Module 25: Muscle Tissue

Lesson 3: Muscle Fiber Contraction and Relaxation

Sự Co và Nghỉ (Giãn) Của Sợi Cơ

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Mỗi bài học (lesson) bao gồm 4 phần chính: Thuật ngữ, Luyện Đọc, Luyện Nghe, và Bàn Luận.
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Dưới đây là danh sách những thuật ngữ Y khoa của module Muscle Tissue.
Khái quát được số lượng thuật ngữ sẽ xuất hiện trong bài đọc và nghe sẽ giúp bạn thoải mái tiêu thụ nội dung hơn. Sau khi hoàn thành nội dung đọc và nghe, bạn hãy quay lại đây và luyện tập (practice) để quen dần các thuật ngữ này. Đừng ép bản thân phải nhớ các thuật ngữ này vội vì bạn sẽ gặp và ôn lại danh sách này trong những bài học (lesson) khác của cùng một module.

Medical Terminology: Muscle Tissue

acetylcholine (ACh)
neurotransmitter that binds at a motor end-plate to trigger depolarization
actin
protein that makes up most of the thin myofilaments in a sarcomere muscle fiber
action potential
change in voltage of a cell membrane in response to a stimulus that results in transmission of an electrical signal; unique to neurons and muscle fibers
aerobic respiration
production of ATP in the presence of oxygen
angiogenesis
formation of blood capillary networks
aponeurosis
broad, tendon-like sheet of connective tissue that attaches a skeletal muscle to another skeletal muscle or to a bone
ATPase
enzyme that hydrolyzes ATP to ADP
atrophy
loss of structural proteins from muscle fibers
autorhythmicity
heart’s ability to control its own contractions
calmodulin
regulatory protein that facilitates contraction in smooth muscles
cardiac muscle
striated muscle found in the heart; joined to one another at intercalated discs and under the regulation of pacemaker cells, which contract as one unit to pump blood through the circulatory system. Cardiac muscle is under involuntary control.
concentric contraction
muscle contraction that shortens the muscle to move a load
contractility
ability to shorten (contract) forcibly
contraction phase
twitch contraction phase when tension increases
creatine phosphate
phosphagen used to store energy from ATP and transfer it to muscle
dense body
sarcoplasmic structure that attaches to the sarcolemma and shortens the muscle as thin filaments slide past thick filaments
depolarize
to reduce the voltage difference between the inside and outside of a cell’s plasma membrane (the sarcolemma for a muscle fiber), making the inside less negative than at rest
desmosome
cell structure that anchors the ends of cardiac muscle fibers to allow contraction to occur
eccentric contraction
muscle contraction that lengthens the muscle as the tension is diminished
elasticity
ability to stretch and rebound
endomysium
loose, and well-hydrated connective tissue covering each muscle fiber in a skeletal muscle
epimysium
outer layer of connective tissue around a skeletal muscle
excitability
ability to undergo neural stimulation
excitation-contraction coupling
sequence of events from motor neuron signaling to a skeletal muscle fiber to contraction of the fiber’s sarcomeres
extensibility
ability to lengthen (extend)
fascicle
bundle of muscle fibers within a skeletal muscle
fast glycolytic (FG)
muscle fiber that primarily uses anaerobic glycolysis
fast oxidative (FO)
intermediate muscle fiber that is between slow oxidative and fast glycolytic fibers
fibrosis
replacement of muscle fibers by scar tissue
glycolysis
anaerobic breakdown of glucose to ATP
graded muscle response
modification of contraction strength
hyperplasia
process in which one cell splits to produce new cells
hypertonia
abnormally high muscle tone
hypertrophy
addition of structural proteins to muscle fibers
hypotonia
abnormally low muscle tone caused by the absence of low-level contractions
intercalated disc
part of the sarcolemma that connects cardiac tissue, and contains gap junctions and desmosomes
isometric contraction
muscle contraction that occurs with no change in muscle length
isotonic contraction
muscle contraction that involves changes in muscle length
lactic acid
product of anaerobic glycolysis
latch-bridges
subset of a cross-bridge in which actin and myosin remain locked together
latent period
the time when a twitch does not produce contraction
motor end-plate
sarcolemma of muscle fiber at the neuromuscular junction, with receptors for the neurotransmitter acetylcholine
motor unit
motor neuron and the group of muscle fibers it innervates
muscle tension
force generated by the contraction of the muscle; tension generated during isotonic contractions and isometric contractions
muscle tone
low levels of muscle contraction that occur when a muscle is not producing movement
myoblast
muscle-forming stem cell
myofibril
