원문정보
초록
영어
The thiol-disulfide oxidoreductase thioredoxin-1 (TRX) is known to be secreted by leukocytes and to exhibit cytokine-like properties. Extracellular effects of TRX require a functional active site, suggesting a redox-based mechanism of action.
However, specific cell surface proteins and pathways coupling extracellular TRX redox activity to cellular responses have not been identified so far. We first found that exogenous TRX not only scavenger but also effected intracellular proteins using proteomic approaches. Therefore, the effect of a thiol-antioxidant protein TRX have appropriated on regulation in a human skin malignant melanoma cell line (A375). Mechanism-based Histidine pull down and immunoprecipitation technique used to identify TRX binding partner proteins. We found that up/down regulated intracellular proteins were identified under the condition of LPS-treated A375
cells and co-treat with exogenous TRX using in vitro 2-DE proteomic approaches.
As well as, confirmed in vivo mouse inflammation models used to quantitatively measure IL-6, IL-10, MCP-1 and TNF protein levels in serum samples. Our studies demonstrate that exogenous TRX has anti-inflammatory properties and intracellular regulator activity in vivo and in vitro. These results have a therapeutic role in skin inflammation therapy.