847

ABSTRACT

This study evaluated the effects of four highland barley proteins (HBPs), namely, albumin, globulin, gliadin and glutenin, on the short-term retrogradation of highland barley starch (HBS). The findings reveal that HBPs could reduce the viscosity, storage modulus and hardness of HBS, with albumin and globulin showing more prominent effects. Furthermore, with the addition of HBPs, the loss tangent (tan δ) of HBS loss increased from 0.07 to 0.10, and the enthalpy of gelatinization decreased from 8.33 to 7.23. The degree of retrogradation (DR%) of HBS was 5.57%, and the DR% decreased by 26.65%, 38.78%, 11.67% and 20.29% with the addition of albumin, globulin, gliadin and glutenin, respectively. Moreover, the relative crystallinity (RC) and the double helix structures were inhibited with the HBPs' incorporation. Meanwhile, the HBPs also could inhibit water migration and improve the structure of HBS gels. In summary, HBPs could inhibit the retrogradation behavior of HBS, which provides new theoretical insights for the production studies of highland barley foods.


Subject(s)
Globulins , Hordeum , Starch/chemistry , Gliadin/chemistry , Albumins
13.
Sci Rep ; 14(1): 7219, 2024 03 27.
Article in English | MEDLINE | ID: mdl-38538743

ABSTRACT

Petroleum aromatic hydrocarbons are considered one of the most dangerous aquatic pollutants due to their widespread across water bodies, persistence, and extension to the food chain. To our knowledge, there hasn't been any research investigating the hepatorenoprotective effects of Spirulina platensis (SP) against toxicity induced by these environmental toxicants in fish. Thus, we decided to explore its potential safeguarding against benzene and toluene exposure in adult Clarias gariepinus. To achieve this objective, fish were divided into five groups (60 per group; 20 per replicate). The first group served as a control. The second and third groups were intoxicated with benzene and toluene at doses of 0.762 and 26.614 ng/L, respectively for 15 days. The fourth and fifth groups (SP + benzene and SP + toluene, respectively) were challenged with benzene and toluene as previously mentioned following dietary inclusion of SP at a dose of 5 g/kg diet for 30 days. The marked increase in liver metabolizing enzymes, glucose, total protein, albumin, globulin, albumin/globulin ratio, and creatinine confirmed the hepato- and nephrotoxic impacts of benzene and toluene. These outcomes were coupled with cytopathological affections and excessive collagen deposition. The incorporation of SP in ration formulation, on the contrary, restored the previously mentioned toxicological profile due to its antioxidant and cytoprotective attributes. Regardless of SP intervention, the renal tissues still displayed histo-architectural lesions, because of insufficient dose and timeframe. Additional research will be required to identify the ideal SP remediation regimen.


Subject(s)
Catfishes , Globulins , Spirulina , Animals , Benzene/metabolism , Catfishes/metabolism , Globulins/metabolism , Toluene/metabolism , Albumins/metabolism
14.
J Agric Food Chem ; 72(12): 6601-6612, 2024 Mar 27.
Article in English | MEDLINE | ID: mdl-38480492

ABSTRACT

ß-conglycinin (ß-CG) induces intestinal damage in piglets; however, its regulatory mechanisms are not fully understood. This study aimed to investigate the molecular mechanisms by which ß-CG regulates intestinal injury in piglets through downstream genes and proteins. Our findings revealed that ß-CG significantly reduced villus height while increasing the crypt depth. In addition, we analyzed the transcriptome and proteome of jejunum tissues after the ß-CG treatment. In total, 382 differentially expressed genes (DEGs) and 292 differentially expressed proteins (DEPs) were identified between the treatment and the control groups. The expression levels of DEGs and DEPs were validated by using quantitative reverse transcription polymerase chain reaction (qRT-PCR) and Western blotting, respectively. The findings revealed a consistent correlation between their expression levels and transcriptomic and proteomic data. In addition, Gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses of DEGs and DEPs revealed their enrichment in oxidation-related GOs, as well as in lysosome-related pathways. A protein-protein interaction (PPI) regulatory network was constructed based on the DEPs. The integration of transcriptomic and proteomic analyses identified six genes that were significantly different at both the transcript and the protein levels. This study provides valuable insights into the molecular mechanisms underlying ß-CG-induced intestinal injury in piglets.