long, cylindrical organelle that runs parallel within the muscle fiber and contains the sarcomeres
myogram
instrument used to measure twitch tension
myosin
protein that makes up most of the thick cylindrical myofilament within a sarcomere muscle fiber
myotube
fusion of many myoblast cells
neuromuscular junction (NMJ)
synapse between the axon terminal of a motor neuron and the section of the membrane of a muscle fiber with receptors for the acetylcholine released by the terminal
neurotransmitter
signaling chemical released by nerve terminals that bind to and activate receptors on target cells
oxygen debt
amount of oxygen needed to compensate for ATP produced without oxygen during muscle contraction
pacesetter cell
cell that triggers action potentials in smooth muscle
pericyte
stem cell that regenerates smooth muscle cells
perimysium
connective tissue that bundles skeletal muscle fibers into fascicles within a skeletal muscle
power stroke
action of myosin pulling actin inward (toward the M line)
pyruvic acid
product of glycolysis that can be used in aerobic respiration or converted to lactic acid
recruitment
increase in the number of motor units involved in contraction
relaxation phase
period after twitch contraction when tension decreases
sarcolemma
plasma membrane of a skeletal muscle fiber
sarcomere
longitudinally, repeating functional unit of skeletal muscle, with all of the contractile and associated proteins involved in contraction
sarcopenia
age-related muscle atrophy
sarcoplasm
cytoplasm of a muscle cell
sarcoplasmic reticulum (SR)
specialized smooth endoplasmic reticulum, which stores, releases, and retrieves Ca++
satellite cell
stem cell that helps to repair muscle cells
skeletal muscle
striated, multinucleated muscle that requires signaling from the nervous system to trigger contraction; most skeletal muscles are referred to as voluntary muscles that move bones and produce movement
slow oxidative (SO)
muscle fiber that primarily uses aerobic respiration
smooth muscle
nonstriated, mononucleated muscle in the skin that is associated with hair follicles; assists in moving materials in the walls of internal organs, blood vessels, and internal passageways
somites
blocks of paraxial mesoderm cells
stress-relaxation response
relaxation of smooth muscle tissue after being stretched
synaptic cleft
space between a nerve (axon) terminal and a motor end-plate
T-tubule
projection of the sarcolemma into the interior of the cell
tetanus
a continuous fused contraction
thick filament
the thick myosin strands and their multiple heads projecting from the center of the sarcomere toward, but not all to way to, the Z-discs
thin filament
thin strands of actin and its troponin-tropomyosin complex projecting from the Z-discs toward the center of the sarcomere
treppe
stepwise increase in contraction tension
triad
the grouping of one T-tubule and two terminal cisternae
tropomyosin
regulatory protein that covers myosin-binding sites to prevent actin from binding to myosin
troponin
regulatory protein that binds to actin, tropomyosin, and calcium
twitch
single contraction produced by one action potential
varicosity
enlargement of neurons that release neurotransmitters into synaptic clefts
visceral muscle
smooth muscle found in the walls of visceral organs
voltage-gated sodium channels
membrane proteins that open sodium channels in response to a sufficient voltage change, and initiate and transmit the action potential as Na+ enters through the channel
wave summation
addition of successive neural stimuli to produce greater contraction
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Dưới đây là các bài văn nằm ở bên trái. Ở bên phải là các bài luyện tập (practice) để đánh giá khả năng đọc hiểu của bạn. Sẽ khó khăn trong thời gian đầu nếu vốn từ vựng của bạn còn hạn chế, đặc biệt là từ vựng Y khoa. Hãy kiên nhẫn và đọc nhiều nhất có kể, lượng kiến thức tích tụ dần sẽ giúp bạn đọc thoải mái hơn.
The sequence of events that result in the contraction of an individual muscle fiber begins with a signal—the neurotransmitter, ACh—from the motor neuron innervating that fiber. The local membrane of the fiber will depolarize as positively charged sodium ions (Na+) enter, triggering an action potential that spreads to the rest of the membrane which will depolarize, including the T-tubules. This triggers the release of calcium ions (Ca++) from storage in the sarcoplasmic reticulum (SR). The Ca++ then initiates contraction, which is sustained by ATP (Figure 1). As long as Ca++ ions remain in the sarcoplasm to bind to troponin, which keeps the actin-binding sites “unshielded,” and as long as ATP is available to drive the cross-bridge cycling and the pulling of actin strands by myosin, the muscle fiber will continue to shorten to an anatomical limit.

