Skeletal muscle sarcomeres

Itoh, Y., Suzuki, T., and Kimura, S. (1988). Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. / Biochem. (Tokyo) 104, 504-508. 

Fig. 14. Diagram of the parallel elastic component of vertebrate skeletal muscle sarcomere. Connectin filaments originating from the edges of the central bare zone of a thick (myosin) filament run through the thin (aclin) filament to the Z lines.

Immunostaining studies of cells isolated from the contracting areas within the EBs confirmed the presence of cardiac-specific proteins (MHC, sarcomeric a-actinin, des-min, cTnf, ANP). These studies also demonstrated the presence of early-cardiac morphology with a typical early-striated staining pattern. The cells, however, did not exhibit immunoreactivify with anti-nebuhn monoclonal antibodies (mAbs), a specific skeletal muscle sarcomeric protein shown to be expressed early in skeletal myoblast differentiation. 

FIGURE 17.12 Electron micrograph of a skeletal muscle myofibril (in longitndinal section). The length of one sarcomere is indicated, as are the A and I bands, the H zone, the M disk, and the Z lines. Cross-sections from the H zone show a hexagonal array of thick filaments, whereas the I band cross-section shows a hexagonal array of thin filaments. (Photo courtesy of Hugh Huxley, Brandeis University)... 

The principal molecular constituent of thin filaments is actin. Actin has been highly conserved during the course of evolution and is present in all eukaryotes, including single-celled organisms such as yeasts. Actin was first extracted and purified from skeletal muscle, where it forms the thin filaments of sarcomeres. It also is the main contractile protein of smooth muscle. Refined techniques for the detection of small amounts of actin (e.g., immunofluorescence microscopy, gel electrophoresis, and EM cytochemistry) subsequently confirmed the presence of actin in a great variety of nonmuscle cells. Muscle and nonmuscle actins are encoded by different genes and are isoforms. 

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.

Smooth muscles have molecular structures similar to those in striated muscle, but the sarcomeres are not aligned so as to generate the striated appearance. Smooth muscles contain a-actinin and tropomyosin molecules, as do skeletal muscles. They do not have the troponin system, and the fight chains of smooth muscle myosin molecules differ from those of striated muscle myosin. Regulation of smooth muscle contraction is myosin-based, unlike striated muscle, which is actin-based. However, like striated muscle, smooth muscle contraction is regulated by Ca. ... 

The contractile elements in smooth muscle are not organized into sarcomeres. Furthermore, the resting length of smooth muscle is much shorter than its optimal length. In other words, this muscle can be significantly stretched and the amount of tension developed may actually increase because the muscle is closer to its optimal length. Finally, thick filaments are longer in smooth muscle than they are in skeletal muscle. As a result, overlap... 

Skeletal muscle is under conscious control. Each fibre is an enormous, multi-nucleate cell, formed by fusing hundreds of myoblasts end-to-end. They show a striated pattern, reflecting the regular arrangement of sarcomeres within each cell. 

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.

Fig. 4. Electron myograph of skeletal muscle. The band structure caused by the sarcomeres, two capillaries (1) and several small lipid droplets (2) are shown. The intramyocellular lipid droplets (size approximately 0.1-1 pm) make up the IMCL content mentioned in the context.

Figure 1.12 Diagrammatic interpretation of contraction in a myo-fibril of skeletal muscle. The diagram shows a single sarcomere, the basic contractile unit, limited at each end by a Z-disc. Muscle fibres are packed with hundreds of parallel myofibrils, each of which consists of many, often thousands, of sarcomeres arranged end to end. Contraction is the conseguence of the thin actin filaments being pulled over the thick filaments to increase the region of overlap and telescope the sarcomere.

The striation of the muscle fibers is characteristic of skeletal muscle. It results from the regular arrangement of molecules of differing density. The repeating contractile units, the sarcomeres, are bounded by Z lines from which thin filaments of F-actin (see p. 204) extend on each side. In the A bands, there are also thick parallel filaments of myosin. The H bands in the middle of the A bands only contain myosin, while only actin is found on each size of the Z lines. 

Figure 19-6 (A) The structure of a typical sarcomere of skeletal muscle. The longitudinal section depicted corresponds to that of the electron micrograph, Fig. 19-7A. The titin molecules in their probable positions are colored green. The heads of only a fraction of the myosin molecules are shown protruding toward the thin actin filaments with which they interact.

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