Structure of skeletal muscle

Muscle fibers are incapable of mitosis. In fact, the number of muscle fibers per muscle is likely determined by the second trimester of fetal development. Therefore, enlargement of a whole muscle is not due to an increase in the number of fibers in the muscle, but rather to the hypertrophy of existing fibers. Because muscle fibers have no gap junctions between them, electrical activity cannot spread from one cell to the next. Therefore, each muscle fiber is innervated by a branch of an alpha motor neuron. A motor unit is defined as an alpha motor neuron and all of the muscle fibers that it innervates. 

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. 

Thin filaments. The thin filaments are composed of three proteins  

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Figure 2. Representation of the three dimensional structure of skeletal muscle.

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. 

FIGURE 2.2 Schematic structure of skeletal muscle tendon (1), epimysium (2), perimysium (3), endomysium (4), sarcolemma (5), myofibril (6), muscle fiber (7), and bundle of muscle fibers (8). 

Figure 21-1 schematically illustrates the structure of skeletal muscle. Individual muscle cells, or fibers, are elongated, roughly cylindrical, and usually unbranched, with a mean diameter of 10-100 jxm. The plasma membrane of muscle fibers is called the sarcolemma, and fibers are surrounded by structural filaments of the extracellular matrix which are often described as forming a basement membrane. 

Fig. 7). In this case, splicing of the pre-mRNA results in the insertion or omission of 7 amino acids after amino acid 209, near the ATP binding region (Kelley et al., 1993 Babij, 1993 White et al., 1993). When superimposed on the 3D structure of skeletal muscle HC S-1, this sequence of amino acids is part of what is postulated to be a flexible surface loop that does not appear in the crystal structure and is referred to as loop 1 (see Section IIEB). 

It is useful to first consider the structure of muscle s mechanochemical transduction elements, actin and the subfragment-1 (S-1) portion of myosin, before analyzing the effects of regulatory proteins that modulate interactions of the two and have the potential therefore to control force generation. Molecular details of the structure of skeletal muscle actin (Kabsch et al, 1990 Holmes and Kabsch, 1991 Lorenz et al., 1993) and S-1 (Rayment etal., 1993a) are known at the atomic level (Fig. 1), and given the general similarity of F-actin and S-1 in smooth and in skeletal muscle, it is reasonable to assume that they are closely related in the two... 

IV. The Proteins of the Myofibril and the Fine Structure of Skeletal Muscle... 237... 

Wei, R., A. Bhattacharya, R. T. Hamilton et al. Differential effects of mutant SODl on protein structure of skeletal muscle and spinal cord of familial amyotrophic lateral sclerosis Role of chaperone network. 438(1), 2013 218-23. 

The cells of the latter three types contain only a single nucleus and are called myocytes. The cells of skeletal muscle are long and multinucleate and are referred to as muscle fibers. At the microscopic level, skeletal muscle and cardiac muscle display alternating light and dark bands, and for this reason are often referred to as striated muscles. The different types of muscle cells vary widely in structure, size, and function. In addition, the times required for contractions and relaxations by various muscle types vary considerably. The fastest responses (on the order of milliseconds) are observed for fast-twitch skeletal... 

The structure of heart myocytes is different from that of skeletal muscle fibers. Heart myocytes are approximately 50 to 100 p,m long and 10 to 20 p,m in diameter. The t-tubules found in heart tissue have a fivefold larger diameter than those of skeletal muscle. The number of t-tubules found in cardiac muscle differs from species to species. Terminal cisternae of mammalian cardiac muscle can associate with other cellular elements to form dyads as well as triads. The association of terminal cisternae with the sarcolemma membrane in a dyad structure is called a peripheral coupling. The terminal cisternae may also form dyad structures with t-tubules that are called internal couplings (Figure 17.31). As with skeletal muscle, foot structures form the connection between the terminal cisternae and t-tubule membranes. 

Organization into macromolecular structures. There are no apparent templates necessary for the assembly of muscle filaments. The association of the component proteins in vitro is spontaneous, stable, and relatively quick. Filaments will form in vitro from the myosins or actins from all three kinds of muscle. Yet in vitro smooth muscle myosin filaments are found to be stable only in solutions somewhat different from in vivo conditions. The organizing principles which govern the assembly of myosin filaments in smooth muscle are not well understood. It is clear, however, a filament is a sturdy structure and that individual myosin molecules go in and out of filaments whose structure remains in a functional steady-state. As described above, the crossbridges sticking out of one side of a smooth muscle myosin filament are all oriented and presumably all pull on the actin filament in one direction along the filament axis, while on the other side the crossbridges all point and pull in the opposite direction. The complement of minor proteins involved in the structure of the smooth muscle myosin filament is unknown, albeit not the same as that of skeletal muscle since C-protein and M-protein are absent. 

