1.

Structure of muscles
Smooth muscle contains spindle-shaped cells 50 to 250 μm in length by 5 to
10 μm in diameter. These cells possess a single, central nucleus. Surrounding the
nucleus and throughout most of the cytoplasm are the thick (myosin) and thin
(actin) filaments. Tiny projections that originate from the myosin filament are
believed to be cross bridges. The ratio of actin to myosin filaments (approximately
12 to 1) is twice that observed in striated muscle and thus may provide a greater
opportunity for a cross bridge to attach and generate force in smooth muscle. An
increased probability for attachment may in part account for the ability of smooth
muscle to generate, with far less myosin, comparable or greater force than striated
muscle.
Smooth muscle differs from striated muscle in its lack of any apparent
organization of the actin and myosin contractile filaments into the discrete
contractile units called sarcomeres. Research has shown that a sarcomere-like
structure may nonetheless exist in smooth muscle. Such a sarcomere-like unit
would be composed of the actin filaments that are anchored to
dense amorphous bodies in the cytoplasm as well as dense plaques on
the cell membrane. These dense areas are composed of the protein α-actinin, found
in the Z lines of striated muscle, to which actin filaments are known to be attached.
Thus, force generated by myosin cross bridges attached to actin is transmitted
through actin filaments to dense bodies and then through neighbouring contractile
units, which ultimately terminate on the cell membrane.
Relaxed smooth muscle cells possess a smooth cell membrane appearance,
but upon contraction, large membrane blebs (or eruptions) form as a result of
inwardly directed contractile forces that are applied at discrete points on the
muscle membrane. These points are presumably the dense plaques on the cell
membrane to which the actin filaments attach. As an isolated cell shortens, it does
so in a corkscrewlike manner. It has been hypothesized that, in order for a single
cell to shorten in such a unique fashion, the contractile proteins in smooth muscle
are helically oriented within the muscle cell. This helical arrangement agrees with
earlier speculation that the contractile apparatus in smooth muscle may be arranged
at slight angles relative to the long axis of the cell. Such an arrangement of
contractile proteins could contribute to the slower shortening velocity
and enhanced force-generating ability of smooth muscle.
The contractile proteins interact to generate a force that must be transmitted
to the tissue in which the individual smooth muscle cells are embedded. Smooth
muscle cells do not have the tendons present in striated muscles that allow for
transfer of muscular force to operate the skeleton. Smooth muscles, however, are
generally embedded in a dense connective tissuematrix that connects the smooth
muscle cells within the tissue into a larger functional unit.
Other organelles of the cell interior are related to energyproduction and
calcium storage. Mitochondria are located most frequently near the cell nucleus
and at the periphery of the cell. As in striated muscles, these mitochondria are
linked to ATP production. The sarcoplasmic reticulum is involved in the storage of
intracellular calcium. As in striated muscle, this intracellular membrane system
plays an important role in determining whether or not contraction occurs by
regulating the concentration of intracellular calcium.
2. The muscle proteins and role of its in contraction processes
Smooth muscle cells contract in response to neuronal or hormonal
stimulation, either of which results in an increase in intracellular calcium as
calcium enters through membrane channels or is released from intracellular storage
sites. The elevated level of calcium in the cell cytoplasm results in force
generation. The rise in the level of intracellular calcium, however, initiates
contraction through a mechanism that differs substantially from that in striated
muscle. In striated muscle, myosin cross bridges are prevented from attaching to
actin by the presence of the troponin-tropomyosin system molecules on the actin
filament (see above Striated muscle). In smooth muscle, although tropomyosin is
present, troponin is not, which means that an entirely different regulatory scheme
operates in smooth muscle. Regulation of the contractile system in smooth muscle
is linked to the myosin filament; regulation in striated muscle is linked to the actin

