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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]
A myofibril (also known as a muscle fibril or sarcostyle) [1] is a basic rod-like organelle of a muscle cell. [2] Skeletal muscles are composed of long, tubular cells known as muscle fibers, and these cells contain many chains of myofibrils. [3]
The third type of myofilament is an elastic filament composed of titin, a very large protein. In striations of muscle bands, myosin forms the dark filaments that make up the A band. Thin filaments of actin are the light filaments that make up the I band.
Myofibroblasts usually stain for the intermediate filament vimentin, which is a general mesenchymal marker, α-smooth muscle actin (human gene = ACTA2), and for palladin, which is a cytoskeletal actin scaffold protein.
Sliding filament theory: A sarcomere in relaxed (above) and contracted (below) positions. The sliding filament theory explains the mechanism of muscle contraction based on muscle proteins that slide past each other to generate movement. [1]
The myosin head is the part of the thick myofilament made up of myosin that acts in muscle contraction, by sliding over thin myofilaments of actin.Myosin is the major component of the thick filaments and most myosin molecules are composed of a head, neck, and tail domain; the myosin head binds to thin filamentous actin, and uses ATP hydrolysis to generate force and "walk" along the thin filament.
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These changes alter the myofilament response to calcium, and are of interest in targeting heart failure. Multiple reaction monitoring of human cTnI has revealed that there are 14 phosphorylation sites and the pattern of phosphorylation observed at these sites is changed in response to disease.