The universe of galectin-binding partners and their functions in health and disease

MF Troncoso, MT Elola, AG Blidner, L Sarrias… - Journal of Biological …, 2023 - ASBMB
Galectins, a family of evolutionarily conserved glycan-binding proteins, play key roles in
diverse biological processes including tissue repair, adipogenesis, immune cell …

Inhibition of galectins in cancer: Biological challenges for their clinical application

DJ Laderach, D Compagno - Frontiers in Immunology, 2023 - frontiersin.org
Galectins play relevant roles in tumor development, progression and metastasis.
Accordingly, galectins are certainly enticing targets for medical intervention in cancer. To …

Receptor clustering by a precise set of extracellular galectins initiates FGFR signaling

D Zukowska, A Gedaj, N Porebska, M Pozniak… - Cellular and Molecular …, 2023 - Springer
FGF/FGFR signaling is critical for the development and homeostasis of the human body and
imbalanced FGF/FGFR contributes to the progression of severe diseases, including cancers …

[HTML][HTML] Exploring galectin interactions with human milk oligosaccharides and blood group antigens identifies BGA6 as a functional galectin-4 ligand

AJ Cagnoni, M Massaro, AM Cutine, A Gimeno… - Journal of Biological …, 2024 - Elsevier
Galectins (Gals), a family of multifunctional glycan-binding proteins, have been traditionally
defined as β-galactoside binding lectins. However, certain members of this family have …

Galectin‐8 inhibition and functions in immune response and tumor biology

E Purić, UJ Nilsson, M Anderluh - Medicinal Research Reviews, 2024 - Wiley Online Library
Galectins are among organisms' most abundantly expressed lectins (carbohydrate‐binding
proteins) that specifically bind β‐galactosides. They act not only outside the cell, where they …

[HTML][HTML] Benzimidazole–galactosides bind selectively to the Galectin-8 N-Terminal domain: Structure-based design and optimisation

M Hassan, S van Klaveren, M Håkansson… - European journal of …, 2021 - Elsevier
We have obtained the X-ray crystal structure of the galectin-8 N-terminal domain (galectin-
8N) with a previously reported quinoline–galactoside ligand at a resolution of 1.6 Å. Based …

[HTML][HTML] Linker remodels human Galectin-8 structure and regulates its hemagglutination and pro-apoptotic activity

Y Si, J Cai, J Zhu, Y Wang, F Zhang, L Meng… - International Journal of …, 2023 - Elsevier
Numerous articles have reported the involvement of linker in regulating bioactivity of tandem-
repeat galectins. We hypothesize that linker interacts with N/C-CRDs to regulate the …

[HTML][HTML] Engineered intrinsically fluorescent galectin-8 variants with altered valency, ligand recognition and biological activity

M Kalka, A Chorążewska, A Gędaj, D Żukowska… - International Journal of …, 2024 - Elsevier
Galectin-8 is a small soluble lectin with two carbohydrate recognition domains (CRDs). N-
and C-terminal CRDs of Gal-8 differ in their specificity for glycan ligands. Here, we wanted to …

Differential cellular responses to adhesive interactions with galectin-8-and fibronectin-coated substrates

W Li, A Sancho, WL Chung, Y Vinik… - Journal of Cell …, 2021 - journals.biologists.com
The mechanisms underlying the cellular response to extracellular matrices (ECMs) that
consist of multiple adhesive ligands are still poorly understood. Here, we address this topic …

A brief history of galectin evolution

J Günther, SP Galuska - Frontiers in Immunology, 2023 - frontiersin.org
Galectins are a family of carbohydrate-binding proteins found in vertebrates in great
abundance and diversity in terms of both structure and ligand-binding properties as well as …