Muscle contraction usually stops when signaling from the motor neuron ends, which repolarizes the sarcolemma and T-tubules, and closes the voltage-gated calcium channels in the SR. Ca++ ions are then pumped back into the SR, which causes the tropomyosin to reshield (or re-cover) the binding sites on the actin strands. A muscle also can stop contracting when it runs out of ATP and becomes fatigued (Figure 2).

The molecular events of muscle fiber shortening occur within the fiber’s sarcomeres (see Figure 3). The contraction of a striated muscle fiber occurs as the sarcomeres, linearly arranged within myofibrils, shorten as myosin heads pull on the actin filaments.

The region where thick and thin filaments overlap has a dense appearance, as there is little space between the filaments. This zone where thin and thick filaments overlap is very important to muscle contraction, as it is the site where filament movement starts. Thin filaments, anchored at their ends by the Z-discs, do not extend completely into the central region that only contains thick filaments, anchored at their bases at a spot called the M-line. A myofibril is composed of many sarcomeres running along its length; thus, myofibrils and muscle cells contract as the sarcomeres contract.
When signaled by a motor neuron, a skeletal muscle fiber contracts as the thin filaments are pulled and then slide past the thick filaments within the fiber’s sarcomeres. This process is known as the sliding filament model of muscle contraction (Figure 3). The sliding can only occur when myosin-binding sites on the actin filaments are exposed by a series of steps that begins with Ca++ entry into the sarcoplasm.

Tropomyosin is a protein that winds around the chains of the actin filament and covers the myosin-binding sites to prevent actin from binding to myosin. Tropomyosin binds to troponin to form a troponin-tropomyosin complex. The troponin-tropomyosin complex prevents the myosin “heads” from binding to the active sites on the actin microfilaments. Troponin also has a binding site for Ca++ ions.

To initiate muscle contraction, tropomyosin has to expose the myosin-binding site on an actin filament to allow cross-bridge formation between the actin and myosin microfilaments. The first step in the process of contraction is for Ca++ to bind to troponin so that tropomyosin can slide away from the binding sites on the actin strands. This allows the myosin heads to bind to these exposed binding sites and form cross-bridges. The thin filaments are then pulled by the myosin heads to slide past the thick filaments toward the center of the sarcomere. But each head can only pull a very short distance before it has reached its limit and must be “re-cocked” before it can pull again, a step that requires ATP.
For thin filaments to continue to slide past thick filaments during muscle contraction, myosin heads must pull the actin at the binding sites, detach, re-cock, attach to more binding sites, pull, detach, re-cock, etc. This repeated movement is known as the cross-bridge cycle. This motion of the myosin heads is similar to the oars when an individual rows a boat: The paddle of the oars (the myosin heads) pull, are lifted from the water (detach), repositioned (re-cocked) and then immersed again to pull (Figure 4). Each cycle requires energy, and the action of the myosin heads in the sarcomeres repetitively pulling on the thin filaments also requires energy, which is provided by ATP.

