Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.
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Dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) is a DC-specific C-type lectin that plays an important role in recognizing and capturing pathogens, DC migration and initiation of T cell responses. Here, we show that anti-P-selectin lectin-EGF domain monoclonal antibody (PsL-EGFmAb), originally prepared for blockade of the adhesive molecule P-selectin, significantly down-regulated DC-SIGN expression as well as expression of mature DC-related molecules including CD83, CD86 and CD80 on human DCs. This PsL-EGFmAb treatment of DCs resulted in impaired allogeneic T cell proliferation and IL-12 production. Furthermore, we show that PsL-EGFmAb-induced down-regulation of DC-SIGN may inhibit NF-kappaB expression in DCs, which accounts for the inhibition of DC maturation and stimulatory function. Our present studies indicate that PsL-EGFmAb may be a useful reagent for regulating DC-SIGN expression and DC function.