Myofilament

Last updated
Myofilament
Myofilament.svg
Myofilament
Details
Part of Myofibril
Identifiers
Latin myofilamentum
TH H2.00.05.0.00006
FMA 67897
Anatomical terms of microanatomy

Myofilaments are the three protein filaments of myofibrils in muscle cells. The main proteins involved are myosin, actin, and titin. Myosin and actin are the contractile proteins and titin is an elastic protein. The myofilaments act together in muscle contraction, and in order of size are a thick one of mostly myosin, a thin one of mostly actin, and a very thin one of mostly titin. [1] [2]

Contents

Types of muscle tissue are striated skeletal muscle and cardiac muscle, obliquely striated muscle (found in some invertebrates), and non-striated smooth muscle. [3] 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.

Structure

Muscle fiber showing thick and thin myofilaments of a myofibril. 1002 Organization of Muscle Fiber.jpg
Muscle fiber showing thick and thin myofilaments of a myofibril.

There are three different types of myofilaments: thick, thin, and elastic filaments. [1]

Function

The protein complex composed of actin and myosin, contractile proteins, is sometimes referred to as actomyosin. In striated skeletal and cardiac muscle, the actin and myosin filaments each have a specific and constant length in the order of a few micrometers, far less than the length of the elongated muscle cell (up to several centimeters in some skeletal muscle cells). [5] The contractile nature of this protein complex is based on the structure of the thick and thin filaments. The thick filament, myosin, has a double-headed structure, with the heads positioned at opposite ends of the molecule. During muscle contraction, the heads of the myosin filaments attach to oppositely oriented thin filaments, actin, and pull them past one another. The action of myosin attachment and actin movement results in sarcomere shortening. Muscle contraction consists of the simultaneous shortening of multiple sarcomeres. [6]

Muscle fiber contraction

The axon terminal of a motor neuron releases the neurotransmitter, acetylcholine, which diffuses across the synaptic cleft and binds to the muscle fiber membrane. This depolarizes the muscle fiber membrane, and the impulse travels to the muscle's sarcoplasmic reticulum via the transverse tubules. Calcium ions are then released from the sarcoplasmic reticulum into the sarcoplasm and subsequently bind to troponin. Troponin and the associated tropomyosin undergo a conformational change after calcium binding and expose the myosin binding sites on actin, the thin filament. The filaments of actin and myosin then form linkages. After binding, myosin pulls actin filaments toward each other, or inward. Thus muscle contraction occurs, and the sarcomere shortens as this process takes place. [7]

Muscle fiber relaxation

The enzyme acetylcholinesterase breaks down acetylcholine and this ceases muscle fiber stimulation. Active transport moves calcium ions back into the sarcoplasmic reticulum of the muscle fiber. ATP causes the binding between actin and myosin filaments to break. Troponin and tropomyosin revert to their original conformation and thereby block binding sites on the actin filament. The muscle fiber relaxes and the entire sarcomere lengthens. The muscle fiber is now prepared for the next contraction. [8]

Response to exercise

The changes that occur to the myofilament in response to exercise have long been a subject of interest to exercise physiologists and the athletes who depend on their research for the most advanced training techniques. Athletes across a spectrum of sporting events are particularly interested to know what type of training protocol will result in maximal force generation from a muscle or set of muscles, so much attention has been given to changes in the myofilament under bouts of chronic and acute forms of exercise.

While the exact mechanism of myofilament alteration in response to exercise is still being studied in mammals, some interesting clues have been revealed in Thoroughbred race horses. Researchers studied the presence of mRNA in skeletal muscle of horses at three distinct times; immediately before training, immediately after training, and four hours after training. They reported statistically significant differences in mRNA for genes specific to production of actin. This study provides evidence of the mechanisms for both immediate and delayed myofilament response to exercise at the molecular level. [9]

More recently, myofilament protein changes have been studied in humans in response to resistance training. Again, researchers are not completely clear about the molecular mechanisms of change, and an alteration of fiber-type composition in the myofilament may not be the answer many athletes have long assumed. [10] This study looked at the muscle specific tension in the quadriceps femoris and vastus lateralis of forty-two young men. Researchers report a 17% increase in specific muscle tension after a period of resistance training, despite a decrease in the presence of MyHC, myosin heavy-chain. This study concludes that there is no clear relationship between fiber-type composition and in vivo muscle tension, nor was there evidence of myofilament packing in the trained muscles.