Cross-bridge formation occurs when the myosin head attaches to the actin while adenosine diphosphate (ADP) and inorganic phosphate (Pi) are still bound to myosin (Figure 4a,b). Pi is then released, causing myosin to form a stronger attachment to the actin, after which the myosin head moves toward the M-line, pulling the actin along with it. As actin is pulled, the filaments move approximately 10 nm toward the M-line. This movement is called the power stroke, as movement of the thin filament occurs at this step (Figure 4c). In the absence of ATP, the myosin head will not detach from actin.

One part of the myosin head attaches to the binding site on the actin, but the head has another binding site for ATP. ATP binding causes the myosin head to detach from the actin (Figure 4d). After this occurs, ATP is converted to ADP and Pi by the intrinsic ATPase activity of myosin. The energy released during ATP hydrolysis changes the angle of the myosin head into a cocked position (Figure 4e). The myosin head is now in position for further movement.

When the myosin head is cocked, myosin is in a high-energy configuration. This energy is expended as the myosin head moves through the power stroke, and at the end of the power stroke, the myosin head is in a low-energy position. After the power stroke, ADP is released; however, the formed cross-bridge is still in place, and actin and myosin are bound together. As long as ATP is available, it readily attaches to myosin, the cross-bridge cycle can recur, and muscle contraction can continue.

Note that each thick filament of roughly 300 myosin molecules has multiple myosin heads, and many cross-bridges form and break continuously during muscle contraction. Multiply this by all of the sarcomeres in one myofibril, all the myofibrils in one muscle fiber, and all of the muscle fibers in one skeletal muscle, and you can understand why so much energy (ATP) is needed to keep skeletal muscles working. In fact, it is the loss of ATP that results in the rigor mortis observed soon after someone dies. With no further ATP production possible, there is no ATP available for myosin heads to detach from the actin-binding sites, so the cross-bridges stay in place, causing the rigidity in the skeletal muscles.
ATP supplies the energy for muscle contraction to take place. In addition to its direct role in the cross-bridge cycle, ATP also provides the energy for the active-transport Ca++ pumps in the SR. Muscle contraction does not occur without sufficient amounts of ATP. The amount of ATP stored in muscle is very low, only sufficient to power a few seconds worth of contractions. As it is broken down, ATP must therefore be regenerated and replaced quickly to allow for sustained contraction. There are three mechanisms by which ATP can be regenerated in muscle cells: creatine phosphate metabolism, anaerobic glycolysis, and aerobic respiration.

Creatine phosphate is a molecule that can store energy in its phosphate bonds. In a resting muscle, excess ATP transfers its energy to creatine, producing ADP and creatine phosphate. This acts as an energy reserve that can be used to quickly create more ATP. When the muscle starts to contract and needs energy, creatine phosphate transfers its phosphate back to ADP to form ATP and creatine. This reaction is catalyzed by the enzyme creatine kinase and occurs very quickly; thus, creatine phosphate-derived ATP powers the first few seconds of muscle contraction. However, creatine phosphate can only provide approximately 15 seconds worth of energy, at which point another energy source has to be used (Figure 5).

As the ATP produced by creatine phosphate is depleted, muscles turn to glycolysis as an ATP source. Glycolysis is an anaerobic (non-oxygen-dependent) process that breaks down glucose (sugar) to produce ATP; however, glycolysis cannot generate ATP as quickly as creatine phosphate. Thus, the switch to glycolysis results in a slower rate of ATP availability to the muscle. The sugar used in glycolysis can be provided by blood glucose or by metabolizing glycogen that is stored in the muscle. The breakdown of one glucose molecule produces two ATP and two molecules of pyruvic acid, which can be used in aerobic respiration or when oxygen levels are low, converted to lactic acid (Figure 5b).

