Integrin β6 (E4M9P) XP^® Rabbit mAb #95153

Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with extracellular environment (inside-out signaling) (1,2).

The avβ6 subunit was identified in epithelial cells and interacts with the fibronectin receptor integrin α5 (3,4). It is expressed during development, but expression becomes repressed in adulthood (5). It is involved in wound healing, fibrosis, pulmonary fibrosis in particular, and tumorigenesis (6-8). When the dimer is unregulated in the membrane in response to injury, the integrin β6 subunit binds directly to an RGD motif present in fibronectin and TGF-β, both present in the extracellular matrix. Integrin β6 cleaves and binds the LAP fragment of latent TGF-β, thereby releasing active TGF-β into the ECM to activate myofibroblasts which consequently mediate ECM remodeling (6-8).