earticle

영어

Autoantibody is the principal mediators of autoimmune disease. IVIG is a milestone of the therapy of autoimmune disease. Recently, it has been reported that sialylation on Fc doamin of immunogloublin is critical for the effect of intravenous immunoglobulin (IVIG) and seems to be mediated by lectins which are expressed on splenic marginal zone macrophages. And they demonstrated that SIGN-R1 preferentially binds to 2,6-sialylated Fc compared with similarly sialylated, biantennary glycoproteins, thus suggesting that a specific binding site is created by the sialylation of IgG Fc. Moreover, it was showed that a human homologue of SIGN-R1, DC-SIGN, displays a similar binding specificity to SIGN-R1 but differs in its cellular distribution, potentially accounting for some of the species differences observed in IVIG protection.
However, the function of DC-SIGN in IVIG effects is controversial now, given that DC-SIGN and alpha2,6-sialylated IgG Fc interaction is dispensable for the anti-inflammatory activity of IVIg on human dendritic cells. Therefore, further studies of SIGN-R1-mediated IVIG effect could identify the IVIG-mediated intracellular signaling and the unknown anti-inflammatory factors, leading to unravel the specific mechanism of autoimmune diseases. These studies could be applied to develop the new therapies or new drug candidates by using sialylated SIGN-R1 ligands which mimic the IVIG effect to cure several auto-immune disease.