Galectin family (LGALS)

Galectins are a family of evolutionarily conserved proteins characterized by their affinity for beta-galactoside sugars, mediated by one or more carbohydrate-recognition domains (CRDs) (Cummings et al., 2017). The family includes 15 members in mammals, categorized into prototype, tandem-repeat, and chimeric types, which function both intracellularly and extracellularly to regulate processes such as cell adhesion, apoptosis, and immune signaling (Liu et al., 2005). While Galectin-1 and Galectin-3 are the most extensively studied therapeutic targets, 'other galectins' such as Galectin-7, -8, -9, and -12 play critical roles in various pathologies (Thijssen et al., 2015). For instance, Galectin-9 acts as a checkpoint molecule by binding to TIM-3 on T cells, leading to immune exhaustion in the tumor microenvironment (Zhu et al., 2005). Galectin-7 is often associated with squamous cell carcinomas, while Galectin-8 and -12 are involved in nutrient sensing and adipocyte differentiation, respectively (Johannes et al., 2018). Therapeutic strategies for these targets involve small molecule inhibitors or monoclonal antibodies designed to block the CRD, thereby disrupting the interaction between galectins and their glycosylated ligands (Bresalier et al., 2015). These interventions are currently being explored for the treatment of cancer, fibrosis, and chronic inflammatory diseases where galectin-mediated signaling is aberrant (Sciacchitano et al., 2018).

Other names

S-type lectinsGalaptinsBeta-galactoside-binding lectinsLGALS family

Competitive inhibition of the carbohydrate-recognition domain (CRD) to prevent binding to beta-galactoside-containing glycoproteins and glycolipids.