Lectins and also bacteria modify the glycosylation of gut surface receptors in the rat (original) (raw)
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Acta Histochemica, 1993
Seven recently isolated lectins were tested for their ability to bind to tissue sections of rat gut. Binding sites for N-Acetylgalactosamine specific lectins were found in mucins, in the brush border membrane and in goblet cells. Non-reducing terminal mannose residues were absent from cell surface membranes but were detected in the supranuclear region of goblet cells and enterocytes. The results of lectin binding obtained in this study were generally similar to lectin-gut interactions observed in vivo.
Lectin binding reveals divergent carbohydrate expression in human and mouse Peyer's patches
Histochemistry and Cell Biology, 1996
The nature of cell-associated carbohydrates in the human intestine that may mediate transepithelial transport of bacterial and dietary lectins and their processing by the lymphoid cells of Peyer's patches is not known. Because the cell surface carbohydrate receptors for lectins may vary in different species, the glycoconjugates of human and mouse follicle-associated epithelium and gut-associated lymphoid tissue were compared. A panel of 27, mainly recently isolated, lectins were used to identify glycoconjugate expression in M-cells, enterocytes, goblet cells, lymphocytes and macrophages in mouse and human intestine. Mouse M-cells were exclusively labelled by fucose-specific lectins but in human follicle-associated epithelium no distinct M-cell staining pattern was observed. In the human Peyer's patches,Bryonia dioica lectin bound selectively to paracortical T-lymphocytes andChelidonium majus lectin to germinal centre B-cells. Certain mannose-specific lectins (Galanthus nivalis, Hippeastrum hybrid) stained the tingible body macrophages in the germinal centre of human Peyer's patches but labelled the macrophages in the paracortical T-cell region of the mouse. The results indicate distinct differences in glycosylation between mouse and human Peyer's patches and their associated lymphoid cells. When considering cell surface glycoconjugates as target molecules for the gut immune system, care has to be taken to choose the appropriate lectin for each species.
Lectin binding to parietal cells of human gastric mucosa
Journal of Histochemistry & Cytochemistry, 1986
A light microscopic and ultrastructural analysis of lectin receptors on parietal cells from human gastric mucosa was performed utilizing 12 biotinylated lectins in conjunction with an avidin-biotin-peroxidase complex. Peanut agglutinin conjugated directly to peroxidase was also used. Several fixatives and fixation regimens were evaluated for optimal preservation of parietal cell saccharide moieties. Formalin proved to be the most practical fixative for light microscopic studies. A periodate-lysine-paraformaldehyde (PLP) combination provided good preservation of lectin binding capacity but yielded relatively poor ultrastructure. Conversely, glutaraldehyde provided excellent preservation of ultrastructure but a somewhat diminished lectin binding activity, which was overcome by using long incubation times and high concentrations of reagents. Parietal cells reacted strongly with Bandieraea simplicifolia, Dolichos biflorus, peanut agglutinin, and soybean agglutinin (all specific for gala...
Journal of Veterinary Medical Science, 2000
Composition of glycoconjugates were investigated in Escherichia coli 09:K103:NM, 987P + ST +-infected lower small intestines of 1-week-old pigs by the use of twenty one biotinylated-labelled lectins with avidin-biotin-peroxidase complex method. Piglets with experimental group were inoculated by feeding 5 ml of culture inoculum (5 × 10 9 colony-forming units/ml) with 15 ml of milk replacer. At the onset of diarrhea, experimental piglets and time-matched control piglets were euthanatized using electrocution, necropsied, and tested by lectin histochemistry. As compared with control, staining intensity of seven lectins altered in ileal villus brush border and goblet cells of pigs inoculated with the pathogen.
