Integrin subunit alpha 7 (ITGA7)

Integrin subunit alpha 7 (ITGA7) is a transmembrane protein that forms a heterodimer with beta-1 integrin, serving as the primary laminin receptor in skeletal myoblasts and adult myofibers. It mediates critical cell-matrix interactions by binding laminins such as laminin-1, -2, and -4, and is highly expressed in skeletal, cardiac, and smooth muscle cells, where it localizes to Z-discs and costameres. This integrin plays essential roles in myoblast adhesion, migration, and differentiation during myogenesis, as well as in maintaining myofiber cytoarchitecture, anchorage, viability, and functional integrity. Knockout studies in mice reveal muscular dystrophy-like phenotypes with disrupted myotendinous junctions, fiber size variation, necrosis, and elevated creatine kinase, underscoring its importance in muscle stability, potentially overlapping with sarcoglycan and dystrophin functions. Mutations in ITGA7 cause congenital myopathies, severe congenital fiber type disproportion, and left ventricular non-compaction cardiomyopathy, while altered expression occurs in Duchenne and Becker muscular dystrophies. AAV-mediated overexpression of ITGA7 in DMD mouse models shows protective effects against muscle degeneration, suggesting therapeutic potential, though no approved drugs currently target it.

Other names

Alpha-7 integrinIntegrin alpha-7