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PubMed2000

Mode of molecular recognition of L-fucose by fucose-binding legume lectins.

Recognition of cell surface carbohydrate moieties by lectins plays a vital role in many a biological process. Fucosyated residues are often implicated as key recognition markers in many cellular processes. In particular, the aspects of molecular recognition of fucose by fucose-bindinglectins UEA 1 and LTA pose a special case because no crystal structure of these lectins is available. The study was conducted to elucidate the process of recognition of l-fucose by UEA1 and LTA by correlating structure-based sequence alignment and other available biochemical/biophysical data. The study points out that the mode of recognition of l-fucose is coordinated by the invariant triad of residues the asparagine 137, glycine 105, and aspartate 87. The major hydrophobic stacking residue in this case is the tyrosine 220. The study also reiterates the key role of the conserved triad of residues in the combining site which is a common feature for all legume lectins whose crystal structures are known.

Amino Acid Sequence↗
PubMed2000

Taxonomic significance of fucose in the class Urediniomycetes: distribution of fucose in cell wall and phylogeny of urediniomycetous yeasts.

The carbohydrate compositions of cell wall were determined in the strains of class Urediniomycetes, mainly ballistoconidium-forming yeasts and related taxa. The major component of cell wall was mannose, and glucose was included as the second component, but xylose was not detected in any strain. Out of 41 strains examined, 39 contained galactose, 14 contained arabinose and 12 contained rhamnose. As a minor component, fucose was detected in 30 strains but not in 11 strains. A phylogenetic tree based on 18S rDNA sequences indicated that the fucose-lacking strains, Erythrobasidium hasegawianum, Rhodotolura aurantiaca, R. lactosa, R. minuta, Sakaguchia dacryoidea, Sporobolomyces coprosmae, S. elongatus, S. folicola, S. gracilis, S. kluyverinielii and S. oryzicola, constituted a distinct cluster from those strains which contained fucose. This cluster corresponded to one of the five subclusters, the Erythrobasidium cluster, in the phylogenetic tree of class Urediniomycetes. The carbohydrate composition of cell wall is believed to reflect the phylogenetic relationships among basidiomycetous fungi. The presence or absence of fucose in cell wall should be regarded as an important phenotypic characteristic in the taxonomy of basidiomycetes.

Basidiomycota↗
PubMedDate not supplied

Protection by L-fucose and fucose-rich polysaccharides against ROS-produced cell death in presence of ascorbate.

It was shown previously, that millimolar concentrations of ascorbate have cytotoxic and anti-proliferative effects (Eur. J. Clin. Invest. 32 (2002) 372). With increasing concentrations of ascorbate an increasing number of fibroblasts was detached from the culture dish and shown to be lysed by the effect of ascorbate-induced generation of reactive oxygen species (ROS-s). It also could be shown, that this cytotoxic effect is partly due to the dose-dependent inhibition by ascorbate of fibronectin biosynthesis. Superoxide dismutase (SOD) and catalase were shown to salvage cells from ROS-induced cell-death by preventing the inhibition of fibronectin biosynthesis. We used this model system to test the cyto-protective effect of L-fucose and fucose-rich oligo- and polysaccharides (FROP-s). It appeared that relatively low concentrations of L-fucose and FROP-3 (Biomed. Pharmacother. in press) could efficiently protect fibroblasts from the ascorbate-induced cell-death. These novel pharmacological properties of L-fucose and FROP-3 might well be related to their accelerating effect of wound healing.

Antioxidants↗
PubMedDate not supplied

Effect of L-fucose and fucose-rich oligo- and polysaccharides (FROP-s) on skin aging: penetration, skin tissue production and fibrillogenesis.

Skin thickness is decreasing with age. This loss concerns both dermis and epidermis, cells and extracellular matrix. We could show here that percutaneous application of an L-fucose-containing preparation produced an increase of skin thickness and a densification of collagen bundles. We also could show that 3H-L-fucose penetrates in the dermis, a prerequisite for the above mentioned favorable pharmacological activities. These results, together with the previous favorable activities on the downregulation of matrix-degrading enzymes, free radical scavenging and increased cell proliferation confirm the favorable action of fucose and fucose-rich polysaccharides (FROP-s) on the skin by slowing down its aging.

Administration, Topical↗
PubMed1994

Ligand size is a major determinant of high-affinity binding of fucose- and galactose-exposing (lipo)proteins by the hepatic fucose receptor.

