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Determination of Carbohydrate‐Binding Preferences of Human Galectins with Carbohydrate Microarrays
Author(s) -
Horlacher Tim,
Oberli Matthias A.,
Werz Daniel B.,
Kröck Lenz,
Bufali Simone,
Mishra Rashmi,
Sobek Jens,
Simons Kai,
Hirashima Mitsuomi,
Niki Toshiro,
Seeberger Peter H.
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000020
Subject(s) - galectin , galectin 1 , carbohydrate , biochemistry , binding selectivity , dna microarray , chemistry , glycosylation , galectin 3 , glucose homeostasis , biology , computational biology , microbiology and biotechnology , gene expression , gene , immunology , insulin resistance , insulin
Galectins are a class of carbohydrate‐binding proteins named for their galactose‐binding preference and are involved in a host of processes ranging from homeostasis of organisms to immune responses. As a first step towards correlating the carbohydrate‐binding preferences of the different galectins with their biological functions, we determined carbohydrate recognition fine‐specificities of galectins with the aid of carbohydrate microarrays. A focused set of oligosaccharides considered relevant to galectins was prepared by chemical synthesis. Structure–activity relationships for galectin–sugar interactions were determined, and these helped in the establishment of redundant and specific galectin actions by comparison of binding preferences. Distinct glycosylations on the basic lactosyl motifs proved to be key to galectin binding regulation—and therefore galectin action—as either high‐affinity ligands are produced or binding is blocked. High‐affinity ligands such as the blood group antigens that presumably mediate particular functions were identified.