Biochemistry (Moscow)

, 76:1185

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

Authors

  • O. A. Vokhmyanina
    • Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
  • E. M. Rapoport
    • Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
  • I. M. Ryzhov
    • Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
  • E. Yu. Korchagina
    • Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
  • G. V. Pazynina
    • Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
  • V. V. Severov
    • Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
  • H. Kaltner
    • Institute of Physiological Chemistry, Faculty of Veterinary MedicineLudwig-Maximilians-University
  • S. André
    • Institute of Physiological Chemistry, Faculty of Veterinary MedicineLudwig-Maximilians-University
  • H. -J. Gabius
    • Institute of Physiological Chemistry, Faculty of Veterinary MedicineLudwig-Maximilians-University
    • Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
Article

DOI: 10.1134/S0006297911100130

Cite this article as:
Vokhmyanina, O.A., Rapoport, E.M., Ryzhov, I.M. et al. Biochemistry Moscow (2011) 76: 1185. doi:10.1134/S0006297911100130

Abstract

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 antigensgalectincell glycoconjugates

Abbreviations

BSA

bovine serum albumin

CG8

chicken galectin-8

CRD

carbohydrate recognition domain

FITC

fluorescein isothiocyanate

Glyc-PAA

conjugate of glycan with polyacrylamide

HG8

human galectin-8

PBA

phosphatebuffered saline (pH 7.2) containing 0.2% BSA

PBS

phosphate-buffered saline (pH 7.2)

Copyright information

© Pleiades Publishing, Ltd. 2011