Subject(s)
Antigens, Plant , Globulins , Proteome , Seed Storage Proteins , Soybean Proteins , Transcriptome , Animals , Swine , Proteomics , Intestines , Gene Expression Profiling
15.
Res Vet Sci ; 171: 105203, 2024 May.
Article in English | MEDLINE | ID: mdl-38432158

ABSTRACT

Although haemolysis is the most common source of preanalytical error in clinical laboratories, its influence on cattle biochemistry remains poorly understood. The effect of haemolysis and its clinical relevance were investigated in 70 samples in which haemolysis was artificially induced (by spiking with increasing amounts of haemolysate, yielding 0.0%, 0.2%, 0.5%, 1.0%, 2.5%, 5.0% and 10% haemolysis degree (HD)), focusing on key parameters for bovine metabolic health assessment, including albumin, alkaline phosphatase (ALP), aspartate aminotransferase (AST), blood urea nitrogen (BUN), calcium (Ca), cholesterol, creatinine, creatine kinase (CK), gamma-glutamyl transferase (GGT), globulins, magnesium (Mg), phosphorus (P), total bilirubin (TBIL) and total proteins (TP). Preanalytical haemolysis significantly affected most (8 of 14) of the biochemical parameters analysed, leading to significant increases in concentrations of albumin (starting at 5% HD), cholesterol (at 5% HD) and P (at 10% HD) and to significant decreases in Ca (at 2.5% HD), creatinine (at 5% HD), globulins (at 10% HD), TBIL (at 2.5% HD) and TP (at 10% HD). Comparison of the present and previous data indicated that, for each parameter, the HD required to produce significant bias and the clinical relevance of over- and underestimation are variable and appear to depend on the analytical technique used. Therefore, different laboratories should evaluate the influence of haemolysis in their analytical results and provide advice to clinicians accordingly. Affected parameters should be interpreted together with clinical signs and other analytical data to minimize misinterpretations (false or masked variations). Finally, due to the significant impact on numerous parameters and the limited potential for correction, we recommend rejection of samples with >10% HD.


Subject(s)
Cattle Diseases , Globulins , Cattle , Animals , Hemolysis , Creatinine , Cholesterol , Calcium , Albumins
16.
J Agric Food Chem ; 72(13): 7167-7178, 2024 Apr 03.
Article in English | MEDLINE | ID: mdl-38511978

ABSTRACT

IAVPGEVA, an octapeptide derived from soybean 11S globulin hydrolysis, also known as SGP8, has exhibited regulatory effects on lipid metabolism, inflammation, and fibrosis in vitro. Studies using MCD and HFD-induced nonalcoholic steatohepatitis (NASH) models in mice show that SGP8 attenuates hepatic injury and metabolic disorders. Mechanistic studies suggest that SGP8 inhibits the JNK-c-Jun pathway in L02 cells and liver tissue under metabolic stress and targets DPP4 with DPP4 inhibitory activity. In conclusion, the results suggest that SGP8 is an orally available DPP4-targeting peptide with therapeutic potential in NASH.


