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L-selectin ligands are a diverse group of glycosylated proteins and mucins, such as GlyCAM-1, CD34, and MAdCAM-1, that facilitate the initial attachment and rolling of leukocytes on the vascular endothelium (PMID: 15306663). These ligands are characterized by specific carbohydrate motifs, most notably 6-sulfo sialyl-Lewis X, which are recognized by the C-type lectin domain of L-selectin (CD62L) expressed on the surface of most circulating leukocytes (PMID: 11116172). This molecular interaction is a fundamental step in the homing of naive T-cells to peripheral lymph nodes through high endothelial venules (HEVs) and is critical for the recruitment of immune cells to sites of acute and chronic inflammation (PMID: 17182276). In pathological states, L-selectin ligands play a significant role in promoting excessive leukocyte infiltration in autoimmune diseases and facilitating the hematogenous metastasis of certain cancer cells that mimic leukocyte rolling mechanisms (PMID: 21679069). Therapeutic strategies targeting these ligands or their interactions with CD62L aim to modulate the inflammatory response by blocking the entry of leukocytes into tissues, thereby reducing tissue damage in conditions like rheumatoid arthritis and asthma (PMID: 16163365).
Competitive inhibition of the carbohydrate-binding lectin domain of L-selectin, preventing leukocyte tethering and rolling on the vascular endothelium.
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