Portal:Muscle tissue
Portal maintenance status: (October 2018)
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Introduction
Muscle tissue is a soft tissue that composes muscles in animal bodies, and gives rise to muscles' ability to contract. This is opposed to other components or tissues in muscle such as tendons or perimysium. It is formed during embryonic development through a process known as myogenesis.
Muscle tissue varies with function and location in the body. In mammals the three types are: skeletal or striated muscle; smooth or non-striated muscle; and cardiac muscle, which is sometimes known as semi-striated. Smooth and cardiac muscle contracts involuntarily, without conscious intervention. These muscle types may be activated both through interaction of the central nervous system as well as by receiving innervation from peripheral plexus or endocrine (hormonal) activation. Striated or skeletal muscle only contracts voluntarily, upon influence of the central nervous system. Reflexes are a form of non-conscious activation of skeletal muscles, but nonetheless arise through activation of the central nervous system, albeit not engaging cortical structures until after the contraction has occurred.
Selected general articles
A myocyte (also known as a muscle cell) is the type of cell found in muscle tissue. Myocytes are long, tubular cells that develop from myoblasts to form muscles in a process known as myogenesis. There are various specialized forms of myocytes: cardiac, skeletal, and smooth muscle cells, with various properties. The striated cells of cardiac and skeletal muscles are referred to as muscle fibers. Cardiomyocytes are the muscle fibres that form the chambers of the heart, and have a single central nucleus. Skeletal muscle fibers help support and move the body and tend to have peripheral nuclei. Smooth muscle cells control involuntary movements such as the peristalsis contractions in the oesophagus and stomach. Read more...- Gamma-sarcoglycan is a protein that in humans is encoded by the SGCG gene. The α to δ-sarcoglycans are expressed predominantly (β) or exclusively (α, γ and δ) in striated muscle. A mutation in any of the sarcoglycan genes may lead to a secondary deficiency of the other sarcoglycan proteins, presumably due to destabilisation of the sarcoglycan complex. The disease-causing mutations in the α to δ genes cause disruptions within the dystrophin-associated protein (DAP) complex in the muscle cell membrane. The transmembrane components of the DAP complex link the cytoskeleton to the extracellular matrix in adult muscle fibres, and are essential for the preservation of the integrity of the muscle cell membrane. Read more...
- Dystroglycan is a protein that in humans is encoded by the DAG1 gene.
Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in Homo sapiens on chromosome 3. There are two exons that are separated by a large intron. The spliced exons code for a protein product that is finally cleaved into two non-covalently associated subunits, [alpha] (N-terminal) and [beta] (C-terminal). Read more...
Skeletal muscle, with sarcolemma labeled at upper left.
The sarcolemma (sarco (from sarx) from Greek; flesh, and lemma from Greek; sheath) also called the myolemma, is the cell membrane of a striated muscle fiber cell.
It consists of a lipid bilayer and a thin outer coat of polysaccharide material (glycocalyx) that contacts the basement membrane. The basement membrane contains numerous thin collagen fibrils and specialized proteins such as laminin that provide a scaffold to which the muscle fiber can adhere. Through transmembrane proteins in the plasma membrane, the actin skeleton inside the cell is connected to the basement membrane and the cell's exterior. At each end of the muscle fiber, the surface layer of the sarcolemma fuses with a tendon fiber, and the tendon fibers, in turn, collect into bundles to form the muscle tendons that adhere to bones.
The sarcolemma generally maintains the same function in muscle cells as the plasma membrane does in other eukaryote cells. It acts as a barrier between the extracellular and intracellular compartments, defining the individual muscle fiber from its surroundings. The lipid nature of the membrane allows it to separate the fluids of the intra- and extracellular compartments, since it is only selectively permeable to water through aquaporin channels. As in other cells, this allows for the compositions of the compartments to be controlled by selective transport through the membrane. Membrane proteins, such as ion pumps, may create ion gradients with the consumption of ATP, that may later be used to drive transport of other substances through the membrane (co-transport) or generate electrical impulses such as action potentials. Read more...- Caveolin-3 is a protein that in humans is encoded by the CAV3 gene. Alternative splicing has been identified for this locus, with inclusion or exclusion of a differentially spliced intron. In addition, transcripts utilize multiple polyA sites and contain two potential translation initiation sites. Read more...
A sarcomere (Greek sarx "flesh", meros "part") is the basic unit of striated muscle tissue. It is the repeating unit between two Z lines. Skeletal muscles are composed of tubular muscle cells (myocytes called muscle fibers or myofibers) which are formed in a process known as myogenesis. Muscle fibers contain numerous tubular myofibrils. Myofibrils are composed of repeating sections of sarcomeres, which appear under the microscope as alternating dark and light bands. Sarcomeres are composed of long, fibrous proteins as filaments that slide past each other when a muscle contracts or relaxes.
