Biochemistry (Moscow)

, 76:1185 | Cite as

Carbohydrate specificity of chicken and human tandem-repeat-type galectins-8 in composition of cells

  • O. A. Vokhmyanina
  • E. M. Rapoport
  • I. M. Ryzhov
  • E. Yu. Korchagina
  • G. V. Pazynina
  • V. V. Severov
  • H. Kaltner
  • S. André
  • H. -J. Gabius
  • N. V. BovinEmail author


The network of adhesion/growth-regulatory galectins in chicken (chicken galectin, CG) has only one tandemrepeat-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 (Lec) 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.

Key words

ABH blood group antigens galectin cell glycoconjugates 



bovine serum albumin


chicken galectin-8


carbohydrate recognition domain


fluorescein isothiocyanate


conjugate of glycan with polyacrylamide


human galectin-8


phosphatebuffered saline (pH 7.2) containing 0.2% BSA


phosphate-buffered saline (pH 7.2)


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Copyright information

© Pleiades Publishing, Ltd. 2011

Authors and Affiliations

  • O. A. Vokhmyanina
    • 1
  • E. M. Rapoport
    • 1
  • I. M. Ryzhov
    • 1
  • E. Yu. Korchagina
    • 1
  • G. V. Pazynina
    • 1
  • V. V. Severov
    • 1
  • H. Kaltner
    • 2
  • S. André
    • 2
  • H. -J. Gabius
    • 2
  • N. V. Bovin
    • 1
    Email author
  1. 1.Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesMoscowRussia
  2. 2.Institute of Physiological Chemistry, Faculty of Veterinary MedicineLudwig-Maximilians-UniversityMunichGermany

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