If oxygen is available, pyruvic acid is used in aerobic respiration. However, if oxygen is not available, pyruvic acid is converted to lactic acid, which may contribute to muscle fatigue. This conversion allows the recycling of the enzyme NAD+ from NADH, which is needed for glycolysis to continue. This occurs during strenuous exercise when high amounts of energy are needed but oxygen cannot be sufficiently delivered to muscle. Glycolysis itself cannot be sustained for very long (approximately 1 minute of muscle activity), but it is useful in facilitating short bursts of high-intensity output. This is because glycolysis does not utilize glucose very efficiently, producing a net gain of two ATPs per molecule of glucose, and the end product of lactic acid, which may contribute to muscle fatigue as it accumulates.

Aerobic respiration is the breakdown of glucose or other nutrients in the presence of oxygen (O2) to produce carbon dioxide, water, and ATP. Approximately 95 percent of the ATP required for resting or moderately active muscles is provided by aerobic respiration, which takes place in mitochondria. The inputs for aerobic respiration include glucose circulating in the bloodstream, pyruvic acid, and fatty acids. Aerobic respiration is much more efficient than anaerobic glycolysis, producing approximately 36 ATPs per molecule of glucose versus four from glycolysis. However, aerobic respiration cannot be sustained without a steady supply of O2 to the skeletal muscle and is much slower (Figure 5c). To compensate, muscles store a small amount of excess oxygen in proteins called myoglobin, allowing for more efficient muscle contractions and less fatigue. Aerobic training also increases the efficiency of the circulatory system so that O2 can be supplied to the muscles for longer periods of time.

Muscle fatigue occurs when a muscle can no longer contract in response to signals from the nervous system. The exact causes of muscle fatigue are not fully known, although certain factors have been correlated with the decreased muscle contraction that occurs during fatigue. ATP is needed for normal muscle contraction, and as ATP reserves are reduced, muscle function may decline. This may be more of a factor in brief, intense muscle output rather than sustained, lower intensity efforts. Lactic acid buildup may lower intracellular pH, affecting enzyme and protein activity. Imbalances in Na+ and K+ levels as a result of membrane depolarization may disrupt Ca++ flow out of the SR. Long periods of sustained exercise may damage the SR and the sarcolemma, resulting in impaired Ca++ regulation.

Intense muscle activity results in an oxygen debt, which is the amount of oxygen needed to compensate for ATP produced without oxygen during muscle contraction. Oxygen is required to restore ATP and creatine phosphate levels, convert lactic acid to pyruvic acid, and, in the liver, to convert lactic acid into glucose or glycogen. Other systems used during exercise also require oxygen, and all of these combined processes result in the increased breathing rate that occurs after exercise. Until the oxygen debt has been met, oxygen intake is elevated, even after exercise has stopped.
Relaxing skeletal muscle fibers, and ultimately, the skeletal muscle, begins with the motor neuron, which stops releasing its chemical signal, ACh, into the synapse at the NMJ. The muscle fiber will repolarize, which closes the gates in the SR where Ca++ was being released. ATP-driven pumps will move Ca++ out of the sarcoplasm back into the SR. This results in the “reshielding” of the actin-binding sites on the thin filaments. Without the ability to form cross-bridges between the thin and thick filaments, the muscle fiber loses its tension and relaxes.
The number of skeletal muscle fibers in a given muscle is genetically determined and does not change. Muscle strength is directly related to the amount of myofibrils and sarcomeres within each fiber. Factors, such as hormones and stress (and artificial anabolic steroids), acting on the muscle can increase the production of sarcomeres and myofibrils within the muscle fibers, a change called hypertrophy, which results in the increased mass and bulk in a skeletal muscle. Likewise, decreased use of a skeletal muscle results in atrophy, where the number of sarcomeres and myofibrils disappear (but not the number of muscle fibers). It is common for a limb in a cast to show atrophied muscles when the cast is removed, and certain diseases, such as polio, show atrophied muscles.

