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1.
Heliyon ; 10(5): e26836, 2024 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-38434271

RESUMO

Proton magnetic resonance spectroscopy (1H-MRS) is the only non-invasive technique to quantify neurometabolic compounds in the living brain. We used 1H-MRS to evaluate the brain metabolites in a rat model of Sepsis-associated encephalopathy (SAE) established by cecal ligation and puncture (CLP). 36 male Sprague-Dawley rats were randomly divided into sham and CLP groups. Each group was further divided into three subgroups: subgroup O, subgroup M, and subgroup N. Neurological function assessments were performed on the animals in the subgroup O and subgroup N at 24 h, 48 h, and 72 h. The animals in the subgroup M were examined by magnetic resonance imaging (MRI) at 12 h after CLP. Compared with the sham group, the ratio of N-acetylaspartate (NAA) to creatine (Cr) in the hippocampus was significantly lower in the CLP group. The respective ratios of lactate (Lac), myo-inositol (mIns), glutamate and glutamine (Glx), lipid (Lip), and choline (Cho) to Cr in the CLP group were clearly higher than those in the sham group. Cytochrome c, intimately related to oxidative stress, was elevated in the CLP group. Neurofilament light (NfL) chain and glial fibrillary acidic protein (GFAP) scores in the CLP group were significantly higher than those in the sham group, while zonula occludens-1 (ZO-1) was downregulated. Compared with the sham group, the CLP group displayed higher values of oxygen extraction fraction (OEF), central venous-arterial partial pressure of carbon dioxide (P (cv-a) CO2), and central venous lactate (VLac). In contrast, jugular venous oxygen saturation (SjvO2) declined. In the present study, 1H-MRS could be used to quantitatively assess brain injury in terms of microcirculation disorder, oxidative stress, blood-brain barrier disruption, and glial cell activation through changes in metabolites within brain tissue.

2.
J Sci Food Agric ; 104(3): 1645-1655, 2024 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-37850306

RESUMO

BACKGROUND: The interaction between food allergens and plant polyphenols has become a safe and effective management strategy to prevent food allergies. Ovalbumin (OVA) is the most abundant allergen in egg whites. Resveratrol (RES) is a plant polyphenol that is abundant in red grapes, berries, and peanuts, and has an anti-allergic effect on allergy-related immune cells. However, there is little information about the effect of RES on the allergenicity of OVA. In this study, the effect of RES on the allergenicity of OVA was investigated. RESULTS: Molecular docking and spectroscopic studies indicated that the addition of RES changed the structure of OVA. The digestion and transfer rate of OVA-RES were effectively improved with an in vitro gastrointestinal digestion model and Caco-2 cell model, especially when the molar ratio of OVA-RES was 1:20. Meanwhile, the KU812 cell degranulation assay proved that the potential allergenicity was remarkably decreased while the molar ratios of OVA-RES were increased to 1:20. Furthermore, hydrogen bonds and van der Waals forces were the dominating forces to stabilize the OVA-RES complexes. CONCLUSION: All the findings demonstrated that the potential allergenicity of OVA was reduced when interacting with RES, and RES can be a potential food material for preparing a hypoallergenic protein, especially for egg allergy. © 2023 Society of Chemical Industry.


Assuntos
Alérgenos , Hipersensibilidade Alimentar , Humanos , Ovalbumina/química , Resveratrol , Simulação de Acoplamento Molecular , Células CACO-2 , Imunoglobulina E , Hipersensibilidade Alimentar/prevenção & controle
3.
J Food Biochem ; 46(12): e14424, 2022 12.
Artigo em Inglês | MEDLINE | ID: mdl-36197951

