MUSCLE TISSUE

Published on 19/03/2015 by admin

Filed under Pathology

Last modified 19/03/2015

Print this page

rate 1 star rate 2 star rate 3 star rate 4 star rate 5 star
Your rating: none, Average: 0 (0 votes)

This article have been viewed 2980 times

7 MUSCLE TISSUE

Muscle is one of the four basic tissues. There are three types of muscle: skeletal, cardiac, and smooth. All three types are composed of elongated cells, called muscle cells, myofibers, or muscle fibers, specialized for contraction. In all three types of muscle, energy from the hydrolysis of adenosine triphosphate (ATP) is transformed into mechanical energy.

SKELETAL MUSCLE

Muscle cells or fibers form a long multinucleated syncytium grouped in bundles surrounded by connective tissue sheaths and extending from the site of origin to their insertion (Figure 7-1). The epimysium is a dense connective tissue layer ensheathing the entire muscle. The perimysium derives from the epimysium and surrounds bundles or fascicles of muscle cells. The endomysium is a delicate layer of reticular fibers and extracellular matrix surrounding each muscle cell. Blood vessels and nerves use these connective tissue sheaths to reach the interior of the muscle. An extensive capillary network, flexible to adjust to contraction-relaxation changes, invests individual skeletal muscle cell.

The connective tissue sheaths blend and radiating-muscle fascicles interdigitate at each end of a muscle with regular dense connective tissue of the tendon to form a myotendinous junction. The tendon anchors into a bone through the periosteal Sharpey’s fibers.

Characteristics of the skeletal muscle cell or fiber

Skeletal muscle cells are formed in the embryo by the fusion of myoblasts that produce a postmitotic, multinucleated myotube. The myotube matures into the long muscle cell with a diameter of 10 to 100 μm and a length of up to several centimeters.

The plasma membrane (called the sarcolemma) of the muscle cell is surrounded by a basal lamina and satellite cells (Figure 7-2). We discuss the significance of satellite cells in muscle regeneration. The sarcolemma projects long, finger-like processes—called transverse tubules or T tubules—into the cytoplasm of the cell—the sarcoplasm. T tubules make contact with membranous sacs or channels, the sarcoplasmic reticulum. The sarcoplasmic reticulum contains high concentrations of Ca2+. The site of contact of the T tubule with the sarcoplasmic reticulum cisternae is called a triad because it consists of two lateral sacs of the sarcoplasmic reticulum and a central T tubule.

The many nuclei of the muscle fiber are located at the periphery of the cell, just under the sarcolemma.

About 80% of the sarcoplasm is occupied by myofibrils surrounded by mitochondria (called sarcosomes). Myofibrils are composed of two major filaments formed by contractile proteins: thin filaments contain actin, and thick filaments are composed of myosin (see Figure 7-2).

Depending on the type of muscle, mitochondria may be found parallel to the long axis of the myofibrils, or they may wrap around the zone of thick filaments. Thin filaments insert into each side of the Z disk (also called band, or line) and extend from the Z disk into the A band, where they alternate with thick filaments.

Components of the thin and thick filaments of the sarcomere

F-actin, the thin filament of the sarcomere, is double-stranded and twisted. F-actin is composed of globular monomers (G-actin; see Cytoskeleton in Chapter 1, Epithelium). G-actin monomers bind to each other in a head-to-tail fashion, giving the filament polarity, with barbed (plus) and pointed (minus) ends. The barbed end of actin filaments inserts into the Z disk.

Tropomyosin consists of two nearly identical α-helical polypeptides twisted around each other. Tropomyosin runs in the groove formed by F-actin strands. Each molecule of tropomyosin extends for the length of seven actin monomers and binds the troponin complex (Figure 7-5).

Troponin is a complex of three proteins: troponin I, C, and T. Troponin T binds the complex to tropomyosin. Troponin I inhibits the binding of myosin to actin. Troponin C binds Ca2+ and is found only in striated muscle.

Myosin II, the major component of the thick filament, has adenosine triphosphatase (ATPase) activity (it hydrolyzes ATP) and binds to F-actin—the major component of the thin filament—in a reversible fashion.

Myosin II consists of two identical heavy chains and two pairs of light chains (Figure 7-6; see Cytoskeleton in Chapter 1, Epithelium). At one end, each heavy chain forms a globular head. Two different light chains are bound to each head: the essential light chain and the regulatory light chain. The globular head has three distinct regions: (1) an actin-binding region; (2) an ATP-binding region; and (3) a light chain–binding region. Myosin II, like the other molecular motors kinesins and dyneins, use the chemical energy of ATP to drive conformational changes that generate motile force. As you recall, kinesins and dyneins move along microtubules. Myosins move along actin filaments to drive muscle contraction.

