Glycan Dependence of Galectin-3 Self-Association Properties - Archive ouverte HAL Access content directly
Journal Articles PLoS ONE Year : 2014

Glycan Dependence of Galectin-3 Self-Association Properties

(1) , (2, 1) , (3) , (4) , (1) , (1) , (1)
1
2
3
4

Abstract

Human Galectin-3 is found in the nucleus, the cytoplasm and at the cell surface. This lectin is constituted of two domains: an unfolded N-terminal domain and a C-terminal Carbohydrate Recognition Domain (CRD). There are still uncertainties about the relationship between the quaternary structure of Galectin-3 and its carbohydrate binding properties. Two types of self-association have been described for this lectin: a C-type self-association and a N-type self-association. Herein, we have analyzed Galectin-3 oligomerization by Dynamic Light Scattering using both the recombinant CRD and the full length lectin. Our results proved that LNnT induces N-type self-association of full length Galectin-3. Moreover, from Nuclear Magnetic Resonance (NMR) and Surface Plasmon Resonance experiments, we observed no significant specificity or affinity variations for carbohydrates related to the presence of the N-terminal domain of Galectin-3. NMR mapping clearly established that the N-terminal domain interacts with the CRD. We propose that LNnT induces a release of the N-terminal domain resulting in the glycan-dependent self-association of Galectin-3 through N-terminal domain interactions.
Fichier principal
Vignette du fichier
Halimietal_PLosOne.pdf (1.3 Mo) Télécharger le fichier
Origin : Publication funded by an institution
Loading...

Dates and versions

inserm-01356877 , version 1 (26-08-2016)

Identifiers

Cite

Hubert Halimi, Annafrancesca Rigato, Deborah Byrne, Géraldine Ferracci, Corinne Sebban-Kreuzer, et al.. Glycan Dependence of Galectin-3 Self-Association Properties. PLoS ONE, 2014, 9 (11), pp.e111836. ⟨10.1371/journal.pone.0111836⟩. ⟨inserm-01356877⟩
47 View
138 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More