Mucins are characterized by their extensive and dense array of carbohydrates. The carbohydrate linkages are primarily O-linked with sulfated core groups, termed sialyl Lewis x (sLex). The mucins characterized to date are primarily selectin counter-receptors. L-Selectin binds to at least four distinct mucins: GlyCAM-1, MAdCAM-l, CD34, and a poorly characterized protein called Sgp200. As men-

tinned previously, MAdCAM-1 has both Ig domains and a mucin domain, allowing it to bind to both an integrin (a407) and a selectin (L-selectin). GlyCAM-1 is somewhat unique in that it lacks a transmembrane domain. PSGL-1 binds both E- and P-selectin, although additional ligands have been described for each of these selectins. The E-selectin ligand ESL-1 appears to require N-linked carbohydrate structures rather than the typical O-linked sialomucin structures. The CLA antigen also binds to E-selectin and is expressed on a subset of memory T cells that preferentially migrate to the skin. The protein backbones of mucins are also postulated to play a role in binding specificity.

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