Previous in vivo studies have demonstrated that small galactose-exposing particles are preferentially internalized by the asialoglycoprotein receptor on the parenchymal liver cell and large particles by the galactose-particle receptor on the Kupffer cell. In this study, we have investigated using in vitro binding studies whether the affinity for either receptor is affected by the ligand size. The asialoglycoprotein receptor appeared to bind and process lactosylated proteins irrespective of their size. In contrast, recognition of galactose-exposing proteins by the galactose-particle receptor on the Kupffer cell was strongly dependent on size. The affinity increased 3000-fold with protein sizes increasing from 5 to 15 nm, reaching its maximum at approx. 1 nM for ligands larger than 15 nm. Apparently, the preferential in vivo uptake of large galactose-exposing ligands by Kupffer cells does not result from an inability of the parenchymal liver cells to internalize these ligands, but from the high affinity of large ligands for the galactose-particle receptor and the strategic anatomical localization of the Kupffer cells in the liver. In the preceding paper [Kuiper, Bakkeren, Biessen and Van Berkel (1994) Biochem. J. 299, 285-290] the galactose-particle receptor on the Kupffer cell was suggested to be identical with the fucose receptor. 125I-Lac-LDL-binding studies clearly showed that the galactose-particle receptor exhibited high-affinity binding of fucose-exposing proteins also. The affinity of fucosylated proteins for the galactose-particle receptor was greatly affected by ligand size. The above data strongly support the hypothesis that the galactose-particle receptor is identical with the fucose receptor. The size of neoglycoproteins can be appreciated as a new major determinant of affinity for the fucose receptor.

Animals↗
PubMed1993

N.m.r. spectroscopic studies of fucose-containing oligosaccharides derived from keratanase digestion of articular cartilage keratan sulphates. Influence of fucose residues on keratanase cleavage.

Keratan sulphate chains from bovine articular cartilage were fully digested with keratanase from Pseudomonas sp. and the products were reduced with alkaline borohydride. The resultant fragments were fractionated on a Nucleosil 5SB column and the earliest eluting fucose-containing oligosaccharides were isolated. Structural analysis using 1H n.m.r. spectroscopy (600 MHz) showed the two least-charged species to have the following structure: GlcNAc(6S) beta 1-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc(6S) beta 1- 3Gal beta 1-4GlcNAc(6S) beta 1-3Gal-ol and GlcNAc(6S) beta 1-3Gal beta 1- 4(Fuc alpha 1-3)GlcNAc(6S) beta 1-3Gal beta 1-4GlcNAc(6S) beta 1-6(Gal beta 1- 3)GalNAc-ol. Both galactoses adjacent to the fucosylated N-acetylglucosamine residue are unsulphated. Therefore, it can be deduced from these structures that the presence of fucose on N-acetylglucosamine residues in keratan sulphates protects both of the adjacent unsulphated galactose residues from keratanase cleavage. This result has implications for the interpretation of keratanase fingerprints, because in articular cartilage keratan sulphates the keratanase-resistant blocks are not solely those with fully sulphated galactose residues, but also include the fucosylated sequences, which have unsulphated galactoses. It is, therefore, not possible to estimate their galactose sulphation or the size of the fully sulphated disaccharide-repeat sequences from keratan sulphates that contain fucose.

Acetylglucosamine↗
PubMed1982

Analysis of lambda insertions in the fucose utilization region of Escherichia coli K-12: use of lambda fuc and lambda argA transducing bacteriophages to partially order the fucose utilization genes.

Escherichia coli K-12 strains have deletions for the normal lambda integration site were lysogenized with bacteriophage lambda at a site within the L-fucose utilization system (fuc). The frequency of lambda integration at this site is approximately 2 X 10(-8) to 5 X 10(-7). Studies of the lytic properties of these strains indicated very infrequent cell lysis with a relatively low phage burst size. Transductional ability of the phage lysates was found to be normal, comparable to that found in conventional low-frequency transducing lysates. Two major classes of transducing phage were found. One carried the markers argA and fucA (a fucose utilization gene of unknown function previously referred to as fuc-1) and the gene for D-arabinose utilization (dar+). The other carried only fucC, the gene specifying L-fuculose-1-phosphate aldolase. A minor class of phage was found that carried fucA, but not argA or dar+. Upon consideration of the transductional nature of these phage classes, we are proposing that the gene order for the L-fucose utilization system is dar, fucA, (lambda), fucC.

Aldehyde-Lyases↗
PubMed1994

Isolation and characterization of sets of anti-L-fucose and anti-bovine serum albumin antibodies directed against a glycoconjugate of L-fucose and bovine serum albumin.

