Integrin alpha-7

Integrin alpha-7 (ITGA7) is a cell adhesion molecule that functions as the primary laminin receptor on skeletal myoblasts and mature myofibers (UniProt: Q13683). It mediates myoblast migration and differentiation, promotes myofiber cytoarchitecture maintenance, and supports contractile phenotype acquisition in airway smooth muscle cells. The protein also acts as a Schwann cell receptor for laminin-2 and mediates cartilage oligomeric matrix protein (COMP) effects on vascular smooth muscle maturation.

ITGA7 is primarily associated with skeletal muscle development and maintenance through the integrin-laminin signaling pathway. Mutations in ITGA7 cause congenital muscular dystrophy (MDCI; MIM 613204), characterized by early-onset hypotonia and muscle weakness (UniProt: Q13683).

In Alzheimer's disease, integrin alpha-7 is upregulated in post-mortem AD brain tissue compared to age-matched controls (Chaparral AD proteomics). The protein showed a mean log2 fold-change of +0.672 across analyzed subcellular fractions in TMT-labeled tandem mass spectrometry analysis, suggesting increased integrin-mediated signaling in the AD brain. This upregulation may reflect altered cell adhesion and migration processes in the context of neurodegeneration.