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lüll Emerging role of alpha2,6-sialic acid as a negative regulator of galectin binding and function Zhuo Y; Bellis SLJ Biol Chem 2011[Feb]; 286 (8): 5935-41Galectins are beta-galactoside-binding lectins that regulate diverse cell behaviors, including adhesion, migration, proliferation, and apoptosis. Galectins can be expressed both intracellularly and extracellularly, and extracellular galectins mediate their effects by associating with cell-surface oligosaccharides. Despite intensive current interest in galectins, strikingly few studies have focused on a key enzyme that acts to inhibit galectin signaling, namely beta-galactoside alpha2,6-sialyltransferase (ST6Gal-I). ST6Gal-I adds an alpha2,6-linked sialic acid to the terminal galactose of N-linked glycans, and this modification blocks galectin binding to beta-galactosides. This minireview summarizes the evidence suggesting that ST6Gal-I activity serves as an "off switch" for galectin function.|Animals[MESH]|Galactosides/*metabolism[MESH]|Galectins/*metabolism[MESH]|Humans[MESH]|Oligosaccharides/*metabolism[MESH]|Protein Binding/physiology[MESH]|Sialic Acids/*metabolism[MESH] |