Subject(s)
Globulins , Non-alcoholic Fatty Liver Disease , Soybean Proteins , Mice , Animals , Non-alcoholic Fatty Liver Disease/drug therapy , Non-alcoholic Fatty Liver Disease/metabolism , Dipeptidyl Peptidase 4/metabolism , Liver/metabolism , Globulins/metabolism , Mice, Inbred C57BL , Disease Models, Animal
17.
J Agric Food Chem ; 72(11): 5926-5934, 2024 Mar 20.
Article in English | MEDLINE | ID: mdl-38457471

ABSTRACT

Glycinin (11S) and ß-conglycinin (7S) from soybean (glycine max) cause diarrhea and intestinal barrier damage in young animals. Understanding the mechanisms underlying the damage caused by 7S and 11S, it is vital to develop strategies to eliminate allergenicity. Consequently, we investigated 7S/11S-mediated apoptosis in porcine intestinal epithelial (IPEC-J2) cells. IPEC-J2 cells suffered endoplasmic reticulum stress (ERS) in response to 7S and 11S, activating protein kinase RNA-like ER kinase, activating transcription factor 6, C/EBP homologous protein, and inositol-requiring enzyme 1 alpha. 4-Phenylbutyric acid (4-PBA) treatment alleviated ERS; reduced the NLR family pyrin domain containing 3, interleukin-1ß, and interleukin-18 levels; inhibited apoptosis; increased mitofusin 2 expression; and mitigated Ca2+ overload and mitochondria-associated ER membrane (MAM) dysfunction, thereby ameliorating IPEC-J2 injury. We demonstrated the pivotal role of ERS in MAM dysfunction and 7S- and 11S-mediated apoptosis, providing insights into 7S- and 11S-mediated intestinal barrier injury prevention and treatment.


Subject(s)
Antigens, Plant , Apoptosis , Globulins , Glycine max , Phenylbutyrates , Seed Storage Proteins , Soybean Proteins , Animals , Swine , Endoplasmic Reticulum , Mitochondria , Endoplasmic Reticulum Stress
18.
Int J Med Sci ; 21(4): 742-754, 2024.
Article in English | MEDLINE | ID: mdl-38464832

ABSTRACT

Purpose: We aimed to investigate the impact of Omicron variant infection on the perioperative organ function in patients undergoing elective surgery. Methods: A total of 5029 patients who underwent elective surgery between October 2022 and January 2023 at our hospital were enrolled. Among them, the patients who underwent elective surgery between October 2022 and November 2022 composed Group 1 (not infected with the Omicron variant) the control group; those who underwent elective surgery between December 2022 and January 2023 composed Group 2 (one month after Omicron variant infection) the experimental group. We further divided the patients into two subgroups for analysis: the tumor subgroup and the nontumor subgroup. Data on organ system function indicators, including coagulation parameters, liver function, complete blood count (CBC), and kidney function, were collected before and after surgery. Differences between the two groups were subsequently analyzed via binary logistic regression analysis. Results: Compared with those in the uninfected patient group, the following changes were observed in patients with Omicron variant infection who underwent elective surgery one month after infection: prothrombin activity (PTa), prothrombin time (PT), fibrinogen, albumin/globulin, alanine aminotransferase (ALT), mean corpuscular hemoglobin concentration (MCHC), platelet (PLT), and anemia were increased AST/ALT, indirect bilirubin (IBILI), eosinophils, and uric acid were decreased before surgery; and lung infection/pneumonia and fibrinogen were increased, while AST/ALT, globulin, total bilirubin (TBIL), white blood cell count (WBC), and uric acid were decreased after surgery. There was no significant difference in the mortality rate or length of hospital stay (LOS) between the two groups. Subgroup analysis revealed elevated monocyte, PLT, and fibrinogen classification, levels and decreased globulin, prealbumin (PBA), eosinophil, and uric acid levels in the tumor subgroup of patients who underwent elective surgery one month after Omicron infection compared with those in the uninfected patients. Compared with the nontumor subgroup, fibrinogen levels, lung infection/pneumonia, TBIL, and PLT count were increased in the uninfected patients, while the globulin and eosinophil levels were decreased. Conclusion: Compared with uninfected patients, patients who underwent elective surgery one month after Omicron variant infection exhibited minimal changes in perioperative coagulation parameters, liver function, CBC counts, and kidney function. Additionally, no significant differences in postoperative mortality or LOS were observed between the two groups.


