IMR Press / FBL / Volume 13 / Issue 9 / DOI: 10.2741/2946

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 as a courtesy and upon agreement with Frontiers in Bioscience.

PsL-EGFmAb inhibits the stimulatory functions of human dendritic cells via DC-SIGN
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1 Department of Nephrology, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, 197 Rui jin Er road, Shanghai 200025, China
2 Shanghai Institute of Immunology and Institute of Health Sciences, Shanghai Jiao Tong University School of Medicine and Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 227 South Chongqing Road, Shanghai 200025, China

*Author to whom correspondence should be addressed.

Front. Biosci. (Landmark Ed) 2008, 13(9), 3525–3532;
Published: 1 May 2008

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.

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