Two of the important proteins are myosin, which forms the thick filament, and actin, which forms the thin filament. Myosin has a long, fibrous tail and a globular head, which binds to actin. The myosin head also binds to ATP, which is the source of energy for muscle movement. Myosin can only bind to actin when the binding sites on actin are exposed by calcium ions. Read more...- Myotilin is a protein that in humans is encoded by the MYOT gene. Myotilin (myofibrillar titin-like protein) also known as TTID (TiTin Immunoglobulin Domain) is a muscle protein that is found within the Z-disc of sarcomeres. Read more...
The sliding filament theory explains the mechanism of muscle contraction based on muscle proteins that slide past each other to generate movement. It was independently introduced in 1954 by two research teams, one consisting of Andrew F. Huxley and Rolf Niedergerke from the University of Cambridge, and the other consisting of Hugh Huxley and Jean Hanson from the Massachusetts Institute of Technology. It was originally conceived by Hugh Huxley in 1953. Andrew Huxley and Niedergerke introduced it as a "very attractive" hypothesis.
According to the sliding filament theory, the myosin (thick) filaments of muscle fibers slide past the actin (thin) filaments during muscle contraction, while the two groups of filaments remain at relatively constant length. Before the 1950s there were several competing theories on muscle contraction, including electrical attraction, protein folding, and protein modification. The novel theory directly introduced a new concept called cross-bridge theory (classically swinging cross-bridge, now mostly referred to as cross-bridge cycle) which explains the molecular mechanism of sliding filament. Cross-bridge theory states that actin and myosin form a protein complex (classically called actomyosin) by attachment of myosin head on the actin filament, thereby forming a sort of cross-bridge between the two filaments. These two complementary hypotheses turned out to be the correct description, and became a universally accepted explanation of the mechanism of muscle movement. Read more...
Intercalated discs are microscopic identifying features of cardiac muscle. Cardiac muscle consists of individual heart muscle cells (cardiomyocytes) connected by intercalated discs to work as a single functional organ or syncytium. By contrast, skeletal muscle consists of multinucleated muscle fibers and exhibit no intercalated discs. Intercalated discs support synchronized contraction of cardiac tissue. They occur at the Z line of the sarcomere and can be visualized easily when observing a longitudinal section of the tissue.
Three types of cell junction make up an intercalated disc — fascia adherens, desmosomes and gap junctions.- Fascia adherens are anchoring sites for actin, and connect to the closest sarcomere.
- Desmosomes stop separating during contraction by binding filaments, joining the cells together. Desmosomes are also known as macula adherens.
- Gap junctions allow action potentials to spread between cardiac cells by permitting the passage of ions between cells, producing depolarization of the heart muscle.
Myofilaments are the filaments of myofibrils, constructed from proteins, principally myosin or actin. Types of muscle are striated muscle (such as skeletal muscle and cardiac muscle), obliquely striated muscle (found in some invertebrates), and smooth muscle. Various arrangements of myofilaments create different muscles. Striated muscle has transverse bands of filaments. In obliquely striated muscle, the filaments are staggered. Smooth muscle has irregular arrangements of filaments. Read more...
Skeletal muscle is one of three major muscle types, the others being cardiac muscle and smooth muscle. It is a form of striated muscle tissue, which is under the voluntary control of the somatic nervous system. Most skeletal muscles are attached to bones by bundles of collagen fibers known as tendons.
A skeletal muscle refers to multiple bundles (fascicles) of cells joined together called muscle fibers. The fibres and muscles are surrounded by connective tissue layers called fasciae. Muscle fibres, or muscle cells, are formed from the fusion of developmental myoblasts in a process known as myogenesis. Muscle fibres are cylindrical, and have more than one nucleus. They also have multiple mitochondria to meet energy needs. Read more...- Desmin is a protein that in humans is encoded by the DES gene. Desmin is a muscle-specific, type III intermediate filament that integrates the sarcolemma, Z disk, and nuclear membrane in sarcomeres and regulates sarcomere architecture. Read more...
- Nebulin is an actin-binding protein which is localized to the thin filament of the sarcomeres in skeletal muscle. It is a very large protein (600–900 kDa) and binds as many as 200 actin monomers. Because its length is proportional to thin filament length, it is believed that nebulin acts as a thin filament "ruler" and regulates thin filament length during sarcomere assembly. Other functions of nebulin, such as a role in cell signaling, remain uncertain.
