Carbohydrate specificity of lectin, purified from the fruiting bodies of Mycena pura /Fr./ Kumm. and its use in histochemical investigation (original) (raw)
Related papers
ijser.org
Lectins are the carbohydrate-binding proteins and are known for their toxic relevance. History provides various evidences for their toxicity profile and initially, it was thought that lectins are associated solely with toxic content. However, recent research shows a remarkable development in lectin science and their use in studying glycoprotein biosynthesis, investigating carbohydrates on cells/cellorganelles, mapping neuronal pathways, anti-cancer therapies and in mitogenic stimulation of lymphocytes is well documented. Even though lectins have intrigued current researchers for the investigation of their therapeutic values, not enough studies have been conducted so far and knowledge about lectins is limited to certain plants or animal sources and further research is important to identify lectins and their importance in as many sources as possible. This review is a comprehensive account of lectins starting from their initial discovery, their purification, biological role and also presents an outline of their toxic effects and therapeutic contribution. In the search for their functions, the end may not be in sight but, at last, it is conceivably around the corner. Lectins could be the next generation medicines if efficient research is contributed in their understanding.
European Journal of Biochemistry, 2005
Glycopeptides and oligosaccharides of either the N-acetyllactosaminic or the oligomannosidic type derived from glycoproteins containing the N-glycosylamine linkage were used to define the specificity of different lectins (concanavalin A, Lens culinaris agglutinin, Vicia faba agglutinin, Pisum sativum agglutinin, Ricinus communis agglutinins, soybean agglutinin, wheat germ agglutinin, Solanum tuberosum agglutinin, Datura stramonium agglutinin, Lotus tetragonolobus agglutinin, Ulex europeus agglutinin) by studying the inhibition of human red blood cell agglutination by these structures. The results obtained show that lectins considered 'identical' in terms of monosaccharide specificity, possess the ability to recognize fine differences in more complex structures. In fact, different lectins are able to recognize different saccharidic sequences on the same glycan structure. As these sequences are likely to be common to numerous glycoproteins, including cell membrane glycoproteins, the results obtained with lectins in the study of cell surface carbohydrates have to be very carefully interpreted. Moreover, our results confirm previous data on the spatial configuration of the glycan moiety of glycoproteins deduced from the construction of molecular models: the fact that oligosaccharides bearing an alpha-NeuAc-(2 leads to 6)-Gal unit are more powerful inhibitors than oligosaccharides bearing an alpha-NeuAc-(2 leads to 3)-Gal unit could be related to the high rotational freedom of alpha-2,6 linkage; the observation that glycoasparagines, glycopeptides and glycoproteins possess a higher affinity for lectins than the related oligosaccharides could be explained by the fact that the glycan--amino acid linkage leads to structures more rigid than those of the oligosaccharides themselves.
European Journal of Biochemistry, 1990
Seven plant lectins, Dolichos bijlorus agglutinin (DBA), Grijjfonia simplicifolia agglutinin (GSA, isolectin A4), Helix pomatia agglutinin (HPA), soybean (Glycine max) agglutinin (SBA), Salvia sclarea agglutinin (SSA), Vicia villosa agglutinin (VVA, isolectin B4) and Wistariafloribunda agglutinin (WFA), known to be specific for N-acetyl-D-galactosamine-(GalNAc) bearing glycoconjugates, have been compared by the binding of their radiolabelled derivatives, to eight well-characterized synthetic oligosaccharides immobilized via a spacer on an inert silica matrix (Synsorb). The eight oligosaccharides included the Forssman, the blood group A and the T antigens, as well as ctGalNAc coupled directly to the support (Tn antigen) and also structures with GalNAc linked a or /3 to positions 3 or 4 of an unsubstituted Gal. The binding studies clearly distinguished the lectins into aGalNAc-specific agglutinins like DBA, GSA and SSA, and lectins which recognize a-as well as P-linked GalNAc residues like HPA, VVA, WFA and SBA. HPA was the only lectin which bound to the P G a l l -+ 3aGalNAc-Synsorb adsorbent (T antigen) indicating that it also recognizes internal GalNAc residues. Among the aGalNAc-specific lectins, DBA strongly recognized blood group A structures while GSA displayed weaker recognition, and SSA bound only slightly to this affinity matrix. In addition, DBA and SSA were able to distinguish between GalNAc linked a1 -+ 3 and GalNAc linked a1 -+ 4, to the support, the latter being a much weaker ligand.
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...
Activity Dependence of a Novel Lectin Family on Structure and Carbohydrate-Binding Properties
Molecules
A GalNAc/Gal-specific lectins named CGL and MTL were isolated and characterized from the edible mussels Crenomytilus grayanus and Mytilus trossulus. Amino acid sequence analysis of these lectins showed that they, together with another lectin MytiLec-1, formed a novel lectin family, adopting β-trefoil fold. In this mini review we discuss the structure, oligomerization, and carbohydrate-binding properties of a novel lectin family. We describe also the antibacterial, antifungal, and antiproliferative activities of these lectins and report about dependence of activities on molecular properties. Summarizing, CGL, MTL, and MytiLec-1 could be involved in the immunity in mollusks and may become a basis for the elaboration of new diagnostic tools or treatments for a variety of cancers.
Carbohydrate Research, 1991
Glycosylated Wins represent a series of glycoproteins with related activities and, in the case of the Leguminosae, related amino acid sequences. Therefore, they offer a model system in which to study the diversity of N-linked oligosaccharide structures of plant glycoproteins. The influence of the polypeptide on the type of oligosaccharide substitution and the problem of inter-and intra-genus variation in glycosylation can also be addressed. Analysis of the glycosylation of 18 lectins has shown that they can be classified into four qualitatively similar groups on the basis of the Bio-Gel P-4 elution protiles of the oligosaccharides released by hydrazinolysis: (a) The Erythrina cristagalli profile, with a major component at 8.8 glucose units (gu) and minor components at 8.0,7.2, and 5.8 gu. The major component is the heptasaccharide, a-o-Manp-