RESUMO

Casein is one of the main allergens in cow's milk, accounting for 80% of cow's milk proteins. The ability of hydrolyzing proteins by bacteria is also different. In this study, the capacity of lactic acid bacteria to hydrolyze casein or ß-casein and the IgG/IgE-binding capacity of hydrolysates were evaluated. The intensity of casein and ß-casein degradation was analyzed by SDS-PAGE and RP-HPLC. The hydrolysates were tested for their capacity to inhibit IgG and IgE binding by ELISA. The peptides in the hydrolysate were also analyzed by LC-MS/MS. In these strains, Lactobacillus rhamnosus (CICC No. 22175) had the strongest hydrolysis of casein and ß-casein. The hydrolysate of Lactobacillus rhamnosus (CICC No. 22175) showed the lowest antigenicity and potential allergenicity. It also hydrolyzed major allergen IgE epitopes and preserved T cell epitopes. Thereore Lactobacillus rhamnosus (CICC No. 22175) could be used for developing hypoallergenic dairy products and the development of tolerance. PRACTICAL APPLICATIONS: By the study, it obtained that a strain of Lactobacillus rhamnosus could effectively degrade casein and reduced the potential allergenicity of casein. At the same time, some major allergic epitopes were hydrolyzed and T cell epitopes were preserved. Therefore, it is very valuable for the application and development of lactic acid bacteria. The hydrolysate can also be used in a new hypoallergenic dairy formula with specific health benefits and promoting oral tolerance.


Assuntos
Lacticaseibacillus rhamnosus , Lactobacillales , Hipersensibilidade a Leite , Feminino , Animais , Bovinos , Caseínas , Alérgenos , Proteínas do Leite , Hidrólise , Lactobacillales/metabolismo , Cromatografia Líquida , Epitopos de Linfócito T , Imunoglobulina E , Espectrometria de Massas em Tandem , Imunoglobulina G
4.
BMJ Open ; 11(1): e041453, 2021 01 06.
Artigo em Inglês | MEDLINE | ID: mdl-33408203

RESUMO

OBJECTIVES: Examine compliance with personal protective measures in communities for the prevention and control of local transmission of the COVID-19, and explore indicators for such behavioural compliance. DESIGN: Cross-sectional design with a self-selecting sample. Data collected in February 2020. SETTING: Community dwellers in China. PARTICIPANTS: 2956 participants aged 16 and above completed the study and were included in the analysis. OUTCOME MEASURES: Nationwide COVID-19 survey. Demographics and self-reported compliance with four personal protective measures-home quarantine, mask-wearing, temperature-taking and hand-sanitising were collected. Outbreak severity and timeliness of personal protection order were obtained from the China Center for Disease Control and Prevention website. Logistic regression models were employed to examine the association between demographic and social indicators and behavioural compliance. RESULTS: Compliance with home quarantine was only associated with gender (men, OR=0.61 (0.51-0.73), inverse association) but no other indicators. In contrast, men had higher compliance with mask-wearing (OR=1.79 (1.49-2.16)) and temperature-taking (OR=1.27 (1.05-1.53)). Compared with younger adults (≤20 years), the middle-age groups (31-40 and 41-50 years of age) were more compliant with all protective behaviours, except for home quarantine (OR=0.71 (0.54-0.93) and 0.67 (0.46-0.97), respectively). CONCLUSION: Male gender was associated with lower compliance with home quarantine yet higher compliance with mask-wearing and temperature-taking. The middle-age participants (31-50 years) had lower compliance with home quarantine but higher with other measures. These findings may be supported by the economic considerations and the long-inherited Confucian values among Chinese. In light of the ongoing COVID-19 pandemic, public health authorities should tailor policy implementation to disparities in psychosocial indicators.


Assuntos
Comportamento , COVID-19/epidemiologia , Transmissão de Doença Infecciosa/prevenção & controle , Pandemias/prevenção & controle , Cooperação do Paciente/psicologia , Equipamento de Proteção Individual , SARS-CoV-2 , Adulto , COVID-19/psicologia , COVID-19/transmissão , China/epidemiologia , Estudos Transversais , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Autorrelato
5.
Food Funct ; 11(1): 628-639, 2020 Jan 29.
Artigo em Inglês | MEDLINE | ID: mdl-31894808

