galectin8

Galectin-8 is a member of the galectin family of beta-galactoside-binding lectins and is encoded by the LGALS8 gene in humans. Unlike single-domain galectins, galectin-8 is a tandem-repeat galectin with two carbohydrate-recognition domains linked by a short peptide, enabling crosslinking of glycans on cell surfaces and extracellular matrices. Its primary ligands are beta-galactoside-containing glycans, including N-acetyllactosamine, and it can recognize a range of glycoprotein targets.

Galectin-8 is expressed in multiple tissues and exists in several isoforms produced by alternative splicing. It can function inside cells and be secreted extracellularly, where it participates in cell adhesion, cell migration, and modulation of immune responses. Through interactions with glycoproteins and integrins, it can influence cytokine production and inflammatory signaling.

A key, well-supported function of galectin-8 is in selective autophagy. When intracellular membranes are damaged, galectin-8 detects exposed glycans and recruits autophagy receptors such as NDP52 to promote clearance of damaged membranes or intracellular pathogens.

In health and disease, galectin-8 has been studied in cancer, infection, and inflammatory disorders. Its effects are context-dependent, with reports of both pro- and anti-tumor activities, as well as roles in angiogenesis and immune regulation. Ongoing research seeks to clarify its mechanisms and evaluate its potential as a biomarker or therapeutic target.