filament.
In order for the smooth muscle myosin cross bridge to interact cyclically
with actin, a small protein on the myosin molecule called the light chain must be
phosphorylated (receive a phosphate group). This phosphorylation is the result of a
series of interdependent biochemical reactions that are initiated by the rise in
intracellular calcium. For the cell to relax, the concentration of intracellular
calcium falls, thus inactivating these biochemical processes associated with light
chain phosphorylation. The phosphate molecule that was added in the previous
steps, however, still must be removed from the light chain so that attachment of the
cross bridge to actin is prevented. Phosphatases are enzymes in the muscle cell
that cleave the phosphate group from the myosin light chain.
3. Sliding Filament Model of Contraction
When a muscle contracts, the actin is pulled along myosin toward the center
of the sarcomere until the actin and myosin filaments are completely overlapped.
In other words, for a muscle cell to contract, the sarcomere must shorten. However,
thick and thin filaments—the components of sarcomeres—do not shorten. Instead,
they slide by one another, causing the sarcomere to shorten while the filaments
remain the same length. The sliding filament theory of muscle contraction was
developed to fit the differences observed in the named bands on the sarcomere at
different degrees of muscle contraction and relaxation. The mechanism of
contraction is the binding of myosin to actin, forming cross-bridges that generate
filament movement (Figure 1).

Figure 1. When (a) a sarcomere (b) contracts, the Z lines move closer
together and the I band gets smaller. The A band stays the same width and, at
full contraction, the thin filaments overlap.
When a sarcomere shortens, some regions shorten whereas others stay the
same length. A sarcomere is defined as the distance between two consecutive Z
discs or Z lines; when a muscle contracts, the distance between the Z discs is
reduced. The H zone—the central region of the A zone—contains only thick
filaments (myosin) and is shortened during contraction. The H zone becomes
smaller and smaller due to the increasing overlap of actin and myosin filaments,
and the muscle shortens. Thus when the muscle is fully contracted, the H zone is
no longer visible. The I band contains only thin filaments and also shortens. The A
band does not shorten—it remains the same length—but A bands of different
sarcomeres move closer together during contraction, eventually disappearing. Thin
filaments are pulled by the thick filaments toward the center of the sarcomere until
the Z discs approach the thick filaments. The zone of overlap, in which thin
filaments and thick filaments occupy the same area, increases as the thin filaments
move inward.
Note that the actin and myosin filaments themselves do not change length,
but instead slide past each other.
4. Passive Streching. 5.Active contraction.
Passive Stretching: In passive stretching, there is an external force being
provided. You are being stretched instead of actively stretching. Passive
stretching can be accomplished through partner stretches, using stretching
accessories and/or just using gravity to assist your stretch. If the stretch is reliant
on an external force, it is a passive stretch.
There is a time and place for both forms of stretching. Passive static
stretches are a great way to improve flexibility and can be used as a cool
down. Active dynamic stretches are most commonly used as a warm up and are
ideal to promote blood flow to the exercised muscle groups prior to activity.
Muscle fiber generates tension through the action of actin and myosin cross-
bridge cycling. While under tension, the muscle may lengthen, shorten, or remain
the same. Although the term contraction implies shortening, when referring to the
muscular system, it means muscle fibers generating tension with the help of motor
neurons. Several types of muscle contractions occur and they are defined by the
changes in the length of the muscle during contraction. Active Stretching: In
active stretching, there is no external force being provided. You are actively
moving one muscle group to stretch another. Active stretches can be completed
without a stretching partner or stretching accessories. If you are performing the
stretch with no external force, it is an active stretch.
Isotonic Contractions
Isotonic contractions maintain constant tension in the muscle as the muscle
changes length. This can occur only when a muscle’s maximal force of contraction
exceeds the total load on the muscle. Isotonic muscle contractions can be either
concentric (muscle shortens) or eccentric (muscle lengthens).
Concentric Contractions
A concentric contraction is a type of muscle contraction in which the
muscles shorten while generating force. This is typical of muscles that contract due
to the sliding filament mechanism, and it occurs throughout the muscle. Such
contractions also alter the angle of the joints to which the muscles are attached, as
they are stimulated to contract according to the sliding filament mechanism.
This occurs throughout the length of the muscle, generating force at the
musculo-tendinous junction; causing the muscle to shorten and the angle of the
joint to change. For instance, a concentric contraction of the biceps would cause
the arm to bend at the elbow as the hand moves from near to the leg to close to the
shoulder (a biceps curl). A concentric contraction of the triceps would change the
angle of the joint in the opposite direction, straightening the arm and moving the
hand toward the leg.
Eccentric Contractions
An eccentric contraction results in the elongation of a muscle. Such
contractions decelerate the muscle joints (acting as “brakes” to concentric
contractions) and can alter the position of the load force. These contractions can be
both voluntary and involuntary. During an eccentric contraction, the muscle
elongates while under tension due to an opposing force which is greater than the
force generated by the muscle. Rather than working to pull a joint in the direction
of the muscle contraction, the muscle acts to decelerate the joint at the end of a
movement or otherwise control the repositioning of a load.
This can occur involuntarily (when attempting to move a weight too heavy
for the muscle to lift) or voluntarily (when the muscle is “smoothing out” a
movement). Over the short-term, strength training involving both eccentric and
concentric contractions appear to increase muscular strength more than training
with concentric contractions alone.
Isometric Contractions
In contrast to isotonic contractions, isometric contractions generate force
without changing the length of the muscle . This is typical of muscles found in the
hands and forearm: the muscles do not change length, and joints are not moved, so
force for grip is sufficient. An example is when the muscles of the hand and
forearm grip an object; the joints of the hand do not move, but muscles generate
sufficient force to prevent the object from being dropped.

