Glycoconjugate Journal

, Volume 26, Issue 4, pp 423–432

Functional characterization of an eosinophil-specific galectin, ovine galectin-14

  • Anna R. Young
  • Garry J. Barcham
  • Joanna M. Kemp
  • Jillian L. Dunphy
  • Andrew Nash
  • Els N. Meeusen
Article

DOI: 10.1007/s10719-008-9190-0

Cite this article as:
Young, A.R., Barcham, G.J., Kemp, J.M. et al. Glycoconj J (2009) 26: 423. doi:10.1007/s10719-008-9190-0

Abstract

Across mammalian species, human galectin-10 and ovine galectin-14 are unique in their expression in eosinophils and their release into lung and gastrointestinal tissues following allergen or parasite challenge. Recombinant galectin-14 is active in carbohydrate binding assays and has been used in this study to unravel the function of this major eosinophil constituent. In vitro cultures revealed that galectin-14 is spontaneously released by eosinophils isolated from allergen-stimulated mammary gland lavage, but not by resting peripheral blood eosinophils. Galectin-14 secretion from peripheral blood eosinophils can be induced by the same stimuli that induce eosinophil degranulation. Flow cytometric analysis showed that recombinant galectin-14 can bind in vitro to eosinophils, neutrophils and activated lymphocytes. Glycan array screening indicated that galectin-14 recognizes terminal N-acetyllactosamine residues which can be modified with α1-2-fucosylation and, uniquely for a galectin, prefers α2- over α2-sialylation. Galectin-14 showed the greatest affinity for lacto-N-neotetraose, an immunomodulatory oligosaccharide expressed by helminths. Galectin-14 binds specifically to laminin in vitro, and to mucus and mucus producing cells on lung and intestinal tissue sections. In vivo, galectin-14 is abundantly present in mucus scrapings collected from either lungs or gastrointestinal tract following allergen or parasite challenge, respectively. These results suggest that in vivo secretion of eosinophil galectins may be specifically induced at epithelial surfaces after recruitment of eosinophils by allergic stimuli, and that eosinophil galectins may be involved in promoting adhesion and changing mucus properties during parasite infection and allergies.

Keywords

Galectin Eosinophil Mucus Glycan array Allergy Helminth 

Copyright information

© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  • Anna R. Young
    • 1
  • Garry J. Barcham
    • 2
  • Joanna M. Kemp
    • 1
  • Jillian L. Dunphy
    • 4
  • Andrew Nash
    • 3
  • Els N. Meeusen
    • 1
  1. 1.Department of Physiology, School of Biomedical SciencesMonash UniversityClaytonAustralia
  2. 2.Centre for Animal Biotechnology, School of Veterinary ScienceThe University of MelbourneVictoriaAustralia
  3. 3.CSL Ltd45 Poplar RoadParkvilleAustralia
  4. 4.School of Community HealthCharles Sturt UniversityAlburyAustralia

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