Lectin-based glycomics: how and when was the technology born? 2014

Jun Hirabayashi
Research Center for Stem Cell Engineering, National Institute of Advance Industrial Science and Technology (AIST), Central-2, 1-1-1, Umezono, Tsukuba, Ibaraki, 305-8568, Japan, jun-hirabayashi@aist.go.jp.

Lectin-based glycomics is an emerging, comprehensive technology in the post-genome sciences. The technique utilizes a panel of lectins, which is a group of biomolecules capable of deciphering "glycocodes," with a novel platform represented by a lectin microarray. The method enables multiple glycan-lectin interaction analyses to be made so that differential glycan profiling can be performed in a rapid and sensitive manner. This approach is in clear contrast to another advanced technology, mass spectrometry, which requires prior glycan liberation. Although the lectin microarray cannot provide definitive structures of carbohydrates and their attachment sites, it gives useful clues concerning the characteristic features of glycoconjugates. These include differences not only in terminal modifications (e.g., sialic acid (Sia) linkage, types of fucosylation) but also in higher ordered structures in terms of glycan density, depth, and direction composed for both N- and O-glycans. However, before this technique began to be implemented in earnest, many other low-throughput methods were utilized in the late twentieth century. In this chapter, the author describes how the current lectin microarray technique has developed based on his personal experience.

UI MeSH Term Description Entries
D011134 Polysaccharides Long chain polymeric CARBOHYDRATES composed of MONOSACCHARIDES linked by glycosidic bonds. Glycan,Glycans,Polysaccharide
D006001 Glycoconjugates Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed) Glycoconjugate
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D046228 Microarray Analysis The simultaneous analysis, on a microchip, of multiple samples or targets arranged in an array format. Microarray Analytical Devices,Microarray Microchips,Nanoarray Analytical Devices,Analysis, Microarray,Analytical Device, Microarray,Analytical Device, Nanoarray,Analytical Devices, Microarray,Analytical Devices, Nanoarray,Device, Microarray Analytical,Device, Nanoarray Analytical,Devices, Microarray Analytical,Devices, Nanoarray Analytical,Microarray Analytical Device,Microarray Microchip,Microchip, Microarray,Microchips, Microarray,Nanoarray Analytical Device
D054794 Glycomics The systematic study of the structure and function of the complete set of glycans (the glycome) produced in a single organism and identification of all the genes that encode glycoproteins. Sugar Code,Glycobiology
D037102 Lectins Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition. Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal

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