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1.
Front Bioeng Biotechnol ; 11: 1261178, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-37790258

RESUMO

Nickel serves as an essential micronutrient for the human body, playing a vital role in various enzymatic processes. However, excessive nickel entering the environment can cause pollution and pose serious risks to animals, plants, and human health. High concentrations of nickel ions in the human body increase the risk of various diseases, highlighting the need for accurate measurement of nickel ions levels. In this study, we designed a sequence-specific cleavage probe for nickel (II) ion called SSC-Ni. Similar to the TaqMan probe, SSC-Ni is an off-on fluorescent probe with an exceptionally low background fluorescence signal. It exhibits high detection specificity, making it highly selective for nickel ions, and the detection limit of the probe towards Ni2+ is as low as 82 nM. The SSC-Ni probe can be utilized for convenient and cost-effective high-throughput quantitative detection of nickel ions in serum. Its user-friendly operation and affordability make it a practical solution. By addressing the lack of simple and effective nickel ion detection methods, this probe has the potential to contribute significantly to environmental monitoring and the protection of human health.

2.
Cell Mol Immunol ; 17(7): 741-752, 2020 07.
Artigo em Inglês | MEDLINE | ID: mdl-31388100

RESUMO

Recognition of viral dsRNA by Toll-like receptor 3 (TLR3) leads to the induction of downstream antiviral effectors and the innate antiviral immune response. Here, we identified the zinc-finger FYVE domain-containing protein ZFYVE1, a guanylate-binding protein (GBP), as a positive regulator of TLR3-mediated signaling. Overexpression of ZFYVE1 promoted the transcription of downstream antiviral genes upon stimulation with the synthetic TLR3 ligand poly(I:C). Conversely, ZFYVE1 deficiency had the opposite effect. Zfyve1-/- mice were less susceptible than wild-type mice to inflammatory death induced by poly(I:C) but not LPS. ZFYVE1 was associated with TLR3, and the FYVE domain of ZFYVE1 and the ectodomain of TLR3 were shown to be responsible for their interaction. ZFYVE1 was bound to poly(I:C) and increased the binding affinity of TLR3 to poly(I:C). These findings suggest that ZFYVE1 plays an important role in the TLR3-mediated innate immune and inflammatory responses by promoting the ligand binding of TLR3.


Assuntos
Proteínas de Membrana/deficiência , Transdução de Sinais , Receptor 3 Toll-Like/metabolismo , Dedos de Zinco , Animais , Endossomos/efeitos dos fármacos , Endossomos/metabolismo , Imunidade Inata/efeitos dos fármacos , Inflamação/patologia , Ligantes , Proteínas de Membrana/metabolismo , Camundongos Endogâmicos C57BL , Camundongos Knockout , Poli I-C/farmacologia , Ligação Proteica/efeitos dos fármacos , Transdução de Sinais/efeitos dos fármacos
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