Specificity of human galectins on cell surfaces

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• 作者：E. M. Rapoport ; N. V. Bovin
• 关键词：galectins ; glycans ; cells ; carbohydrate specificity ; carbohydrate ; recognition domain
• 刊名：Biochemistry (Moscow)
• 出版年：2015
• 出版时间：July 2015
• 年：2015
• 卷：80
• 期：7
• 页码：846-856
• 全文大小：556 KB
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  23.Cueni, L
• 作者单位：E. M. Rapoport (1)
  N. V. Bovin (1)
  
  1. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997, Moscow, Russia
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Bioorganic Chemistry
  Microbiology
  Biomedicine
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3040

文摘

Galectins are ?-galactoside-binding proteins sharing homology in amino acid sequence of their carbohydraterecognition domain. Their carbohydrate specificity outside cells has been studied previously. The main conclusion of these studies was that several levels of glycan ligand recognition exist for galectins: (i) disaccharide Gal?1-4GlcNAc (LN, Nacetyllactosamine) binds stronger than ?-galactopyranose; (ii) substitution at 0 -2 and 0 -3 of galactose residue as well as core fragments (“right-from GlcNAc) provides significant increase in affinity; (iii) similarly glycosylated proteins can differ significantly in affinity to galectins. Information about the natural cellular receptors of galectins is limited. Until recently, it was impossible to study specificity of cell-bound galectins. A model based on controlled incorporation of a single protein into glycocalyx of cells and subsequent interaction of loaded cells with synthetic glycoprobes measured by flow cytometry made this possible recently. In this review, data about glycan specificity of proto-, chimera-, and tandem-repeat type galectins on the cell surface are systematized, and comparative analysis of the results with data on specificity of galectins in artificial systems was performed. The following conclusions from these studies were made: (i) cellular galectins have practically no ability to bind disaccharide LNn, but display affinity to 3'-substituted oligolactosamines and oligomers LNn; (ii) tandem-repeat type galectins recognize another disaccharide, namely Gal?1-3GlcNAc (Lec); (iii) on the cell surface, tandemrepeat type galectins conserve the ability to display high affinity to blood group antigens of ABH system; (iv) in general, when galectins are immersed into glycocalyx, they are more selective regarding glycan interactions. Thus, we conclude that competitive interaction of galectins with cell microenvironment (endogenous cell glycans) is the main factor providing selectivity of galectins in vivo.