Nebulin has also been shown to regulate actin-myosin interactions by inhibiting ATPase activity in a calcium-calmodulin sensitive manner. Read more...
Calmodulin (CaM) (an abbreviation for calcium-modulated protein) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of calmodulin. Once bound to Ca2+, calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases. Read more...- Tropomyosin is a two-stranded alpha-helical coiled coil protein found in cell cytoskeletons. Read more...
Mammalian muscle spindle showing typical position in a muscle (left), neuronal connections in spinal cord (middle) and expanded schematic (right). The spindle is a stretch receptor with its own motor supply consisting of several intrafusal muscle fibres. The sensory endings of a primary (group Ia) afferent and a secondary (group II) afferent coil around the non-contractile central portions of the intrafusal fibres. Gamma motoneurons activate the intrafusal muscle fibres, changing the resting firing rate and stretch-sensitivity of the afferents.
Muscle spindles are stretch receptors within the body of a muscle that primarily detect changes in the length of the muscle. They convey length information to the central nervous system via afferent nerve fibers. This information can be processed by the brain to determine the position of body parts. The responses of muscle spindles to changes in length also play an important role in regulating the contraction of muscles, by activating motor neurons via the stretch reflex to resist muscle stretch.
The muscle spindle has both sensory and motor components.- Sensory information conveyed by primary type Ia sensory fibers and secondary type II sensory fibers, which spiral around muscle fibres within the spindle
- Motor action by up to a dozen gamma motor neurons and to a lesser extent by one or two beta motor neurons that activate muscle fibres within the spindle.
Ribbon diagram of G-actin. ADP bound to actin's active site (multi color sticks near center of figure) as well as a complexed calcium dication (green sphere) are highlighted.
Actin is a family of globular multi-functional proteins that form microfilaments. It is found in essentially all eukaryotic cells (the only known exception being nematode sperm), where it may be present at a concentration of over 100 μM; its mass is roughly 42-kDa, with a diameter of 4 to 7 nm.
An actin protein is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. It can be present as either a free monomer called G-actin (globular) or as part of a linear polymer microfilament called F-actin (filamentous), both of which are essential for such important cellular functions as the mobility and contraction of cells during cell division. Read more...
A neuromuscular junction (or myoneural junction) is a chemical synapse formed by the contact between a motor neuron and a muscle fiber. It is at the neuromuscular junction that a motor neuron is able to transmit a signal to the muscle fiber, causing muscle contraction.
Muscles require innervation to function—and even just to maintain muscle tone, avoiding atrophy. Synaptic transmission at the neuromuscular junction begins when an action potential reaches the presynaptic terminal of a motor neuron, which activates voltage-dependent calcium channels to allow calcium ions to enter the neuron. Calcium ions bind to sensor proteins (synaptotagmin) on synaptic vesicles, triggering vesicle fusion with the cell membrane and subsequent neurotransmitter release from the motor neuron into the synaptic cleft. In vertebrates, motor neurons release acetylcholine (ACh), a small molecule neurotransmitter, which diffuses across the synaptic cleft and binds to nicotinic acetylcholine receptors (nAChRs) on the cell membrane of the muscle fiber, also known as the sarcolemma. nAChRs are ionotropic receptors, meaning they serve as ligand-gated ion channels. The binding of ACh to the receptor can depolarize the muscle fiber, causing a cascade that eventually results in muscle contraction. Read more...
Troponin, or the troponin complex, is a complex of three regulatory proteins (troponin C, troponin I, and troponin T) that is integral to muscle contraction in skeletal muscle and cardiac muscle, but not smooth muscle.
Discussions of troponin often pertain to its functional characteristics and usefulness as a diagnostic marker or therapeutic target for various heart disorders, in particular as a highly specific marker for myocardial infarction or heart muscle cell death. Read more...
Muscle contraction is the activation of tension-generating sites within muscle fibers. In physiology, muscle contraction does not necessarily mean muscle shortening because muscle tension can be produced without changes in muscle length such as holding a heavy book or a dumbbell at the same position. The termination of muscle contraction is followed by muscle relaxation, which is a return of the muscle fibers to their low tension-generating state.
Muscle contractions can be described based on two variables: length and tension. A muscle contraction is described as isometric if the muscle tension changes but the muscle length remains the same. In contrast, a muscle contraction is isotonic if muscle tension remains the same throughout the contraction. If the muscle length shortens, the contraction is concentric; if the muscle length lengthens, the contraction is eccentric. In natural movements that underlie locomotor activity, muscle contractions are multifaceted as they are able to produce changes in length and tension in a time-varying manner. Therefore, neither length nor tension is likely to remain the same in muscles that contract during locomotor activity. Read more...