OpenStax. (2022). Anatomy and Physiology 2e. Rice University. Retrieved June 15, 2023. ISBN-13: 978-1-711494-06-7 (Hardcover) ISBN-13: 978-1-711494-05-0 (Paperback) ISBN-13: 978-1-951693-42-8 (Digital). License: Attribution 4.0 International (CC BY 4.0). Access for free at openstax.org.

A cross-bridge forms between actin and the myosin heads triggering contraction. As long as Ca++ ions remain in the sarcoplasm to bind to troponin, and as long as ATP is available, the muscle fiber will continue to shorten.

Ca++ ions are pumped back into the SR, which causes the tropomyosin to reshield the binding sites on the actin strands. A muscle may also stop contracting when it runs out of ATP and becomes fatigued.

When a sarcomere contracts, the Z lines move closer together, and the I band becomes smaller. The A band stays the same width. At full contraction, the thin and thick filaments overlap completely.

(a) The active site on actin is exposed as calcium binds to troponin. (b) The myosin head is attracted to actin, and myosin binds actin at its actin-binding site, forming the cross-bridge. (c) During the power stroke, the phosphate generated in the previous contraction cycle is released. This results in the myosin head pivoting toward the center of the sarcomere, after which the attached ADP and phosphate group are released. (d) A new molecule of ATP attaches to the myosin head, causing the cross-bridge to detach. (e) The myosin head hydrolyzes ATP to ADP and phosphate, which returns the myosin to the cocked position.

(a) Some ATP is stored in a resting muscle. As contraction starts, it is used up in seconds. More ATP is generated from creatine phosphate for about 15 seconds. (b) Each glucose molecule produces two ATP and two molecules of pyruvic acid, which can be used in aerobic respiration or converted to lactic acid. If oxygen is not available, pyruvic acid is converted to lactic acid, which may contribute to muscle fatigue. This occurs during strenuous exercise when high amounts of energy are needed but oxygen cannot be sufficiently delivered to muscle. (c) Aerobic respiration is the breakdown of glucose in the presence of oxygen (O2) to produce carbon dioxide, water, and ATP. Approximately 95 percent of the ATP required for resting or moderately active muscles is provided by aerobic respiration, which takes place in mitochondria.

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Dưới đây là video và các luyện tập (practice) của bài này. Nghe là một kĩ năng khó, đặc biệt là khi chúng ta chưa quen nội dung và chưa có nhạy cảm ngôn ngữ. Nhưng cứ đi thật chậm và đừng bỏ cuộc.
Xem video và cảm nhận nội dung bài. Bạn có thể thả trôi, cảm nhận dòng chảy ngôn ngữ và không nhất thiết phải hiểu toàn bộ bài. Bên dưới là script để bạn khái quát nội dụng và tra từ mới.
Script:
  1. A sarcomere is the smallest contractile portion of a muscle.
  2. Myofibrils are composed of thick and thin filaments.
  3. Thick filaments are composed of the protein myosin; thin filaments are composed of the protein actin.
  4. Troponin and tropomyosin are regulatory proteins.
  5. Muscle contraction is described by the sliding filament model of contraction.
  6. Acetylcholine is the neurotransmitter that binds at the neuromuscular junction to trigger depolarization, and an action potential travels along the sarcolemma to trigger calcium release from sarcoplasmic reticulum.
  7. The actin sites are exposed after calcium enters the sarcoplasm from its sarcoplasmic reticulum storage to activate the troponin-tropomyosin complex so that the tropomyosin shifts away from the sites.
  8. The cross-bridging of myosin heads docking into actin-binding sites is followed by the “power stroke”—the sliding of the thin filaments by thick filaments.
  9. The “power strokes” are powered by ATP.
  10. Ultimately, the sarcomeres, myofibrils, and muscle fibers shorten to produce movement.
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