Subject(s)
Globulins , Neoplasms , Pneumonia , Humans , Retrospective Studies , Case-Control Studies , Uric Acid , Liver/surgery , Liver/pathology , Kidney/surgery , Fibrinogen , Bilirubin , Neoplasms/pathology
19.
BMC Vet Res ; 20(1): 79, 2024 Mar 05.
Article in English | MEDLINE | ID: mdl-38443906

ABSTRACT

BACKGROUND: Inflammatory myopathy and perivasculitis have been recently described in horses with chronic equine piroplasmosis (EP). These alterations may be linked to poor performances. The aims of this study were to evaluate the prevalence for EP in clinically healthy Italian Standardbred (IS) racehorses and to compare laboratory parameters and performance metrics between positive and negative horses. Real-time PCR was applied for the detection of T. equi and B. caballi positivity. Haematology parameters, blood chemistry results, subjective muscle mass scores, and performance metrics were compared between PCR-positive and -negative horses. RESULTS: This cross-sectional study included 120 well-trained IS racehorses and was performed over a two-years period. The prevalence of T. equi was 36.3%, whereas all samples were negative for B. caballi. Red blood cells count, haemoglobin concentration, aspartate aminotransferase, alkaline phosphatase, and gamma-glutamyl transferase activities were significantly higher in PCR-positive horses, whereas blood urea nitrogen, globulin concentration and globulin-to-albumin ratio were significantly lower in PCR-positive horses compared to PCR-negative ones. Nonetheless, all values fell within the physiological range. The best racing time, which was selected as the most representative of the performance metrics at the principal component analysis, was not affected by PCR positivity, the muscle mass score or the training yard. The best racing time was significantly better in horses with a mild or no signs of muscular atrophy, within the PCR-positive group. The muscle mass score was associated with the training yard in PCR-negative horses. CONCLUSIONS: Prevalence of T. equi was high in IS racehorses in southern Italy. The absence of obvious changes in haematological and biochemical parameters, as well as performance metrics in positive horses, highlights the need for specific diagnostic tests to identify chronically infected horses.


Subject(s)
Globulins , Theileria , Animals , Horses , Cross-Sectional Studies , Theileria/genetics , Real-Time Polymerase Chain Reaction/veterinary , Italy/epidemiology
20.
J Sci Food Agric ; 104(7): 4363-4370, 2024 May.
Article in English | MEDLINE | ID: mdl-38299730

ABSTRACT

BACKGROUND: The two major storage proteins of soymilk are the globulins 7S and 11S. Freeze-thaw fractionation is a simple method for separating these proteins in raw soymilk. In this study, we assessed the freeze-thaw fractionation ability of raw soymilk under various pH (4.3-11.6) conditions and added salt (sodium chloride) concentrations (0.00-0.67 mol L-1). RESULTS: We successfully achieved fractionation within a pH range of 5.8-6.7 and when the salt concentration was 0.22 mol L-1 or lower. Analysis of particle size distribution and microscopic examination of soymilk revealed no direct correlation between particle size and freeze-thaw fractionation ability. Interestingly, it was confirmed that the ranges of zeta potential values associated with successful freeze-thaw fractionation in raw soymilk remained consistent across different pH and salt concentration conditions. These ranges were between -23 and -28 mV at pH levels ranging from 5.8 to 6.7 and between -18 and -29 mV at added salt concentrations ranging from 0 to 0.22 mol L-1. CONCLUSION: The pH and salt concentration in raw soymilk markedly influence the freeze-thaw fractionation process. We confirmed that the range of zeta potential values where fractionation was possible remained consistent under various pH and salt concentration conditions. These findings suggest that the zeta potential value might serve as an indicator for evaluating the freeze-thaw fractionation ability of raw soymilk. © 2024 Society of Chemical Industry.


Subject(s)
Globulins , Soy Milk , Soybean Proteins/metabolism , Sodium Chloride , Soy Milk/metabolism , Globulins/metabolism , Hydrogen-Ion Concentration
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