Research

Other promising areas of research that may illumine the exact molecular nature of exercise-induced protein remodeling in muscle may be the study of related proteins involved with cell architecture, such as desmin and dystrophin. These proteins are thought to provide the cellular scaffolding necessary for the actin-myosin complex to undergo contraction. Research on desmin revealed that its presence increased greatly in a test group exposed to resistance training, while there was no evidence of desmin increase with endurance training. According to this study, there was no detectable increase in dystrophin in resistance or endurance training. [11] It may be that exercise-induced myofilament alterations involve more than the contractile proteins actin & myosin.

While the research on muscle fiber remodeling is on-going, there are generally accepted facts about the myofilament from the American College of Sports Medicine.[ citation needed ] It is thought that an increase in muscle strength is due to an increase in muscle fiber size, not an increase in number of muscle fibers and myofilaments. However, there is some evidence of animal satellite cells differentiating into new muscle fibers and not merely providing a support function to muscle cells.

The weakened contractile function of skeletal muscle is also linked to the state of the myofibrils. Recent studies suggest that these conditions are associated with altered single fiber performance due to decreased expression of myofilament proteins and/or changes in myosin-actin cross-bridge interactions. Furthermore, cellular and myofilament-level adaptations are related to diminished whole muscle and whole body performance. [12]

Related Research Articles

The muscular system is an organ system consisting of skeletal, smooth, and cardiac muscle. It permits movement of the body, maintains posture, and circulates blood throughout the body. The muscular systems in vertebrates are controlled through the nervous system although some muscles can be completely autonomous. Together with the skeletal system in the human, it forms the musculoskeletal system, which is responsible for the movement of the body.

Rigor mortis, or postmortem rigidity, is the fourth stage of death. It is one of the recognizable signs of death, characterized by stiffening of the limbs of the corpse caused by chemical changes in the muscles postmortem. In humans, rigor mortis can occur as soon as four hours after death. Contrary to folklore and common belief, rigor mortis is not permanent and begins to pass within hours of onset. Typically, it lasts no longer than eight hours at "room temperature".

<span class="mw-page-title-main">Smooth muscle</span> Involuntary non-striated muscle

Smooth muscle is an involuntary non-striated muscle, so-called because it has no sarcomeres and therefore no striations. It is divided into two subgroups, single-unit and multiunit smooth muscle. Within single-unit muscle, the whole bundle or sheet of smooth muscle cells contracts as a syncytium.

<span class="mw-page-title-main">Skeletal muscle</span> One of three major skeletal system types that connect to bones

Skeletal muscles are organs of the vertebrate muscular system and typically are attached by tendons to bones of a skeleton. The muscle cells of skeletal muscles are much longer than in the other types of muscle tissue, and are often known as muscle fibers. The muscle tissue of a skeletal muscle is striated – having a striped appearance due to the arrangement of the sarcomeres.

<span class="mw-page-title-main">Myofibril</span> Contractile element of muscle

A myofibril is a basic rod-like organelle of a muscle cell. Skeletal muscles are composed of long, tubular cells known as muscle fibers, and these cells contain many chains of myofibrils. Each myofibril has a diameter of 1–2 micrometres. They are created during embryonic development in a process known as myogenesis.

<span class="mw-page-title-main">Sarcomere</span> Repeating unit of a myofibril in a muscle cell

A sarcomere is the smallest functional unit of striated muscle tissue. It is the repeating unit between two Z-lines. Skeletal muscles are composed of tubular muscle cells which are formed during embryonic 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. The costamere is a different component that connects the sarcomere to the sarcolemma.

<span class="mw-page-title-main">Cardiac muscle</span> Muscular tissue of heart in vertebrates

Cardiac muscle is one of three types of vertebrate muscle tissues, with the other two being skeletal muscle and smooth muscle. It is an involuntary, striated muscle that constitutes the main tissue of the wall of the heart. The cardiac muscle (myocardium) forms a thick middle layer between the outer layer of the heart wall and the inner layer, with blood supplied via the coronary circulation. It is composed of individual cardiac muscle cells joined by intercalated discs, and encased by collagen fibers and other substances that form the extracellular matrix.

