Disease relevance of fucose

• Glycoproteins binding to Ulex europaeus agglutinin-I (UEA-I) lectin, which recognizes the terminal alpha-L-fucose residue, were analyzed in 18 cases of human colorectal carcinoma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by the Western blotting method [1].
• Ulex europeus (Ulex 1) has been used to study the expression of cell surface alpha-L-fucose on oral epithelial cells of normal human mucosa, white lesions and carcinomas [2].
• Suppression of allergic contact dermatitis by alpha-L-fucose [3].
• Alpha-L-fucose: a potentially critical molecule in pathologic processes including neoplasia [4].
• The observation that UEA-I showed a strong staining reaction in mucus-producing adenocarcinomas, such as goblet cell and bronchial gland cell types, indicates that localization of alpha-L-fucose may be a specific carbohydrate from non-mucus-producing pulmonary adenocarcinomas [5].

High impact information on fucose

• In this report, we show that a monosaccharide, alpha-L-fucose, significantly enhances the cytolytic capacity of MLC-induced or preincubated effector cells [6].
• To target the sialylic residues on murine enterocytes, we functionalized microspheres with wheat germ agglutinin (WGA) and, to target alpha-L-fucose on M cells, with a lectin from Aleuria aurantia (AAL), the orange peel mushroom [7].
• Sugar receptors on melanocytes are mainly specific for alpha-L-fucose [8].
• Treatment of spermatozoa with alpha-L-fucose, fucoidan, or p-aminophenyl fucoside also reduced sperm attachment when compared to Millipore-filtered artificial seawater controls [9].
• Additionally, the occurrence of alpha-L-fucose in the goblet cells of chub, grass carp and sneep was confirmed [10].

Chemical compound and disease context of fucose

• The crystal structure of a fucose-binding lectin from the bacteria Pseudomonas aeruginosa in complex with alpha-L-fucose has been recently determined [11].

Biological context of fucose

• Current results suggest that alpha-L-fucose provides the essential structure that enables carbohydrate ligands to bind to selectins and to carbohydrate counterligands and thereby alter cellular homeostasis [4].
• Characterization of a new alpha-L-fucosidase isolated from the marine mollusk Pecten maximus that catalyzes the hydrolysis of alpha-L-fucose from algal fucoidan (Ascophyllum nodosum) [12].
• Twenty non-neoplastic parotid glands (removed during neck dissection for regional tumours) were examined for cellular and subcellular binding sites of Ulex europaeus-lectin I (UEA-I), a lectin reported to be specific for alpha-L-fucose [13].
• We investigate here the change in exposure of surface alpha-L-fucose residues during thymocyte and P815 cell apoptosis [14].
• RESULTS: The 4-copy gallic acid construct inhibited UEA1 binding to Caco-2 cell membranes with an IC50 of 3 microM, a 650- to 5000-fold increase over the natural UEA1 substrate alpha-L-fucose [15].

Anatomical context of fucose

• Our previous studies have shown that the monosaccharide alpha-L-fucose significantly enhances the cytolytic capacity of peripheral blood mononuclear leukocytes (PBMLs) [16].
• Lotus tetragonolobus agglutinin, another lectin specific for some alpha-L-fucose-containing moieties failed to react with endothelial cells [17].
• UEA-I, specific for alpha-L-fucose, bound slightly to rat and not to guinea-pig myocytes [18].
• In another series of experiments tumor cells were treated with alpha-L-fucosidase prior to co-cultivation with macrophages to determine whether the presence of alpha-L-fucose on the tumor cell surface had any effect on macrophage mediated cytotoxicity [19].
• In addition, due to the lack of terminal alpha-L-fucose, the alpha-D-N-acetyl-galactosamine and alpha-D-galactose residues cannot be transferred to the plasma membranes and, therefore, the antigens for blood groups A and B remain incomplete in psoriatic epidermis [20].

Associations of fucose with other chemical compounds

• At pH 5.0, a specific binding of the fluorescein-labelled neoglycoprotein bearing alpha-L-fucose was observed [21].
• This inhibition was relieved by alpha-L-fucose but not by alpha-D-fucose and reduced after treatment with alpha-L-fucosidase [22].
• After incubation of human monocyte-derived macrophages with alpha-L-fucosidase, a glycosidase which splits terminal alpha-L-fucose from oligosaccharides, the macrophages were no longer able to respond to lipopolysaccharide (LPS) [19].
• The pre-implantation blastocysts of both pig and sheep, throughout the period studied, had a continuous reaction for alpha-L-fucose, which has been suggested to be important in compaction and the expression of SSEA-1 antigen in mouse embryos [23].
• The epithelial cells and luminal secretion of the caprine ceruminous glands contained large amounts of neutral and smaller amounts of acidic glycoconjugates with different terminal sugars (alpha- d-mannose, alpha-L-fucose, alpha-N-acetyl-D-galactosamine, beta-D-galactose, beta-N-acetyl-D-glucosamine, and N-acetyl-neuraminic acid) [24].

Gene context of fucose

• We conclude that targeting allergens to alpha-L-fucose-receptor bearing cells using AAL-microspheres induces specific Th1-antibody responses possibly counteracting Th2-dominated allergy, and therefore provides a potentially useful formulation for oral immunotherapy [25].
• Human leucocyte migration inhibitory factor (LIF) was subjected to affinity column chromatography on Sepharose-bound alpha-L-fucose [26].
• Following the addition of alpha-L-fucose to the running buffer adsorbed lymphokine was eluted almost quantitatively [26].
• Lectin cytochemistry analysis of the egg surface indicated that alpha-L-fucose terminal residues are present on the chorion with a strongly polarized localization on the micropyle [27].
• Incubation of UEA1-coated microspheres with alpha-L-fucose reduced M-cell binding to a level comparable with BSA-coated microspheres [28].

Analytical, diagnostic and therapeutic context of fucose

• The alpha-l-fucose-specific lectin Ulex europaeus agglutinin I was utilized both in lectin blotting and in affinity chromatography and cross-reacted with the 200- and 270/260-kDa bands [29].
• We constructed alpha-L-fucose-targeting particles for oral immunotherapy of IgE-mediated allergy [25].
• Extracts of R lupini obtained by disrupting a bacterial pellet through a French press were stabilized at pH 5.6 by gel filtration and purified to homogeneity by affinity chromatography on Agarose A4 substituted with alpha-L-fucose [21].
• Therefore, our results suggest that alpha-L-fucose participates in the nucleation and immobilization of heavy metals in P. gymnospora cell walls [30].

References