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1.
Environ Monit Assess ; 195(12): 1446, 2023 Nov 10.
Artigo em Inglês | MEDLINE | ID: mdl-37946068

RESUMO

The translocation and accumulation patterns of polycyclic aromatic hydrocarbons (PAHs) in the soil-crop system have important implications for the fate of PAHs and human health. This study summarized the concentrations of 16 priority PAHs in the soils and various parts of mature winter wheat in China, sourced from a screening of previous literature in English and Chinese databases. The study analyzes the distribution characteristics, transfer patterns, and human health risks of PAHs in sites studied in Shaanxi, Henan, and Shandong provinces. The results showed that the concentrations of Σ16 PAHs in the rhizosphere soil of wheat ranged from 10.30 to 893.68 ng/g, in descending order of Shaanxi > Henan > average > Shandong. In sites with mild to moderate contamination (200 < Σ16 PAHs < 600 ng/g; i.e., Henan and Shaanxi), the concentration of Σ16 PAHs in the roots was higher than that in the stems or the grains, while in contamination-free sites (Σ16 PAHs < 200 ng/g; i.e., Shandong), the highest concentration of Σ16 PAHs was found in the stems. Generally, the concentrations of PAHs increased in the order of roots-stems-grains. The predominant PAHs in each part of wheat were 2- or 3-ring compounds, with five- or six-ring PAHs being more prevalent in wheat from Shanghe, Shandong. The bioaccumulation factors of different wheat parts from Shaanxi and Henan were consistently smaller than 1, and low- and medium-ring (2-4 rings) PAHs had bigger bioconcentration factors than high-ring (5-6 rings) PAHs. However, the accumulation of PAHs in the aboveground parts of wheat was larger than that in the underground parts of the Shandong sites. The linear regression relationship between the octanol-water partition coefficient and root concentration factor (RCF) of PAHs reflected that low and medium-ring PAHs were more easily absorbed by wheat roots than high-ring PAHs in Shaanxi and Henan. Our assessment of the health risks of oral wheat intake in adults and children by the incremental lifetime cancer risk (ILCR) model found a potential carcinogenic risk for both age groups in each province, with higher risks in adults than in children.


Assuntos
Hidrocarbonetos Policíclicos Aromáticos , Poluentes do Solo , Adulto , Criança , Humanos , Hidrocarbonetos Policíclicos Aromáticos/análise , Solo , Triticum , Ecossistema , Monitoramento Ambiental , Poluentes do Solo/análise , China , Medição de Risco
2.
Int Arch Allergy Immunol ; 182(3): 167-181, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-33378763

RESUMO

INTRODUCTION: Biological rhythm is inextricably linked to the physiological mechanisms of allergic diseases, but the exact mechanisms are still poorly understood. Clinical studies have reported rhythmic fluctuations in allergic diseases. The search for natural and harmless active ingredients based on biological rhythm with which to regulate allergic diseases is essential for the control of food allergy. METHODS: In this study, mice were treated at different time points to determine the link between the severity of allergic reactions and the circadian clock genes. The mice were treated with lentinan, either continuously or discontinuously, to assess their clinical symptoms, vascular permeability, immune cells, cytokines, and clock genes. Specifically, rat basophilic leukemia (RBL-2H3) cells were treated with lentinan and the rhythmic changes of cell degranulation were measured. RESULTS: The results in different models showed that the allergic reactions in mice treated at different time points were significantly different and thus related to fluctuations in biological rhythm. Treatment with lentinan was found to reduce the amplitude of changes in the clock genes, such as the activation of Per and Cry proteins in allergic mice, as well as to regulate biological rhythm in cells, inhibit the activation of Th2 cells, and alleviate allergic reactions. Furthermore, lentinan changed the rhythm of degranulation in RBL-2H3 cells. CONCLUSION: Lentinan was, therefore, determined to successfully alleviate allergic reactions by reducing the amplitude of changes in the body's biological rhythm, inhibiting the activation of Th2 cells, and affecting the immune microenvironment.


Assuntos
Hipersensibilidade/etiologia , Lentinano/farmacologia , Ativação Linfocitária/efeitos dos fármacos , Ativação Linfocitária/imunologia , Periodicidade , Células Th2/efeitos dos fármacos , Células Th2/imunologia , Animais , Biomarcadores , Degranulação Celular/efeitos dos fármacos , Degranulação Celular/genética , Degranulação Celular/imunologia , Relógios Circadianos/genética , Modelos Animais de Doenças , Suscetibilidade a Doenças , Expressão Gênica , Hipersensibilidade/diagnóstico , Hipersensibilidade/tratamento farmacológico , Hipersensibilidade/metabolismo , Camundongos , Índice de Gravidade de Doença , Células Th2/metabolismo
3.
J Agric Food Chem ; 57(21): 10357-62, 2009 Nov 11.
Artigo em Inglês | MEDLINE | ID: mdl-19886686

RESUMO

Glutaredoxins (Grxs) play important roles in the reduction of disulfides via reduced glutathione as a reductant. A cDNA (503 bp, EU193660) encoding a putative Grx was cloned from Taiwanofugus camphorata (Tc). The deduced amino acid sequence is conserved among the reported dithiol Grxs. A 3D homology structure was created for this TcGrx. To characterize the TcGrx enzyme, the coding region was subcloned into an expression vector pET-20b(+) and transformed into Escherichia coli . Functional TcGrx was expressed and purified by Ni(2+)-nitrilotriacetic acid Sepharose. The purified enzyme showed bands of approximately 15 kDa on 15% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The TcGrx encodes a protein possessing both Grx and dehydroascorbate reductase (DHAR) activity. The Michaelis constant (K(m)) values for beta-hydroxyethyl disulfide (HED) and dehydroascorbate (DHA) were 0.57 and 1.85 mM, respectively. The half-life of deactivation of the protein at 100 degrees C was 8.5 min, and its thermal inactivation rate constant K(d) was 6.52 x 10(-2) min(-1). The enzyme was active under a broad pH range from 6.0 to 10.0 and in the presence of imidazole up to 0.4 M. The enzyme was susceptible to SDS denaturation and protease degradation/inactivation.


Assuntos
Clonagem Molecular , Proteínas Fúngicas/química , Expressão Gênica , Glutarredoxinas/química , Oxirredutases/química , Polyporales/enzimologia , Estabilidade Enzimática , Proteínas Fúngicas/genética , Proteínas Fúngicas/isolamento & purificação , Proteínas Fúngicas/metabolismo , Glutarredoxinas/genética , Glutarredoxinas/isolamento & purificação , Glutarredoxinas/metabolismo , Cinética , Oxirredutases/genética , Oxirredutases/isolamento & purificação , Oxirredutases/metabolismo , Polyporales/química , Polyporales/genética , Processamento de Proteína Pós-Traducional
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