A set of anti-carbohydrate antibodies and a set of anti-protein antibodies were isolated from the serum of rabbits immunized with a glycoconjugate of L-fucose and bovine serum albumin. The sets were separated by affinity chromatography by a two-column method on adsorbents with L-fucose or bovine serum albumin ligands. Isoelectrofocusing results showed that the anti-carbohydrate antibodies consisted of 11 molecular species and the anti-bovine serum albumin antibodies consisted of seven molecular species. The anti-carbohydrate antibodies are all of the IgG type while the anti-protein antibodies contain three types of globulin molecules, IgA, IgG, and IgM. The former antibodies should be useful as markers for unique glycoproteins of diseased cells and the latter antibodies may be useful for investigating the mechanism of simultaneous synthesis of three types of immunoglobulins.

Animals↗
PubMed2001

Identification and characterization of GDP-d-mannose 4,6-dehydratase and GDP-l-fucose snthetase in a GDP-l-fucose biosynthetic gene cluster from Helicobacter pylori.

In this study two open reading frames, namely HP0044 and HP0045 from H. pylori, were cloned and overexpressed in E. coli. The two recombinant proteins were demonstrated to have GDP-d-mannose 4,6-dehydratase (GMD) and GDP-l-fucose synthetase (GFS) activities, respectively. The recombinant GMD was a tetramer and had an optimum pH of 6.5. Exogenous NADP(+) was essential for its activity. The K(m) and K(cat) for GDP-d-mannose were 117.3 microM and 0.27 s(-1), respectively. The recombinant GFS was a homodimer with an optimum pH of 8.0. The K(m) and K(cat) for GDP-4-keto-6-deoxy-d-mannose were 64.08 microM and 0.75 s(-1), respectively. It can use both NADPH and NADH, but less efficient with the latter. Amino acid sequence alignment and phylogenetic analysis showed that H. pylori GFS was highly homologous to the GFS of E. coli O111 and both of them were located on a separate phylogenetic branch from other GFS. The unique clustering and origin of the two genes were also discussed.

Amino Acid Sequence↗
PubMed2004

l-Galactose replaces l-fucose in the pectic polysaccharide rhamnogalacturonan II synthesized by the l-fucose-deficient mur1 Arabidopsis mutant.

Arabidopsis thaliana mur1 is a dwarf mutant with altered cell-wall properties, in which l-fucose is partially replaced by l-galactose in the xyloglucan and glycoproteins. We found that the mur1 mutation also affects the primary structure of the pectic polysaccharide rhamnogalacturonan II (RG-II). In mur1 RG-II a non-reducing terminal 2- O-methyl l-galactosyl residue and a 3,4-linked l-galactosyl residue replace the non-reducing terminal 2- O-methyl l-fucosyl residue and the 3,4-linked l-fucosyl residue, respectively, that are present in wild-type RG-II. Furthermore, we found that a terminal non-reducing l-galactosyl residue, rather than the previously reported d-galactosyl residue, is present on the 2- O-methyl xylose-containing side chain of RG-II in both wild type and mur1 plants. Approximately 95% of the RG-II from wild type and mur1 plants is solubilized as a high-molecular-weight (>100 kDa) complex, by treating walls with aqueous potassium phosphate. The molecular mass of RG-II in this complex was reduced to 5-10 kDa by treatment with endopolygalacturonase, providing additional evidence that RG-II is covalently linked to homogalacturonan. The results of this study provide additional information on the structure of RG-II and the role of this pectic polysaccharide in the plant cell wall.

Arabidopsis↗
PubMed1994

Fucose and fucose-containing sugar epitopes enhance hippocampal long-term potentiation in the freely moving rat.

Male Wistar rats were intrahippocampally injected with L-fucose and the sugar epitope 2'-fucosyl-lactose prior to induction of long-term potentiation (LTP). Both substances had only a minimal and short-lasting depressive effect on the monosynaptically evoked field potential recorded in the dorsal blade of the dentate gyrus of freely moving rats upon stimulation of the perforant pathway. However, LTP induced by fractionated tetanization of the perforant pathway, which declined within 24 h in control animals injected with Lactose, remained at the initial level even 48 h after tetanization (difference to the control group significant with P < 0.01). The results support earlier findings which have indicated a participation of fucosylated macromolecules in the maintenance of LTP. Different molecular mechanisms concerning the effect of both substances and the significance of the data in elucidation of the relationship between LTP and memory formation are discussed.

Animals↗