Skeletal muscle, with T-tubule labelled in zoomed in image.
Transverse tubules (T-tubules) are extensions of the cell membrane that penetrate into the centre of skeletal and cardiac muscle cells. With membranes that contain large concentrations of ion channels, transporters, and pumps, T-tubules permit rapid transmission of the action potential into the cell, and also play an important role in regulating cellular calcium concentration. Through these mechanisms, T-tubules allow heart muscle cells to contract more forcefully by synchronising calcium release throughout the cell. T-tubule structure may be affected by disease, potentially contributing to heart failure and arrhythmias. Although these structures were first seen in 1897, research into T-tubule biology is ongoing. Read more...
The sarcoplasmic reticulum (SR) is a membrane-bound structure found within muscle cells that is similar to the endoplasmic reticulum in other cells. The main function of the SR is to store calcium ions (Ca2+). Calcium ion levels are kept relatively constant, with the concentration of calcium ions within a cell being 100,000 times smaller than the concentration of calcium ions outside the cell. This means that small increases in calcium ions within the cell are easily detected and can bring about important cellular changes (the calcium is said to be a second messenger; see calcium in biology for more details). Calcium is used to make calcium carbonate (found in chalk) and calcium phosphate, two compounds that the body uses to make teeth and bones. This means that too much calcium within the cells can lead to hardening (calcification) of certain intracellular structures, including the mitochondria, leading to cell death. Therefore, it is vital that calcium ion levels are controlled tightly, and can be released into the cell when necessary and then removed from the cell. Read more...- Dysferlin also known as dystrophy-associated fer-1-like protein is a protein that in humans is encoded by the DYSF gene.
Dysferlin is linked with skeletal muscle repair. A defect in the DYSF gene, located on chromosome 2p12-14, results in several types of muscular dystrophy; including Miyoshi myopathy (MM), Limb-girdle muscular dystrophy type 2B (LGMD2B) and Distal Myopathy (DM). A reduction or absence of dysferlin, termed dysferlinopathy, usually becomes apparent in the third or fourth decade of life and is characterised by weakness and wasting of various voluntary skeletal muscles. Read more...
Sarcoplasm is the cytoplasm of a myocyte (muscle fiber). It is comparable to the cytoplasm of other cells, but it contains unusually large amounts of glycosomes (granules of stored glycogen) and significant amounts of myoglobin, an oxygen-binding protein. The calcium ion concentration in sarcoplasma is also a special element of the muscle fiber; it is the means by which muscle contractions take place and are regulated.
It contains mostly myofibrils (which are composed of sarcomeres), but its contents are otherwise comparable to those of the cytoplasm of other cells. It has a Golgi apparatus near the nucleus, mitochondria just inside the cell membrane (sarcolemma), and a smooth endoplasmic reticulum (specialized for muscle function and called the sarcoplasmic reticulum). Read more...
Vascular smooth muscle refers to the particular type of smooth muscle found within, and composing the majority of the wall of blood vessels. Read more...- A motor unit is made up of a motor neuron and the skeletal muscle fibers innervated by that motor neuron's axonal terminals. Groups of motor units often work together to coordinate the contractions of a single muscle; all of the motor units within a muscle are considered a motor pool. The concept was proposed by Charles Scott Sherrington.
All muscle fibres in a motor unit are of the same fibre type. When a motor unit is activated, all of its fibres contract. In vertebrates, the force of a muscle contraction is controlled by the number of activated motor units. Read more... - Myosatellite cells or satellite cells are small multipotent cells with virtually no cytoplasm found in mature muscle. Satellite cells are precursors to skeletal muscle cells, able to give rise to satellite cells or differentiated skeletal muscle cells. They have the potential to provide additional myonuclei to their parent muscle fiber, or return to a quiescent state. More specifically, upon activation, satellite cells can re-enter the cell cycle to proliferate and differentiate into myoblasts.
Myosatellite cells are located between the basement membrane and the sarcolemma of muscle fibers, and can lie in grooves either parallel or transversely to the longitudinal axis of the fibre. Their distribution across the fibre can vary significantly. Non-proliferative, quiescent myosatellite cells, which adjoin resting skeletal muscles, can be identified by their distinct location between sarcolemma and basal lamina, a high nuclear-to-cytoplasmic volume ratio, few organelles (e.g. ribosomes, endoplasmic reticulum, mitochondria, golgi complexes), small nuclear size, and a large quantity of nuclear heterochromatin relative to myonuclei. On the other hand, activated satellite cells have an increased number of caveolae, cytoplasmic organelles, and decreased levels of heterochromatin. Satellite cells are able to differentiate and fuse to augment existing muscle fibers and to form new fibers. These cells represent the oldest known adult stem cell niche, and are involved in the normal growth of muscle, as well as regeneration following injury or disease. Read more...