6. The power of the contraction.

The main factors affecting muscle power are
 the force of the contraction
 the contraction velocity
The power of a muscle contraction is represented by the Physics formulas
 P= work/time and P= force x velocity

The force developed in a muscle is greatest at zero velocity and near zero at
maximum velocity.
The power of a muscle contraction builds up to a maximum and then
declines.
Thus, for example, a javelin thrower will try to use optimum power, which
occurs at about 40% of maximal force and 30% of maximal velocity.
7. Energetics of the muscle contraction. In order for muscles to contract,
ATP must be available in the muscle fiber. ATP is available from the following
sources:
 Within the muscle fiber. ATP available within the muscle fiber can maintain
muscle contraction for several seconds.
 Creatine phosphate. Creatine phosphate, a high‐energy molecule stored in
muscle cells, transfers its high‐energy phosphate group to ADP to form
ATP. The creatine phosphate in muscle cells is able to generate enough ATP
to maintain muscle contraction for about 15 seconds.
 Glucose stored within the cell. Glucose within the cell is stored in the
carbohydrate glycogen. Through the metabolic process of glycogenolysis,
glycogen is broken down to release glucose. ATP is then generated from
glucose by cellular respiration.
 Glucose and fatty acids obtained from the bloodstream. When energy
requirements are high, glucose from glycogen stored in the liver and fatty
acids from fat stored in adipose cells and the liver are released into the
bloodstream. Glucose and fatty acids are then absorbed from the
bloodstream by muscle cells. ATP is then generated from these energy‐rich
molecules by cellular respiration.
Cellular respiration is the process by which ATP is obtained from energy‐
rich molecules. Several major metabolic pathways are involved, some of which
require the presence of oxygen. Here's a summary of the important pathways:
 In glycolysis, glucose is broken down to pyruvic acid, and two ATP
molecules are generated even though oxygen is not present. The production
of ATP without the use of oxygen is called anaerobic respiration, and,
 because no oxygen is used during the various metabolic steps of this
pathway, glycolysis is called an anaerobic process.
 During anaerobic respiration, pyruvic acid is converted to lactic acid. Lactic
acid (via liver enzymes) can be converted back to pyru‐vic acid and, with the
presence of oxygen, pyruvic acid can enter the mitochondria.
Anaerobic respiration has advantages and disadvantages:
 Advantages: Anaerobic respiration is relatively rapid, and it does not require
oxygen.
 Disadvantages: Anaerobic respiration generates only two ATPs and
produces lactic acid. Most lactic acid diffuses out of the cell and into the
bloodstream and is subsequently absorbed by the liver. Some of the lactic
acid remains in the muscle fibers, where it contributes to muscle fatigue.
During strenuous exercise, a lot of ATP needs to be produced. Since a
person is exercising faster than they are bringing in oxygen, the body tries to
make ATP using the anaerobic pathway. This results in the production of
ATP and lots of lactic acid. After exercise, the liver and muscles need to
convert the lactic acid back to pyruvic acid. In order to do that, a lot of the
oxygen the body is now taking in does the conversion instead of being used
elsewhere. This is known as “repaying the debt,” hence the term “oxygen
debt.”
 In aerobic respiration, pyruvic acid (from glycolysis) and fatty acids (from
the bloodstream) are broken down, producing H 2O and CO 2 (carbon
dioxide) and regenerating the coenzymes for glycolysis. A total of 36 ATP
molecules are produced (including the two from glycolysis). However,
oxygen is required for this pathway.
Aerobic respiration also has advantages and disadvantages:
 Advantages: Aerobic respiration generates a large amount of ATP.
 Disadvantages: Aerobic respiration is relatively slow and requires oxygen.
When the ATP generated from creatine phosphate is depleted, the immediate
requirements of contracting muscle fibers force anaerobic respiration to begin.
Anaerobic respiration can supply ATP for about 30 seconds. If muscle contraction
continues, aerobic respiration, the slower ATP‐producing pathway, begins and
produces large amounts of ATP as long as oxygen is available. Eventually, oxygen
is depleted, and aerobic respiration stops. However, ATP production by anaerobic
respiration may still support some further muscle contraction. Ultimately, the
accumulation of lactic acid from anaerobic respiration and the depletion of
resources (ATP, oxygen, and glycogen) lead to muscle fatigue, and muscle
contraction stops.
8.Troponin and tropomyozin proteins and their functions.
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. Troponin is attached to the protein tropomyosin and lies within
the groove between actin filaments in muscle tissue. In a relaxed muscle,
tropomyosin blocks the attachment site for the myosin crossbridge, thus preventing
contraction. When the muscle cell is stimulated to contract by an action
potential, calcium channels open in the sarcoplasmic membrane and release
calcium into the sarcoplasm. Some of this calcium attaches to troponin, which
causes it to change shape, exposing binding sites for myosin (active sites) on
the actin filaments. Myosin's binding to actin causes crossbridge formation, and
contraction of the muscle begins.