<span class="mw-page-title-main">Muscle cell</span> Type of cell found in muscle tissue

A muscle cell is also known as a myocyte when referring to either a cardiac muscle cell (cardiomyocyte) or a smooth muscle cell, as these are both small cells. A skeletal muscle cell is long and threadlike with many nuclei and is called a muscle fiber. Muscle cells develop from embryonic precursor cells called myoblasts.

<span class="mw-page-title-main">Troponin</span> Protein complex

Troponin, or the troponin complex, is a complex of three regulatory proteins that are integral to muscle contraction in skeletal muscle and cardiac muscle, but not smooth muscle. Measurements of cardiac-specific troponins I and T are extensively used as diagnostic and prognostic indicators in the management of myocardial infarction and acute coronary syndrome. Blood troponin levels may be used as a diagnostic marker for stroke or other myocardial injury that is ongoing, although the sensitivity of this measurement is low.

<span class="mw-page-title-main">Striated muscle tissue</span> Muscle tissue with repeating functional units called sarcomeres

Striated muscle tissue is a muscle tissue that features repeating functional units called sarcomeres. The presence of sarcomeres manifests as a series of bands visible along the muscle fibers, which is responsible for the striated appearance observed in microscopic images of this tissue. There are two types of striated muscle:

<span class="mw-page-title-main">Muscle contraction</span> Activation of tension-generating sites in muscle

Muscle contraction is the activation of tension-generating sites within muscle cells. In physiology, muscle contraction does not necessarily mean muscle shortening because muscle tension can be produced without changes in muscle length, such as when holding something heavy in 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.

<span class="mw-page-title-main">Tropomyosin</span> Protein

Tropomyosin is a two-stranded alpha-helical, coiled coil protein found in many animal and fungal cells. In animals, it is an important component of the muscular system which works in conjunction with troponin to regulate muscle contraction. It is present in smooth and striated muscle tissues, which can be found in various organs and body systems, including the heart, blood vessels, respiratory system, and digestive system. In fungi, tropomyosin is found in cell walls and helps maintain the structural integrity of cells.

<span class="mw-page-title-main">Triad (anatomy)</span> Structure of muscle tissue

In the histology of skeletal muscle, a triad is the structure formed by a T tubule with a sarcoplasmic reticulum (SR) known as the terminal cisterna on either side. Each skeletal muscle fiber has many thousands of triads, visible in muscle fibers that have been sectioned longitudinally. In mammals, triads are typically located at the A-I junction; that is, the junction between the A and I bands of the sarcomere, which is the smallest unit of a muscle fiber.

<span class="mw-page-title-main">Myomesin</span>

Myomesin is a protein family found in the M-line of the sarcomere structure. Myomesin has various forms throughout the body in striated muscles with specialized functions. This includes both slow and fast muscle fibers. Myomesin are made of 13 domains including a unique N-terminal followed by two immunoglobulin-like (Ig) domains, five fibronectin type III (Fn) domains, five more Ig domains. These domains all promote binding which indicates that myomesin is regulated through binding.

<span class="mw-page-title-main">TNNT2</span> Protein-coding gene in the species Homo sapiens

Cardiac muscle troponin T (cTnT) is a protein that in humans is encoded by the TNNT2 gene. Cardiac TnT is the tropomyosin-binding subunit of the troponin complex, which is located on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration.

<span class="mw-page-title-main">TPM1</span> Protein-coding gene in the species Homo sapiens

Tropomyosin alpha-1 chain is a protein that in humans is encoded by the TPM1 gene. This gene is a member of the tropomyosin (Tm) family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells.

<span class="mw-page-title-main">Troponin C type 1</span> Protein-coding gene in the species Homo sapiens

Troponin C, also known as TN-C or TnC, is a protein that resides in the troponin complex on actin thin filaments of striated muscle and is responsible for binding calcium to activate muscle contraction. Troponin C is encoded by the TNNC1 gene in humans for both cardiac and slow skeletal muscle.

<span class="mw-page-title-main">TPM2</span> Protein-coding gene in the species Homo sapiens

β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the TPM2 gene. β-tropomyosin is striated muscle-specific coiled coil dimer that functions to stabilize actin filaments and regulate muscle contraction.

