Terminal alpha-L-fucose residues on glycoconjugates

Terminal alpha-L-fucose residues on glycoconjugates are carbohydrate moieties found at the non-reducing ends of glycoproteins and glycolipids (NCBI, Glycobiology 3rd edition). These residues are primarily processed by the enzyme alpha-L-fucosidase (FUCA1), which cleaves the fucose from the glycan chain (UniProt P04066). In biological systems, these residues play critical roles in cell-cell recognition, adhesion, and inflammation, notably as components of Lewis antigens and blood group determinants (PubMed PMID: 22421014). In pathological states, such as cancer, aberrant fucosylation leads to the overexpression of these terminal residues, which can promote tumor progression and metastasis (PubMed PMID: 28651550). Consequently, these residues serve as important biomarkers, such as AFP-L3 in liver cancer, and are targeted by therapeutic agents like lectins or monoclonal antibodies designed to disrupt their signaling or mediate immune-directed cell killing (PubMed PMID: 15585614, 15897564). In the context of the rare genetic disorder fucosidosis, the inability to degrade these substrates leads to their toxic accumulation in lysosomes (NCBI, GeneReviews). Therapeutic interventions also include small molecule inhibitors that prevent the synthesis of these fucose-containing glycans to reduce tumor growth (PubChem CID 445130). Overall, these terminal residues represent a significant class of glycan targets with broad implications in diagnostics and targeted therapy.

Other names

Fucosylated glycansAlpha-L-fucose epitopesFucosylated glycoconjugatesTerminal fucoseLewis antigens (subset)

Enzymatic hydrolysis of terminal alpha-L-fucose linkages; competitive binding to fucose-containing epitopes to block cell adhesion; inhibition of fucosyltransferases to prevent substrate synthesis.