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• W2030761520 abstract "<i>Background:</i> Interleukin (IL)-4 plays a prominent role in immune response. Mercuric compounds upregulate IL-4 expression in animal tissues, and this upregulation plays a role in mercuric-mediated immunomodulation. Mercuric ions-mediated IL-4 expression was observed in vitro in T lymphocytes and mast cells. In the present study, we investigated molecular mechanisms responsible for this effect of mercuric ions in mast cells. <i>Methods:</i> C1.MC/C57.1 mouse mast cells were exposed in vitro to increasing concentrations of Hg²⁺ in the absence or presence of the specific c-Jun N-terminal kinase (JNK) inhibitor SP600125. The level of phosphorylated c-Jun in mast cells was determined by Western blotting, JNK activity assessed with in vitro kinase assay and the amount of secreted IL-4 determined by ELISA. <i>Results:</i> We observed that Hg²⁺ upregulated c-Jun phosphorylation on Ser 73 at concentrations which overlapped concentrations mediating IL-4 secretion. Phosphorylation of c-Jun in mast cells was associated with an increase in JNK activity. The specific JNK inhibitor SP600125 abolished both mercuric-induced c-Jun phosphorylation and IL-4 secretion in mast cells. <i>Conclusions:</i> These observations are consistent with the hypothesis that JNK is one of the signaling proteins mediating the effect of Hg²⁺ on IL-4 expression in mast cells and is engaged in environmentally mediated immunomodulation." @default.
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• W2030761520 date "2005-01-01" @default.
• W2030761520 modified "2023-09-27" @default.
• W2030761520 title "c-Jun N-Terminal Kinase Is Involved in Mercuric Ions-Mediated Interleukin-4 Secretion in Mast Cells" @default.
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• W2030761520 doi "https://doi.org/10.1159/000083892" @default.
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