Galectin protein (Gal)

Galectins are a family of evolutionarily conserved, soluble, and cell-surface proteins defined by their affinity for beta-galactoside carbohydrates and the presence of a characteristic carbohydrate recognition domain (CRD) [1, 3]. They are classified into prototype, chimera, and tandem-repeat types, with Galectin-1, Galectin-3, and Galectin-9 being the most studied therapeutic targets [1, 13, 21]. Biologically, galectins act as master regulators of immune cell homeostasis, cell-extracellular matrix adhesion, and apoptosis [4, 6, 12]. In pathological conditions, their overexpression fuels chronic inflammation, drives organ fibrosis (such as in NASH and pulmonary fibrosis), and facilitates tumor immune evasion and metastasis [2, 9, 10, 15]. Drug development focuses on small molecules and carbohydrate polymers that competitively bind the CRD to block these deleterious interactions [2, 3, 5]. Notably, Galectin-3 is already utilized as an FDA-approved clinical biomarker for heart failure prognosis [13, 22].

Other names

S-type lectinGalaptinLectin, galactoside-bindingLGALSMac-2 (for Galectin-3)L-14 (for Galectin-1)

Competitive inhibition of the carbohydrate recognition domain (CRD), preventing the binding of galectins to beta-galactoside-containing glycoproteins and glycolipids on the cell surface and extracellular matrix, which disrupts pathological signaling in fibrosis, immune evasion, and tumor growth.