Carbohydrate specificity of chicken and human tandem-repeat-type galectins-8 in composition of cells
| Autor: | Hans-Joachim Gabius, Galina V. Pazynina, E. M. Rapoport, Nicolai V. Bovin, Herbert Kaltner, Ivan M. Ryzhov, Olga A Vokhmyanina, Sabine André, Vyacheslav V. Severov, E. Yu. Korchagina |
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| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
animal structures
Glycoconjugate Galectins Cell Disaccharide Biology Disaccharidases Kidney Biochemistry Cell Line 03 medical and health sciences chemistry.chemical_compound Dogs Tandem repeat Polysaccharides otorhinolaryngologic diseases medicine Animals Humans Glycoside hydrolase 030304 developmental biology Galectin chemistry.chemical_classification 0303 health sciences Molecular Structure 030302 biochemistry & molecular biology General Medicine Carbohydrate Molecular biology stomatognathic diseases medicine.anatomical_structure chemistry Cell culture Tandem Repeat Sequences Blood Group Antigens Chickens |
| Zdroj: | Biochemistry (Moscow) Biochemistry (Moscow); Vol 76 |
| ISSN: | 1608-3040 0006-2979 |
| DOI: | 10.1134/S0006297911100130 |
| Popis: | The network of adhesion/growth-regulatory galectins in chicken (chicken galectin, CG) has only one tandem-repeat-type protein, CG8. Using a cell-based assay and probing galectin reactivity with a panel of fluorescent neoglycoconjugates (glycoprobes), its glycan-binding profile was determined. For internal validation, human galectin-8 (HG8) was tested. 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 Galβ1-3GlcNAc (Le(c)) as well as branched and linear oligolactosamines. The glycan-binding profile was shown to be influenced by glycocalix of the cell, where the galectin is anchored. Particularly, glycosidase treatment of galectin-loaded cells led to the change of the profile. Thus, we suppose the involvement of cis-glycans in the interaction of cell-anchored galectins with external glycoconjugates. |
| Databáze: | OpenAIRE |
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