The integrin family of adhesion molecules participate in important cell-cell and cell-extracellular matrix interactions in a diverse range of biological processes. Integrins are heterodimers consisting of α subunit and β subunit. Both a and b subunit are transmembrane proteins with large extracellular domains (>100 kDa for α subunit and >75 kDa for β subunit) that interact with extracellular matrix proteins and relatively small cytoplasmic domains (50 amino acids or less, except for the β4 subunit) that interact with cytoskeletal proteins. The adhesiveness of integrins is dynamically regulated in response to cytoplasmic signals, termed “inside-out” signaling. It has been reported that, upon ligand binding, integrins regulate many intracellular signaling pathways that involve cytoplasmic alkalization, intracellular Ca²⁺ fluctuation, inositol lipid metabolism, protein kinase C, MAP kinase and phosphatidyl inositol kinase. Integrin α7 is a specific cellular receptor for the basement membrane protein laminin-1, as well as for the laminin isoforms-2 and -4. The α7 subunit is expressed mainly in skeletal and cardiac muscle and may be involved in differentiation and migration processes during myogenesis. Absence of integrin α7 results in muscular dystrophy is revealed.