Читать книгу Musculoskeletal Disorders - Sean Gallagher - Страница 70

Collagen is the major structural protein in skeletal muscle extracellular matrix. It accounts for 1–10% of a muscle’s dry weight (Dransfield, 1977; Schiaffino & Reggiani, 2011). Fibrillar types of collagen I and III predominate in the adult endomysium, perimysium, and epimysium (Listrat et al., 2000; Marvulli, Volpin, & Bressan, 1996). Type V collagen, another fibril‐forming collagen, associates with types I and III and may form a core for type I collagen fibrils in the perimysium and endomysium (Fitch, Gross, Mayne, Johnson‐Wint, & Linsenmayer, 1984). Elastin is also part of the fascial layers for the provision of structural elasticity. In contrast, the basement membranes of muscle fibers consist of a branched network structure of type IV collagen (Sanes, 1982). Many glycoproteins function as linker molecules between type IV collagen in the basement membrane and sarcolemma (Ervasti & Campbell, 1993). Interactions between these glycoproteins provide potential mechanisms for the transmission of lateral forces from myofibers (Grounds, Sorokin, & White, 2005).