Sulfated N-acetyllactosamine (slan)

Sulfated N-acetyllactosamine (LacNAc) is a post-translationally modified carbohydrate structure found on various glycoproteins and glycolipids. The most prominent form, 6-sulfo-LacNAc (commonly known as the slan epitope), serves as a specific marker for a proinflammatory subset of human dendritic cells and non-classical monocytes, termed slanDCs (PLOS ONE, 2013). These cells are major producers of proinflammatory cytokines such as TNF-alpha and IL-12 and are implicated in the pathogenesis of chronic inflammatory diseases, including multiple sclerosis, psoriasis, and rheumatoid arthritis (NIH, 2014). Sulfated LacNAc also acts as a critical ligand for L-selectin (CD62L), facilitating the recruitment of leukocytes to sites of inflammation and secondary lymphoid organs (Trends in Immunology, 2006). In oncology, slanDCs are found in the tumor microenvironment, where they can influence anti-tumor immune responses and mediate antibody-dependent cellular cytotoxicity (ADCC) (AACR, 2023). Therapeutic approaches targeting this molecule include the use of monoclonal antibodies like MDC8 and DD2 to deplete proinflammatory slanDCs or to utilize them for targeted antigen delivery in cancer vaccines (PLOS ONE, 2013). Additionally, aberrant sulfation of LacNAc on therapeutic proteins or as decoys in viral vaccines can impact drug efficacy and host immune responses (NIH, 2021).

Other names

6-sulfo-LacNAc6-sulfo-N-acetyllactosamine3-sulfo-LacNAc4-sulfo-LacNAcslan epitope6-sulfo-Gal-beta-1,4-GlcNAcSialyl 6-sulfo-LacNAc

Antibody-mediated depletion of proinflammatory slanDCs; Targeted antigen delivery to dendritic cells for vaccination; Inhibition of L-selectin-mediated leukocyte adhesion and recruitment.