Carbohydrate specificity of chicken and human tandem-repeat-type galectins-8 in composition of cellsстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 17 мая 2016 г.
Аннотация:The network of adhesion/growthregulatory galectins in chicken (chicken galectin, CG) has only one tandem
repeattype protein, CG8. Using a cellbased assay and probing galectin reactivity with a panel of fluorescent neoglycocon
jugates (glycoprobes), its glycanbinding profile was determined. For internal validation, human galectin8 (HG8) was test
ed. In comparison to HG8, CG8 showed a rather similar specificity: both galectins displayed high affinity to blood group
ABH antigens as well as to 3′sialylated and 3′sulfated lactosamine chains. The most remarkable difference was found to
be an ability of HG8 (but not CG8) to bind the disaccharide Galβ13GlcNAc (Lec) as well as branched and linear oligo
lactosamines. The glycanbinding profile was shown to be influenced by glycocalix of the cell, where the galectin is
anchored. Particularly, glycosidase treatment of galectinloaded cells led to the change of the profile. Thus, we suppose the
involvement of cisglycans in the interaction of cellanchored galectins with external glycoconjugates.