Multiple cell-surface adhesion molecules, extracellular matrix components, and immune cells

The entry 'Multiple cell-surface adhesion molecules, extracellular matrix components, and immune cells' is a descriptive classification rather than a single canonical target, typically referring to the broad interactome of Galectin-3 (LGALS3) (UniProt P17931). Galectin-3 is a chimeric-type lectin that binds to beta-galactoside-containing glycans on various cell-surface receptors, such as integrins and T-cell receptors, as well as extracellular matrix (ECM) proteins like laminin and fibronectin (Dumic et al., 2006). Through these interactions, it acts as a molecular scaffold that modulates cell-cell adhesion, signal transduction, and immune cell activation (Sciacchitano et al., 2018). In pathological states, Galectin-3 promotes tissue fibrosis and tumor immune evasion by cross-linking these components within the microenvironment (Chen et al., 2014). Therapeutic agents like Belapectin (GR-MD-02) target this network by inhibiting the carbohydrate-recognition domain of Galectin-3, thereby disrupting its ability to bind these multiple components (Traber & Zomer, 2013). Because this name encompasses a wide variety of distinct proteins and cell types, it is considered an incorrect or overly broad designation for a specific therapeutic target.

Other names

Galectin-3 interactomeCell-surface and ECM binding partnersLectin-binding glycoconjugates

Inhibition of Galectin-3 (LGALS3) to prevent its multivalent binding to cell-surface receptors and extracellular matrix proteins, thereby disrupting pro-fibrotic and pro-inflammatory signaling pathways.