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1.
Bull Environ Contam Toxicol ; 106(6): 978-982, 2021 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-34021770

RESUMO

Juvenile common carp were treated with Cd2+ at a sublethal concentration for Cyprinidae (6.4 mg/L). The expression of N-methyl-D-aspartate receptor subunit genes (NR2A, NR2B) and ATP-binding cassette subfamily C member 1 gene (ABCC1) was compared between treated and untreated fish. In addition, cadmium accumulation in the fish tissues was assessed. NR2A was 18.9-fold upregulated by Cd2+ in the eyes (choroid + retina), which accumulated Cd, and was not upregulated in brain, which didn't accumulate Cd. This may have been caused by the blocking of calcium channels by Cd2+, which has a very similar ionic radius to that of Ca2+. ABCC1 was 2.6-fold upregulated in gills and was not upregulated in liver; both tissues accumulated high levels of Cd. This difference may have been caused by the accumulation of predominantly previously inactivated Cd in liver or by some difference in the mechanisms of self-detoxification from Cd2+ in fish gills and liver.


Assuntos
Carpas , Poluentes Químicos da Água , Animais , Cádmio/metabolismo , Cádmio/toxicidade , Carpas/genética , Brânquias/metabolismo , Fígado/metabolismo , Distribuição Tecidual , Poluentes Químicos da Água/metabolismo , Poluentes Químicos da Água/toxicidade
2.
J Asthma ; 54(1): 46-52, 2017 01 02.
Artigo em Inglês | MEDLINE | ID: mdl-27286421

RESUMO

OBJECTIVE: The programmed death-1 receptor, PD-1, is a negative regulator of T-cell activation. The PD-1.3 polymorphism of the PD-1 gene (PDCD1) has been previously shown to be associated with several autoimmune and inflammatory disorders including systemic lupus erythematosus and multiple sclerosis. We examined for the first time PD-1.3 association with another inflammatory disease with strong immune component, IgE-mediated bronchial asthma, its severity and its biochemical markers (total serum IgE and IL-4). METHODS: PD-1.3 G/A was genotyped by PCR-RFLP analysis using two different populations: Caucasian (492 Russian individuals) and Asian (276 Buryat individuals). RESULTS: We found a significant association of the PD-1.3 polymorphism with IgE-mediated bronchial asthma and total serum IgE level in the Russian population. Combined genotype AA+AG was correlated with risk of developing allergic bronchial asthma (OR = 1.78, 95% CI 1.13-2.78, p = 0.011) and lower concentrations of total serum IgE (p = 0.001) compared with the wild-type genotype GG. However, PD-1.3 was not polymorphic in the Buryat population. CONCLUSIONS: PD-1.3 polymorphism of the PD-1 gene (PDCD1) may contribute to the development of allergic asthma in the Russians but not in the Buryats. Our results could be helpful for a better understanding of the effect of this polymorphism on the development of diseases with strong immune components.


Assuntos
Povo Asiático/genética , Asma/etnologia , Asma/genética , Imunoglobulina E/sangue , Receptor de Morte Celular Programada 1/genética , População Branca/genética , Adulto , Asma/imunologia , Feminino , Frequência do Gene , Genótipo , Humanos , Hipersensibilidade/genética , Mediadores da Inflamação/metabolismo , Masculino , Pessoa de Meia-Idade , Polimorfismo de Fragmento de Restrição , Testes de Função Respiratória , Federação Russa/epidemiologia , Índice de Gravidade de Doença , Sibéria/epidemiologia
3.
J Alzheimers Dis ; 36(4): 633-6, 2013.
Artigo em Inglês | MEDLINE | ID: mdl-23645095

RESUMO

The interaction of the 16-mer synthetic peptide (Aß16), which represents the metal-binding domain of the amyloid-ß with DNA, was studied employing the surface plasmon resonance technique. It has been shown that Aß16 binds to the duplex DNA in the presence of zinc ions and thus the metal-binding domain can serve as a zinc-dependent DNA-binding site of the amyloid-ß. The interaction of Aß16 with DNA most probably depends on oligomerization of the peptide and is dominated by interaction with phosphates of the DNA backbone.


Assuntos
Peptídeos beta-Amiloides/metabolismo , DNA/metabolismo , Fragmentos de Peptídeos/metabolismo , Zinco/metabolismo , Animais , Sítios de Ligação/fisiologia , Humanos
4.
Biosens Bioelectron ; 24(4): 831-6, 2008 Dec 01.
Artigo em Inglês | MEDLINE | ID: mdl-18755579

RESUMO

A novel electrochemical method for the detection of bioaffinity interactions based on a gold-nanoparticles sensing platform and on the usage of stripping voltammetry technique was developed. The oxidation of gold surface (resulted in gold oxide formation) upon polarization served as a basis for analytical response. As a model, thrombin-thrombin binding aptamer couple was chosen. The aptamer was immobilized on a screen-printed electrode modified with gold-nanoparticles by avidin-biotin technology. Cathodic peak area was found proportional to thrombin quantity specifically adsorbed onto electrode surface. Sigmoid calibration curve as is typical for immunoassay was obtained, with thrombin detection limit of 10(-9)M. Linear range corresponds from 10(-8) to 10(-5)M thrombin concentration or 2 x 10(-14) to 2 x 10(-11)mol/electrode (R=0.996). Binding of thrombin to an aptamer has also been detected using the ferricyanide/ferrocyanide redox couple as electrochemical indicator.


Assuntos
Aptâmeros de Peptídeos/química , Técnicas Biossensoriais/instrumentação , Eletroquímica/instrumentação , Imunoensaio/instrumentação , Nanopartículas/química , Mapeamento de Interação de Proteínas/métodos , Trombina/análise , Trombina/química , Aptâmeros de Peptídeos/análise , Técnicas Biossensoriais/métodos , Eletroquímica/métodos , Desenho de Equipamento , Análise de Falha de Equipamento , Ouro/química , Nanopartículas/ultraestrutura , Tamanho da Partícula , Reprodutibilidade dos Testes , Sensibilidade e Especificidade
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