Integrin receptor (ITG) (ITG)

Integrin receptors are a superfamily of transmembrane cell surface receptors that function as heterodimeric glycoproteins, consisting of non-covalently associated alpha and beta subunits (Hynes, R. O., Cell, 2002). They serve as the primary mechanical and signaling link between the intracellular cytoskeleton and the extracellular matrix (ECM), facilitating bidirectional signaling that regulates cell adhesion, migration, proliferation, and survival (UniProt, 2023). In pathological states, specific integrins such as alpha-V beta-3, alpha-V beta-5, and alpha-5 beta-1 are significantly upregulated and play a central role in driving abnormal angiogenesis and vascular permeability (PubMed, PMID: 24507561). This makes them critical therapeutic targets in ocular diseases like neovascular age-related macular degeneration (nAMD) and diabetic macular edema (DME), as well as in various cancers where they facilitate metastasis (Allegro Ophthalmics, 2023). Drugs like risuteganib (ALG-1001) are designed to act as integrin antagonists, binding to these receptors to inhibit the signaling pathways that lead to vessel leakage and inflammation (ClinicalTrials.gov, NCT02740335). Beyond ophthalmology, integrin-targeting therapies are utilized in treating autoimmune disorders and preventing thrombosis by modulating leukocyte trafficking and platelet aggregation, respectively (PubChem, 2024).

Other names

IntegrinIntegrinsCell adhesion moleculeAdhesion receptorITG

Integrin antagonism; competitive inhibition of ligand binding to the extracellular domain of alpha/beta heterodimers, blocking downstream signaling pathways involved in adhesion and migration.