<span class="mw-page-title-main">TNNI1</span> Protein-coding gene in the species Homo sapiens

Troponin I, slow skeletal muscle is a protein that in humans is encoded by the TNNI1 gene. It is a tissue-specific subtype of troponin I, which in turn is a part of the troponin complex.

Cardiac excitation-contraction coupling (CardiacEC coupling) describes the series of events, from the production of an electrical impulse (action potential) to the contraction of muscles in the heart. This process is of vital importance as it allows for the heart to beat in a controlled manner, without the need for conscious input. EC coupling results in the sequential contraction of the heart muscles that allows blood to be pumped, first to the lungs (pulmonary circulation) and then around the rest of the body (systemic circulation) at a rate between 60 and 100 beats every minute, when the body is at rest. This rate can be altered, however, by nerves that work to either increase heart rate (sympathetic nerves) or decrease it (parasympathetic nerves), as the body's oxygen demands change. Ultimately, muscle contraction revolves around a charged atom (ion), calcium (Ca2+), which is responsible for converting the electrical energy of the action potential into mechanical energy (contraction) of the muscle. This is achieved in a region of the muscle cell, called the transverse tubule during a process known as calcium induced calcium release.

References

  1. 1 2 Saladin, Kenneth (2012). Anatomy & physiology : the unity of form and function (6th ed.). New York, NY: McGraw-Hill. pp. 245–246. ISBN   9780073378251.
  2. Kellermayer, D; Smith JE, 3rd; Granzier, H (May 2019). "Titin mutations and muscle disease". Pflügers Archiv: European Journal of Physiology. 471 (5): 673–682. doi:10.1007/s00424-019-02272-5. PMC   6481931 . PMID   30919088.
  3. Cao, T; Thongam, U; Jin, JP (15 May 2019). "Invertebrate troponin: Insights into the evolution and regulation of striated muscle contraction". Archives of Biochemistry and Biophysics. 666: 40–45. doi:10.1016/j.abb.2019.03.013. PMC   6529277 . PMID   30928296.
  4. Al-Khayat, HA; Kensler, RW; Morris, EP; Squire, JM (12 November 2010). "Three-dimensional structure of the M-region (bare zone) of vertebrate striated muscle myosin filaments by single-particle analysis". Journal of Molecular Biology. 403 (5): 763–76. doi: 10.1016/j.jmb.2010.09.025 . PMC   3314970 . PMID   20851129.
  5. Alberts, Bruce (2015). Molecular biology of the cell (Sixth ed.). New York, NY. p. 918. ISBN   9780815344643.{{cite book}}: CS1 maint: location missing publisher (link)
  6. Alberts, Bruce., et al., "Muscle Contraction." Essential Cell Biology. 3rd. New York: Garland Science, 2010. p. 599. Print.
  7. Shier, David., et al., "Muscular System", Hole's Essentials of Anatomy & Physiology. 9th. McGraw Hill, 2006. p. 175. Print.
  8. Shier, David., et al., "Muscular System", Hole's Essentials of Anatomy & Physiology. 9th. McGraw Hill, 2006. p. 175. Print.
  9. McGivney BA, Eivers SS, MacHugh DE, et al. (2009). "Transcriptional adaptations following exercise in thoroughbred horse skeletal muscle highlights molecular mechanisms that lead to muscle hypertrophy". BMC Genomics. 10: 638. doi: 10.1186/1471-2164-10-638 . PMC   2812474 . PMID   20042072.
  10. Erskine RM, Jones DA, Maffulli N, Williams AG, Stewart CE, Degens H (February 2011). "What causes in vivo muscle specific tension to increase following resistance training?". Exp. Physiol. 96 (2): 145–55. doi: 10.1113/expphysiol.2010.053975 . PMID   20889606. S2CID   20304624.
  11. Parcell AC, Woolstenhulme MT, Sawyer RD (March 2009). "Structural protein alterations to resistance and endurance cycling exercise training". J Strength Cond Res. 23 (2): 359–65. doi:10.1519/JSC.0b013e318198fd62. PMID   19209072. S2CID   29584507.
  12. Miller MS, Callahan DM, Toth MJ (2014). "Skeletal muscle myofilament adaptations to aging, disease, and disuse and their effects on whole muscle performance in older adult humans". Front Physiol. 5: 369. doi: 10.3389/fphys.2014.00369 . PMC   4176476 . PMID   25309456.