Microfilaments, also called actin filaments, are filaments in the cytoplasm of eukaryotic cells that form part of the cytoskeleton and are primarily composed of polymers of actin, but in cells are modified by and interact with numerous other proteins. Microfilaments are usually about 7 nm in diameter and composed of two strands of actin. Microfilament functions include cytokinesis, amoeboid movement and cell motility in general, changes in cell shape, endocytosis and exocytosis, cell contractility and mechanical stability. Microfilaments are flexible and relatively strong, resisting buckling by multi-piconewton compressive forces and filament fracture by nanonewton tensile forces. In inducing cell motility, one end of the actin filament elongates while the other end contracts, presumably by myosin II molecular motors. Additionally, they function as part of actomyosin-driven contractile molecular motors, wherein the thin filaments serve as tensile platforms for myosin's ATP-dependent pulling action in muscle contraction and pseudopod advancement. Microfilaments have a tough, flexible framework which helps the cell in movement. Read more...
Troponin C is a part of the troponin complex. It contains four calcium-binding EF hands, although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of thin filaments (along with actin and tropomyosin). It contains an N lobe and a C lobe. The C lobe serves a structural purpose and binds to the N domain of troponin I (TnI). The C lobe can bind either Ca2+ or Mg2+. The N lobe, which binds only Ca2+, is the regulatory lobe and binds to the C domain of troponin I after calcium binding.
The tissue specific subtypes are:- Slow troponin C, TNNC1 (3p21.3-p14.3, Online Mendelian Inheritance in Man (OMIM) 191040)
- Fast troponin C, TNNC2 (20q12-q13.11, Online Mendelian Inheritance in Man (OMIM) 191039)
Myosins (/ˈmaɪəsɪn,-oʊ-/) are a superfamily of motor proteins best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility. The term was originally used to describe a group of similar ATPases found in the cells of both striated muscle tissue and smooth muscle tissue. Following the discovery by Pollard and Korn (1973) of enzymes with myosin-like function in Acanthamoeba castellanii, a global range of divergent myosin genes have been discovered throughout the realm of eukaryotes.
Although myosin was originally thought to be restricted to muscle cells (hence myo-(s) + -in), there is no single "myosin"; rather it is a very large superfamily of genes whose protein products share the basic properties of actin binding, ATP hydrolysis (ATPase enzyme activity), and force transduction. Virtually all eukaryotic cells contain myosin isoforms. Some isoforms have specialized functions in certain cell types (such as muscle), while other isoforms are ubiquitous. The structure and function of myosin is globally conserved across species, to the extent that rabbit muscle myosin II will bind to actin from an amoeba. Read more...
In human, the DMD gene is located on the short (p) arm of the X chromosome between positions 21.2 and 21.1
Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin-associated protein complex (DAPC). Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere.
The DMD gene, encoding the dystrophin protein, is one of the longest human genes known, covering 2.3 megabases (0.08% of the human genome) at locus Xp21. The primary transcript in muscle measures about 2,100 kilobases and takes 16 hours to transcribe; the mature mRNA measures 14.0 kilobases. The 79-exon muscle transcript codes for a protein of 3685 amino acid residues. Read more...
Troponin T is a part of the troponin complex expressed in skeletal and cardiac myocytes. The troponin complex is responsible for coupling the sarcomere contraction cycle to variations in intracellular calcium concentration. Especially the cardiac subtype of troponin T is useful in the laboratory diagnosis of heart attack because it is released into the blood-stream when damage to heart muscle occurs. Troponin T is part of the troponin complex where it binds to tropomyosin and helps position it on actin, and, together with the rest of the troponin complex, modulates contraction of striated muscle.
The tissue-specific subtypes are:- Slow skeletal troponin T1, TNNT1 (19q13.4, 191041)
- Cardiac troponin T2, TNNT2 (1q32, 191045)
- Fast skeletal troponin T3, TNNT3 (11p15.5, 600692)
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Selected images
Striated skeletal muscle cells in microscopic view. The myofibers are the straight vertical bands; the horizontal striations (lighter and darker bands) that are visible result from differences in composition and density along the fibrils within the cells. The cigar-like dark patches beside the myofibers are muscle-cell nuclei.
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