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Sulfated N-acetyllactosamine-containing glycans are specialized carbohydrate structures found on glycoproteins and glycolipids, characterized by the enzymatic addition of sulfate groups to the N-acetyllactosamine (Galβ1-4GlcNAc) disaccharide unit (Source: PubMed PMID: 15548591). These glycans serve as essential ligands for cell adhesion molecules, most notably L-selectin, which is crucial for the homing of lymphocytes to secondary lymphoid organs and the recruitment of leukocytes to sites of inflammation (Source: PubMed PMID: 15087621). The specific sulfation patterns, such as 6-O-sulfation on GlcNAc or Galactose, are mediated by specific sulfotransferases like CHST1 and CHST2 and are required for high-affinity recognition by lectin receptors (Source: UniProt O00204). In clinical contexts, these glycans are upregulated in chronic inflammatory conditions and various malignancies, facilitating pathological cell recruitment and tumor cell extravasation (Source: PubMed PMID: 16112223). Consequently, they are targeted by therapeutic agents designed to disrupt these interactions, such as selectin inhibitors and glycan-specific antibodies, to treat inflammatory disorders and prevent metastasis (Source: PubMed PMID: 28655140).
Competitive inhibition of selectin-ligand binding to prevent leukocyte adhesion and rolling.
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