In physiology, isotropic bands (better known as I bands) are the lighter bands of skeletal muscle cells (a.k.a. muscle fibers). Isotropic bands contain only actin-containing thin filaments.[1] The thin filaments are placed between 2 myosin filaments and contain only the actin filaments of neighboring sarcomeres. Bisecting the I band and serving as an anchoring point for the two adjacent actin filaments is the Z disc. During muscle contraction, the I band will shorten, while an A band will maintain its width.[2]
The darker bands within skeletal muscle, known as anisotropic bands (A bands), encompass both thick and thin filaments and constitute the central region of the sarcomere, extending across the H-zone. Collectively, the A bands and the I bands create the distinctive striped appearance of skeletal muscle tissue.[3] Tropomyosin, a protein, shields the myosin-binding sites, hindering actin from binding to myosin. It attaches to troponin, which secures it in place. During muscle relaxation, the troponin-tropomyosin complex inhibits myosin heads from binding to the active sites on actin microfilaments. Troponin also possesses a calcium ion binding site. These two regulatory proteins cooperate in response to calcium levels, overseeing sarcomere contraction. During muscle contraction, tropomyosin shifts to expose the myosin-binding site on an actin filament, allowing the interaction between actin and myosin microfilaments to occur. The initiation of contraction involves calcium ions binding to troponin, prompting a reaction that displaces tropomyosin from the actin filament binding sites. Consequently, myosin heads can attach to these exposed sites, forming cross-bridges and initiating muscle contraction.[4]