Myofibrils structure

Cammarato A, Dambacher CM, Knowles AE, et al. (2008) Myosin transducer mutations differentially affect motor function, myofibril structure, and the performance of skeletal and cardiac muscles. Mol Biol Cell 19, 553-62. 

FIGURE 17.11 The structure of a skeletal muscle cell, showing the mauuer iu which t-tubules enable the sarcolemmal membrane to contact the ends of each myofibril iu the muscle fiber. The foot structure is shown iu the box. 

In striated muscles, SR is well developed to surround the myofibrils and is divided into two parts, the terminal cisternae (TC) and longitudinal tubules (LT). TC forms triad (skeletal muscle) or dyad (heart) structure with transverse tubules. The ryanodine receptor is located only in the TC, whereas the Ca2+ pump/SERCA is densely packed in both TC and LT. 

Figure 1. Muscle development. A skeletal muscle fiber is formed by the fusion of many single cells (myoblasts) into a multinucleated myotube. Myotubes then develop into the muscle fiber (see text). Sarcomeres form in longitudinal structures called myofibrils. The repeating structure of the sarcomere contains interdigitating thick and thin filaments.

Histopathological features are dominated by the large number of centrally-placed muscle nuclei, sometimes affecting more than 90% of muscle fibers. The nuclei form long chains in the middle of the fiber and are surrounded by cytoplasm, which contains mitochondria and membranous vesicles, but no myofibrils. This morphological appearance has prompted comparison with myotubes, and in fact centronuclear myopathies are sometimes referred to as myotubular myopathies. This is a misnomer, however, since although the affected fibers retain some of the structural features of myotubes, and maturational arrest may play a role in their formation, the vast majority of such fibers are fully differentiated histochemically into either type 1 or type 2. 

Internally, muscle fibers are highly organized. Each fiber contains numerous myofibrils — cylindrical structures that also lie parallel to the long axis of the muscle. The myofibrils are composed of thick filaments and thin filaments. It is the arrangement of these filaments that creates alternating light and dark bands observed microscopically along the muscle fiber. Thus, skeletal muscle is also referred to as striated muscle. 

The muscle is a highly organized tissue, built up of individual cells known as fibres, which are held together by connective tissue. Each muscle fibre consists of a high number of single strands of myofibrils. The myofibrils are again comprised of myofilaments. The myofilaments are divided into thin and thick filaments, which mainly contain two filamentary proteins, actin and myosin, respectively. The myofibrils occupy approximately 80% of the muscle cell volume, and the majority of the water, which makes up about 75% of the muscle, is located in the spaces between thin and thick filaments. A schematic drawing of muscle structure is shown in Fig. 1. 

The anatomical unit of muscle is an elongated cell called a fibre. Each individual fibre cell consists of myofibrils which are bundles of contractile protein filaments composed of actin and myosin (Figure 7.1). Differences in structure indicate that muscles have evolved to perform particular functions. Although the structure of fibres, myofibrils and filaments of actin and myosin, is similar in all muscle types, their arrangement, action and control allow identification of three tissue types ... 

Fig. 2. Macroscopic and microscopic structure of muscle (a) Entire muscle and its cross-section with fatty septa, (b) Fascicle with several muscle fibres (cells). A layer of fat along the fascicle is indicated, (c) Striated myofibre corresponding with one single muscle cell containing several nuclei. The lengths of a myofibre can be several tens of centimetres, (d) Myofibril inside a myocyte. It is one contractile element and contains actin and myosin and further proteins important for the muscular function, (e) Electron myograph of human skeletal muscle showing the band structure caused by the contractile myofilaments in the sarcomeres. One nucleus (Nu) and small glycogen granules (arrow, size <0.1 pm) are indicated.

Actin and myosin are the two principal muscle proteins in the myofibrils (Fig. 2d). They are arranged in a cylindrical structure, usually with six thin actin strands surrounding a thicker myosin fibril. The myosin fibril has... 

In the cells of this tissue, which are known as fibres, the two major proteins, actin and myosin, are orgaiused to form myofibrils. These are structural rods that can contract (Figure 1.11). This enables muscle cells to shorten, which provides for movement and locomotion (Figure 1.12). There are three types ... 

In 1987 the gene responsible for muscular dystrophy was identified, leading to the isolation of a protein, known as dystrophin, which is either totally absent in Duchenne, or partially absent in the Becker type. The protein is located on the inside of the plasma membrane of all muscles (and some neurones). Although its precise function is not known, the mutant form results in structural abnormalities of the plasma member which results in degradation of myofibrils, but the hnk between the abnormalities of the membrane and degradation is not known. One theory is that it leads to an increase in the activity of a Ca " ion channel in the membrane and, therefore, a marked increase in the Ca ion concentration in the cytosol. This chronic elevation results in the activation of calpain, which leads to protein breakdown and the degeneration within the fibre (Chapter 13). 

Lakritz et al. (32) reported that radiation doses of less than 10 kGy (at 0 to 4 C) produced minimal changes in the micro structure of bovine longissimus dorsi muscle. At doses of 30 kGy or higher, myofibril fragmentation and decreased tensile strength were noted. Lakritz and Maerker (33) reported reductions of 8% and 42% in the activities of lysosomal enzymes and acid phosphatase of irradiated (10 kGy) bovine longissimus dorsi muscle tissue. 

FIGURE 5-31 Structure of skeletal muscle, (a) Muscle fibers consist of single, elongated, multinucleated cells that arise from the fusion of many precursor cells. Within the fibers are many myofibrils (only six are shown here for simplicity) surrounded by the membranous sarcoplasmic reticulum. The organization of thick and thin filaments in the myofibril gives it a striated appearance. When muscle contracts, the I bands narrow and the Z disks come closer together, as seen in electron micrographs of (b) relaxed and (c) contracted muscle. 

That actin and myosin are jointly responsible for contraction was demonstrated long before the fine structure of the myofibril became known. In about 1929, ATP was recognized as the energy source for muscle contraction, but it was not until 10 years later that Engelhardt and Ljubimowa showed that isolated myosin preparations catalyzed the hydrolysis of ATP.138 Szent-Gyorgi139 140 showed that a combination of the two proteins actin (discovered by F. Straub141) and myosin was required for Mg2+-stimulated ATP hydrolysis (ATPase activity). He called this combination actomyosin. 

Myofibrils exhibit longitudinally repeating structures called sarcomeres. The fine structure of the sarcomere is described in figure 5.16. 

Electron micrograph of a longitudinal section of a skeletal muscle fiber showing a number of myofibrils. Muscle protein is an unusual example of a structural protein with enzymatic activity. (Courtesy of Dr. Hugh Huxley)... 

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