Acquired disease of muscle is more common than is generally appreciated. It may result from the use of drugs—prescription or nonprescription—that have a recognized capacity to compromise the structure or function of skeletal muscle. Drugs particularly well recognized as myotoxic include clofibrate and its derivatives, anabolic steroids, penicillamine, and emetine. Many nonprescription drugs, including alcohol and laxatives, are directly or indirectly myotoxic. Other forms of acquired myopathies include the acute myopathic conditions caused by the bites of many snakes. 

Just a year after Stephenson s classical paper of 1956, J. del Castillo and B. Katz published an electrophysiological study of the interactions that occurred when pairs of agonists with related structures were applied simultaneously to the nicotinic receptors at the endplate region of skeletal muscle. Their findings could be best explained in terms of a model for receptor activation that has already been briefly introduced in Section 1.2.3 (see particularly Eq. (1.7)). In this scheme, the occupied receptor can isomerize between an active and an inactive state. This is very different from the classical model of Hill, Clark, and Gaddum in which no clear distinction was made between the occupation and activation of a receptor by an agonist. 

Zot, A. S. and Potter, J. D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Biophys. Chem. 16 535-560,1987. 

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.

At the neuromuscular junction, it produces the contraction of skeletal muscle by its direct action and by inactivation of anticholinesterase and has got anticurare action. By virtue of its structural similarity to acetylcholine, it acts as partial agonist on motor end plate. 

Diagram of the structures involved in the stretch reflex arc. I is an inhibitory interneuron E indicates an excitatory presynaptic terminal la is a primary intrafusal afferent fiber Ca2+ denotes activator calcium stored in the sarcoplasmic reticulum of skeletal muscle RyR channels indicates the Ca2+ release channels. 

There have been three reports of the same dimeric disulfide. It was first isolated from an unidentified sponge from Guam and the structure elucidated by analysis of spectral data. The (E,E) stereochemistry of the disulfide (500) was defined by comparing the I3C NMR spectroscopic data with those of the (E,Z)-isomer (501) that was obtained as an unstable minor product [425]. Compound 500 was isolated from a species of Psammaplysilla and was called psammaplin A [426]. It was also isolated from Thorectopsamma xana, collected from the same location in Guam, together with a minor dimeric metabolite bisaprasin (502). Both compounds inhibited growth of Staphylococcus aureus and Bacillus subtilis [427]. Psammaplin A (bisprasin) (500) was later isolated from a Dysidea species of sponge and shown to act on Ca2+-induced Ca2+ release channels of skeletal muscle [428]. 

Knowledge of the chemical structures of the major vitamins was acquired during the 30 years after 1920, and some were identified as known compounds. They were classified as fat-soluble and water-soluble vitamins. The only heterocyclic compounds in the former class are the tocopherols (vitamin E). They were discovered through their action in preventing sterility in rats, but they appear to play an important part in the metabolism of skeletal muscle. Vitamin E deficiency appears to occur rarely in man, but vitamin E therapy is tried in a number of clinical disorders. The tocopherols may be isolated from vegetable oils, and synthetic a-tocopherol (61) is made by condensing trimethylhydroquinone with phytol or phytyl halides (Scheme 2). For medicinal use they may be converted into their acetates or succinates. 

Several uncertainties have complicated our understanding of the role of Ca2+ in signaling. What is the source of Ca2+ How much of it enters cells from the outside and how much is released from internal stores Where are the internal stores What other kinds of ion channels are present and what second messengers regulate them The sarcoplasmic reticulum of skeletal muscle and also membranes in many other cells contain ryanodine receptors as well as InsP3 receptors.282 293 Both of these receptors have similar structures and contain Ca2+ channels. However, the ryanodine receptors are activated by cyclic ADP ribose (cADPR),294/295 which was first discovered as a compound inducing the release of Ca2+ in sea urchin eggs.296 The 2-phospho derivative of cADPR may also have a similar function.297... 

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