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Myofibrils are composed of long proteins including actin, myosin, and titin, and other proteins that hold them together. These proteins are organized into thick , thin , and elastic myofilaments , which repeat along the length of the myofibril in sections or units of contraction called sarcomeres .
The protein complex composed of actin and myosin, contractile proteins, is sometimes referred to as actomyosin.In striated skeletal and cardiac muscle, the actin and myosin filaments each have a specific and constant length in the order of a few micrometers, far less than the length of the elongated muscle cell (up to several centimeters in some skeletal muscle cells). [5]
Genes and their protein products that are expressed during the process include: myocyte enhancer factors, myogenic regulatory factors, and serum response factor. Expression of skeletal alpha-actin is also regulated by the androgen receptor ; steroids can thereby regulate myogenesis.
Fusion depends on muscle-specific proteins known as fusogens called myomaker and myomerger. [13] A striated muscle fiber contains myofibrils consisting of long protein chains of myofilaments. There are three types of myofilaments: thin, thick, and elastic that work together to produce a muscle contraction. [14]
Sarcomeres are composed of long, fibrous proteins as filaments that slide past each other when a muscle contracts or relaxes. The costamere is a different component that connects the sarcomere to the sarcolemma. Two of the important proteins are myosin, which forms the thick filament, and actin, which forms the thin filament. Myosin has a long ...
Cross-bridge theory states that actin and myosin form a protein complex (classically called actomyosin) by attachment of myosin head on the actin filament, thereby forming a sort of cross-bridge between the two filaments. The sliding filament theory is a widely accepted explanation of the mechanism that underlies muscle contraction.
Muscle tissue contains special contractile proteins called actin and myosin which interact to cause movement. Among many other muscle proteins, present are two regulatory proteins, troponin and tropomyosin. [1] Muscle tissue varies with function and location in the body. In vertebrates, the three types are: skeletal, cardiac (both striated), and
Their formation and turnover are regulated by many proteins, including: [citation needed] Filament end-tracking protein (e.g., formins, VASP, N-WASP) Filament-nucleator known as the Actin-Related Protein-2/3 (or Arp2/3) complex; Filament cross-linkers (e.g., α-actinin, fascin, and fimbrin) Actin monomer-binding proteins profilin and thymosin β4