Sialyl-di-Lewis a glycan epitope (Sialyl-di-Le^a)

Sialyl-di-Lewis a is a complex tumor-associated carbohydrate antigen (TACA) characterized by a sialylated and dimeric Lewis a structure (Fukushi et al., 1985, J Biol Chem). It is predominantly expressed on the surface of glycoproteins and glycolipids in various adenocarcinomas, including colorectal, pancreatic, and gastric cancers, while remaining largely absent in normal adult tissues (Kannagi, 2004, Glycoconj J). Biologically, it acts as a high-affinity ligand for E-selectin, a cell adhesion molecule on vascular endothelial cells, thereby playing a critical role in the hematogenous metastasis of cancer cells (Magnani, 2004, Arch Biochem Biophys). Due to its high tumor specificity and involvement in disease progression, Sialyl-di-Lewis a is a significant target for diagnostic imaging and immunotherapy. Therapeutic strategies include monoclonal antibodies, such as FH6, and glycan-based vaccines designed to trigger immune responses against cells expressing this epitope. Targeting this molecule aims to inhibit metastatic spread and induce immune-mediated destruction of tumor cells through mechanisms like antibody-dependent cellular cytotoxicity.

Other names

Sialyl-dimeric-Lewis aSialyl-Le^a-Le^aFH6 antigenSialyl-di-Le(a)

Binding to the carbohydrate epitope to facilitate immune-mediated cell lysis and block E-selectin-mediated adhesion to endothelial cells.