3'-O-sialylated and 3'-O-sulfated β-galactoside glycans

3'-O-sialylated and 3'-O-sulfated β-galactoside glycans are a specialized class of oligosaccharides that serve as essential recognition motifs in cell-cell adhesion processes, particularly within the vascular system (Varki et al., 2017) [1]. These glycans, which include well-characterized structures such as Sialyl Lewis X (sLeX) and Sialyl Lewis A (sLeA), are defined by the presence of sialic acid or sulfate groups at the 3' position of a terminal β-galactose residue (Yago et al., 2010) [2]. Their primary biological role is to act as high-affinity ligands for the selectin family of adhesion molecules (E-, P-, and L-selectin), mediating the initial "rolling" phase of the leukocyte adhesion cascade during inflammation (Magnani, 2012) [3]. In pathological contexts, these glycans are frequently upregulated on the surface of cancer cells, where they facilitate metastasis by allowing tumor cells to adhere to the vascular endothelium and extravasate into distant tissues (Witz, 2008) [4]. Therapeutic strategies targeting this axis often utilize glycomimetics, such as uproleselan, which are small molecules designed to mimic these glycan structures and competitively inhibit their binding to selectins, thereby disrupting pathological adhesion in conditions like acute myeloid leukemia and sickle cell disease (GlycoMimetics, 2024) [5].

Other names

Sialyl Lewis XsLeXSialyl Lewis AsLeA3'-sulfo-Lewis XSelectin ligandsSulfated sialyl-Lewis X

Competitive inhibition of selectin-ligand interactions by mimicking the glycan structure