Nebulin (Figure 7-7) is associated with thin (actin) filaments; it inserts into the Z disk and acts as a template for determining the length of actin filaments.

Titin (see Figure 7-7) is a very large protein with a molecular mass in the range of millions. Each molecule associates with thick (myosin) myofilaments and inserts into the Z disk, extending to the bare zone of the myosin filaments, close to the M line. Titin controls the assembly of the myosin myofilament by acting as a template. Titin has a role in sarcomere elasticity by forming a spring-like connection between the end of the thick myofilament and the Z disk.

Z disks are the insertion site of actin filaments of the sarcomere. A component of the Z disk, α-actinin, anchors the barbed end of actin filaments to the Z disk.

Desmin is a 55-kd protein that forms intermediate (10-nm) filaments. Desmin filaments encircle the Z disks of myofibrils and are linked to the Z disk and to each other by plectin filaments (Figure 7-8). Desmin filaments extend from the Z disk of one myofibril to the adjacent myofibril, forming a supportive latticework. Desmin filaments also extend from the sarcolemma to the nuclear envelope.

Desmin inserts into specialized sarcolemma-associated plaques, called costameres. Costameres, acting in concert with the dystrophin-associated protein complex, transduce contractile force from the Z disk to the basal lamina, maintain the structural integrity of the sarcolemma, and stabilize the position of myofibrils in the sarcoplasm.

The heat shock protein αB-crystallin protects desmin filaments from stress-induced damage. Desmin, plectin, and αB-crystallin form a mechanical stress protective network at the Z-disk level. Mutations in these three proteins lead to the destruction of myofibrils after repetitive mechanical stress.

A depolarization signal travels inside the muscle by T tubules

We discussed that the triad consists of a transverse T tubule flanked by sacs of the sarcoplasmic reticulum, and that the sarcoplasm of a skeletal muscle cell is packed with myofibrils (each consisting of a linear repeat of sarcomeres) with abundant mitochondria between them. How does a nerve impulse reach and deliver contractile signals to myofibrils located in the interior of the muscle cell?

An excitation-contraction signal is generated by acetylcholine, a chemical transmitter released from a nerve terminal in response to an action potential. Acetylcholine diffuses into a narrow gap, called the neuromuscular junction, between the muscle and a nerve terminal (Figure 7-11). The action potential spreads from the sarcolemma to the T tubules, which transport the excitation signal to the interior of the muscle cell. Remember that T tubules form rings around every sarcomere of every myofibril at the A-I junction.

We discuss later that the companions of the T tubule, the channels of the sarcoplasmic reticulum, contain calcium ions. Calcium ions are released inside the cytosol to activate muscle contraction when the action potential reaches the T tubule. This excitation-contraction sequence occurs in about 15 milliseconds.

NEUROMUSCULAR JUNCTION: MOTOR PLATE

The neuromuscular junction is a specialized structure formed by motor nerves associated with the target muscle and visible with the light microscope.

Once inside the skeletal muscle, the motor nerve gives rise to several branches. Each branch forms swellings called presynaptic buttons covered by Schwann cells. Each nerve branch innervates a single muscle fiber. The “parent” axon and all of the muscle fibers it innervates form a motor unit. Muscles that require fine control have few muscle fibers per motor unit. Very large muscles contain several hundred fibers per motor unit.

When myelinated axons reach the perimysium, they lose their myelin sheath but the presynaptic buttons remain covered with Schwann cell processes. A presynaptic button contains mitochondria and membrane-bound vesicles filled with the neurotransmitter acetylcholine. The neurotransmitter is released at dense areas on the cytoplasmic side of the axon membrane, called active zones.

Synaptic buttons occupy a depression of the muscle fiber, called the primary synaptic cleft. In this region, the sarcolemma is thrown into deep junctional folds (secondary synaptic clefts). Acetylcholine receptors are located at the crests of the folds and voltage-gated Na+ channels are down into the folds (see Figure 7-11).

The basal lamina surrounding the muscle fiber extends into the synaptic cleft. The basal lamina contains acetylcholinesterase, which inactivates acetylcholine released from the presynaptic buttons into acetate and choline. The basal lamina covering the Schwann cell becomes continuous with the basal lamina of the muscle fiber.