Integrin (ITG) (ITG)

Integrins are a superfamily of heterodimeric transmembrane receptors composed of non-covalently associated alpha and beta subunits that mediate cell-extracellular matrix (ECM) and cell-cell adhesion (Source: UniProt). They serve as critical mechanical and chemical links between the intracellular cytoskeleton and the extracellular environment, facilitating bidirectional signaling known as "inside-out" and "outside-in" signaling (Source: PubMed, PMID: 11882270). These processes regulate fundamental cellular activities, including survival, differentiation, and migration (Source: PubMed, PMID: 21867931). In various diseases, integrins are dysregulated; for instance, alpha-v-beta-3 (αvβ3) is often upregulated in tumor vasculature and certain cancers, promoting angiogenesis and metastasis (Source: Nature Reviews Cancer, 2010). In inflammatory conditions, integrins like alpha-4-beta-7 (α4β7) facilitate the recruitment of leukocytes to tissues (Source: Nature Reviews Immunology, 2007). Therapeutic interventions include monoclonal antibodies and small molecules designed to block these interactions, such as vedolizumab for inflammatory bowel disease and abciximab for preventing platelet aggregation in cardiovascular procedures (Source: StatPearls, 2023). However, targeting integrins can lead to significant safety concerns, such as increased bleeding risks or susceptibility to opportunistic infections like progressive multifocal leukoencephalopathy (Source: FDA, Tysabri Labeling).

Other names

Mammalian cell integrinsCell adhesion moleculesHeterodimeric transmembrane receptorsITGCD antigens

Integrin antagonists or inhibitors block the binding of extracellular ligands (such as fibronectin, vitronectin, or ICAMs) to the integrin receptor, thereby preventing downstream signaling and cell adhesion.