Galectin (Gal)

Galectins are a family of evolutionarily conserved proteins characterized by their affinity for beta-galactoside-containing glycans through a highly conserved carbohydrate-recognition domain (CRD) [1]. They function as key regulators of cellular processes including adhesion, migration, and apoptosis, acting both inside and outside the cell [2]. In pathological states, galectins—notably Galectin-1 and Galectin-3—are frequently upregulated and play critical roles in promoting tumor immune evasion, angiogenesis, and the progression of chronic fibrotic diseases such as NASH and idiopathic pulmonary fibrosis [3]. Therapeutic targeting of galectins involves the use of carbohydrate-based inhibitors or small molecules designed to occupy the CRD, preventing the interaction with glycosylated receptors [4]. Current clinical efforts are focused on treating conditions like non-alcoholic steatohepatitis (NASH), idiopathic pulmonary fibrosis, and various solid tumors [5]. These inhibitors aim to disrupt the galectin lattice on the cell surface, which otherwise stabilizes receptor signaling and prevents T-cell activation [6]. By inhibiting these proteins, researchers hope to restore immune surveillance and halt the activation of profibrotic pathways [7]. Sources: [1] UniProt (Family: Galectin), [2] PubMed (PMID: 29107077), [3] Nature Reviews Drug Discovery (PMID: 28937139), [4] Journal of Medicinal Chemistry (PMID: 30113830), [5] ClinicalTrials.gov, [6] Glycobiology (PMID: 25904601), [7] Trends in Pharmacological Sciences (PMID: 30243715).

Other names

S-type lectinS-lac lectinGalaptinBeta-galactoside-binding lectin

Competitive inhibition of the carbohydrate-recognition domain (CRD) to prevent binding to beta-galactoside-containing glycoconjugates [1][4].