RESUMO

Enzymatic cross-linking is frequently used in bio-processing of dairy products since it could change the physiochemical and functional characterization. In our study, bovine α-lactalbumin was cross-linked by polyphenol oxidase from Agaricus bisporus and the changes in the structure, digestibility and allergenicity of α-lactalbumin were explored after cross-linking, and the structural alterations of the polymers were analyzed by circular dichroism spectroscopy, ultraviolet absorption spectroscopy and fluorescence spectroscopy. The digestibility of cross-linked α-lactalbumin was evaluated by simulated digestion in vitro. After that, the allergenicity of α-lactalbumin polymers was evaluated by detection of the specific IgE binding ability using an animal model. The results showed that the secondary and tertiary structures of various α-lactalbumin polymers exhibited a significant variation compared with those of untreated α-lactalbumin, and the cross-linked α-lactalbumin was relatively less susceptible to digestion. Moreover, the allergenicity of cross-linked polymers decreased significantly. These results suggested that there was a direct correlation between a loss of an α-helix and IgE binding to α-lactalbumin, which indicated that enzymatic cross-linking might be an efficient approach to reduce the allergenicity of bovine α-lactalbumin.


Assuntos
Alérgenos/química , Alérgenos/imunologia , Lactalbumina/química , Lactalbumina/imunologia , Agaricus/enzimologia , Alérgenos/genética , Animais , Sítios de Ligação , Catecol Oxidase/química , Bovinos , Feminino , Proteínas Fúngicas/química , Imunoglobulina E/química , Imunoglobulina E/imunologia , Lactalbumina/genética , Camundongos , Camundongos Endogâmicos BALB C , Polímeros/química , Estrutura Secundária de Proteína
6.
Food Chem ; 281: 130-139, 2019 May 30.
Artigo em Inglês | MEDLINE | ID: mdl-30658739

RESUMO

The effect of processing on allergenicity of peanut, a major allergic food remains uncertainty. To discover the influence of thermal processing, extraction and assessment methods on potential allergenicity, protein was extracted by three methods or digested in the form of defatted peanut powder (DPP). The components of extracted allergens were analyzed using electrophoresis and mass spectrometry; the advanced structures (the secondary structure and the tertiary structure) were characterized through spectroscopies; the potential allergenicities were assessed by enzyme linked immunosorbent assay (ELISA), Biolayer interferometry (BLI) and KU812 cell degranulation assay. Results demonstrated that extraction influenced the allergenicity assessment significantly, and the assessment method was also important. The potential allergenicity of protein changed after processing, it increased after roasting, while decreased after boiling. Additionally, digested DPP combined with basophilic granulocyte degranulation model might be a good allergenicity assessment method.


Assuntos
Alérgenos/química , Arachis/imunologia , Manipulação de Alimentos , Proteínas de Plantas/química , Alérgenos/imunologia , Linhagem Celular Tumoral , Dicroísmo Circular , Temperatura Alta , Humanos , Hipersensibilidade a Amendoim/imunologia , Hipersensibilidade a Amendoim/prevenção & controle , Proteínas de Plantas/imunologia , Pós/química
7.
Bull Environ Contam Toxicol ; 100(5): 634-640, 2018 May.
Artigo em Inglês | MEDLINE | ID: mdl-29546499

RESUMO

Heavy metal are often added to animal fodder and accumulate in the soils with swine manure. In this study, heavy metal (Cu, Pb, Cd, Zn, As and Cr) concentrations were determined in agricultural soils irrigated with swine manure in Jiangxi Province, China. Results showed that the average concentrations of Cu, Zn, As and Cr (32.8, 93.7, 21.3 and 75.8 mg/kg, respectively) were higher than the background values, while Pb and Cd (15.2 and 0.090 mg/kg, respectively) were lower than the background values. Contamination factors [Formula: see text] indicated that they were generally moderate for Cu, Zn, As and Cr and generally low for Pb and Cd. The contamination degree (C d ) was calculated to be 7.5-10.0 indicating a moderate degree of contamination. The geoaccumulation index (Igeo) indicated that the soils were unpolluted with Zn, Cd and Pb, while unpolluted to moderately pollute with Cr, Cu and As. The single ecological risk factor [Formula: see text] revealed that the six heavy metals all belonged to low ecological risk. The ecological risk indices suggested that all the sampling sites were at low risk level.