Glycoconjugate Journal, 1987
The display of carbohydrate structures was measured in promyelocytic HL60 cells and in histiocytic U937 cells induced to differentiate to phagocytic cells in vitro during three to seven days of cultivation in thepresence of dimethylsulfoxide (DMSO). it was assessed by micro-or spectrofluorometric quantification of the binding of fluorescent lectins. Changes in the cell size and the association and uptake of IgG-or complementopsonized yeast cells (Saccharomyces cerevisiae) were used as signs of phagocyte differentiation. The binding of wheat germ agglutinin (WGA), concanavalin A (Con A), Ricinus communis agglutinin-I (RCA-I) and Ulex europaeus agglutinin-I (UEA-I) varied due to the presence of DMSO during cultivation, and without DMSO also on the number of days in culture and the type of cell. Cell-cell recognition employs specific reciprocal protein-carbohydrate interactions, as well as non-specific hydrophobic and ionic forces. The recognition is reciprocal in the sense that lectin-like su bstances and corresponding carbohydrate receptors may occur either on bacterial I1-3] or on mammalian [4, 5] cell membranes; either way, cell-cell contact is promoted [5, 6 I. Different glycoconjugates have come into focus as receptor molecules for bacterial timbriae (pili) which bind specifically to different short oligosaccharides [2]. The role of mammalian lectins is particularly well-studied in different liver cells which show affinity for molecules and particles displaying mannose, galactose or fucose residues [7-9]. Lectin-like activity has also been identified as important recognition markers of malignant transformation I5,
Lectin–glycoconjugate interactions in health and disease
Biochemical Society Transactions, 2008
It is increasingly being acknowledged that complex carbohydrates mediate a huge variety of cellular interactions, permitting and regulating recognition and signalling events. This is achieved by the enormous range and complexity of branched structures in glycoconjugates and the ability of carbohydrate-binding proteins (lectins) to decipher this ‘glycocode’. Approx. 120 participants attended the 23rd International Lectin Meeting (Interlec-23) held at the Universities of Edinburgh (2 days) and Stirling (4 days) between 11 and 16 July 2008. These ‘Interlecs’ are truly international multi-disciplinary symposia, providing opportunities for scientists from different backgrounds, but with a common interest in some aspect of protein–carbohydrate interactions, to present their work in an informal and stimulating atmosphere. A major aim is always to induce cross-fertilization of ideas and concepts, and Interlec-23 was intended to have some bias towards lectins (galectins, collectins, selectin...
2016
Introduction: The study of lectins began with the work of Hermann Stillmark in the year 1888. Lectins are carbohydratebinding proteins of nonimmune origin and find application in diagnostic pathology. Objectives: Recent research work shows a remarkable development in lectin science. This comprehensive review tries to emphasize the historical aspects, biological sources, classification, applications, and recent advances of lectins. Materials and methods: Electronic database searches for published literature were performed. The following electronic databases with no language and publication date restrictions were searched: MEDLINE (via Ovid and PubMed), EMBASE (via Ovid), the Cochrane Oral Health Group’s Trials Register, and CENTRAL. Results: Lectins have been proven to be effective in in vitro trials for combating many medical conditions like cancer, autoimmune disorders, etc. Conclusion: Lectins could be the next generation therapy if efficient research work is contributed to the un...
Histochemistry and cell biology, 2002
The glycosylation of the intestinal cell layer is thought to control several key functions of the gut such as vectorial transports, defence against microbial agents or immunological processes. It has been assumed that the gut microflora may modulate the glycosylation pattern of the intestinal cell layer. However, there is no direct evidence for this regulatory process. The first goal of this work was to establish the germ-free mice intestinal glycosylation baseline using a histochemical approach and a panel of ten lectins with defined glycan specificities to tissue sections prepared from various cellular compartments of the small and large intestine. Using this baseline, we have studied the contribution of the gut microflora on the carbohydrate composition of glycoconjugates of intestinal cells by comparing the germ-free and conventional mice glycosylation patterns. Analysis of the germ-free mice intestinal glycosylation baseline revealed that the expression of glycans depends on th...