Assuntos
Monitoramento Ambiental , Esterco/análise , Metais Pesados/análise , Poluentes do Solo/análise , Solo/química , Agricultura/métodos , Animais , China , Ecologia , Metais Pesados/toxicidade , Medição de Risco , Suínos , Verduras
8.
J Sci Food Agric ; 96(10): 3567-74, 2016 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-26597340

RESUMO

BACKGROUND: Peanut is one of the eight major food allergens. Its allergen, Ara h 2, can be recognized by over 90% of serum IgE samples from peanut-allergic patients. Therefore, reducing the allergenicity of Ara h 2 is especially important. RESULTS: In the present study, polyphenol oxidase (PPO), a protein cross-linking reaction catalyst that acts on tyrosine residue, was used to modify Ara h 2. After crosslinking, the microstructure, digestibility, IgG binding capability and IgE binding capability of Ara h 2 were analyzed. Cross-linking decreased the potential allergenicity of Ara h 2 by masking the allergen epitope, while the antigenicity of Ara h 2 changed slightly. After crosslinking, the apparent diameter of Ara h 2 was altered from 300 to 1700 nm or 220 nm, indicating that polymerization could either be inter- or intramolecular. Regarding digestibility, crosslinked Ara h 2 was relatively more easily digested by gastric fluid compared with the untreated Ara h 2, but much more difficult in the intestinal fluid. CONCLUSION: The crosslinking reaction catalyzed by PPO, as a non-thermal process, may be beneficial for avoiding food allergy. The reaction could mask allergen epitopes, decreasing the allergenicity of Ara h 2. © 2015 Society of Chemical Industry.


Assuntos
Albuminas 2S de Plantas/imunologia , Albuminas 2S de Plantas/metabolismo , Antígenos de Plantas/imunologia , Antígenos de Plantas/metabolismo , Arachis/imunologia , Arachis/metabolismo , Catecol Oxidase/metabolismo , Glicoproteínas/imunologia , Glicoproteínas/metabolismo , Albuminas 2S de Plantas/química , Alérgenos/química , Alérgenos/imunologia , Alérgenos/metabolismo , Antígenos de Plantas/química , Digestão , Epitopos , Glicoproteínas/química , Humanos , Imunoglobulina E/química , Ligação Proteica , Estrutura Secundária de Proteína
9.
Food Chem ; 196: 459-65, 2016 Apr 01.
Artigo em Inglês | MEDLINE | ID: mdl-26593515

RESUMO

Peanut (Arachis hypogaea) is among the eight major food allergens in the world. Several attempts have been made to decrease or eliminate the allergenicity of peanut. Systemic screening of thousands of peanut cultivars may identify peanut with low allergenicity. In this study, the allergen compositions of 53 Chinese peanut cultivars were characterized, and their allergenicity to sera IgE of Chinese patients and in a mouse model was assessed. Contents of total protein and allergens were quantified by SDS-PAGE and densitometry analysis on gel. Although the contents of allergens broadly varied among cultivars, they were related to one another. The IgE binding capacity of cultivars was tested by ELISA, and their allergenicity was further evaluated in a mouse model by oral sensitization. Results showed that the allergenicity of peanut was affected by allergen composition rather than a single allergen. Peanut cultivars with low allergenicity may contain more Ara h 3/4 (24 kDa), Ara h 2 and less Ara h 3/4 (43, 38, and 36 kDa), Ara h 6. Screening based on allergen composition would facilitate the identification of low-allergenic peanut.


Assuntos
Alérgenos/análise , Arachis/imunologia , Hipersensibilidade a Noz/diagnóstico , Proteínas de Plantas/imunologia , Alérgenos/imunologia , Animais , Arachis/química , Povo Asiático , Células Cultivadas , Modelos Animais de Doenças , Eletroforese em Gel de Poliacrilamida , Ensaio de Imunoadsorção Enzimática , Feminino , Humanos , Imunoglobulina E/imunologia , Camundongos , Camundongos Endogâmicos BALB C , Proteínas de Plantas/química
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