Troponin activation. Troponin C (red) binds Ca2+, which stabilizes the

activated state, where troponin I (yellow) is no longer bound to actin. Troponin T
(blue) anchors the complex on tropomyosin.

Troponin is found in both skeletal muscle and cardiac muscle, but the
specific versions of troponin differ between types of muscle. The main difference
is that the TnC subunit of troponin in skeletal muscle has four calcium ion-binding
sites, whereas in cardiac muscle there are only three. Views on the actual amount
of calcium that binds to troponin vary from expert to expert and source to source..
In both cardiac and skeletal muscles, muscular force production is controlled
primarily by changes in the intracellular calcium concentration. In general, when
calcium rises, the muscles contract and, when calcium falls, the muscles relax.
Troponin is a component of thin filaments (along
with actin and tropomyosin), and is the protein complex to which calcium binds to
trigger the production of muscular force. Troponin itself has three subunits, TnC,
TnI, and TnT, each playing a role in force regulation. Under resting intracellular
levels of calcium, tropomyosin covers the active sites on actin to which myosin (a
molecular motor organized in muscle thick filaments) binds in order to generate
force. When calcium becomes bound to specific sites in the N-domain of TnC, a
series of protein structural changes occurs such that tropomyosin is rolled away
from myosin-binding sites on actin, allowing myosin to attach to the thin filament
and produce force and/or shorten the sarcomere.
Troponin I has also been shown to inhibit angiogenesis in vivo and in vitro.
Individual subunits serve different functions:
 Troponin C binds to calcium ions to produce a conformational change in TnI
 Troponin T binds to tropomyosin, interlocking them to form a troponin-
tropomyosin complex
 Troponin I binds to actin in thin myofilaments to hold the troponin-
tropomyosin complex in place
Smooth muscle does not have troponin.[7]
According to B. Alberts tropomyosin is an elongated protein, which
stabilizes actin filaments by binding to seven adjacent actin subunits, thus
preventing it from interacting with other proteins . Tropomyosin has a coiled coil
structure caused by the joining of two alpha helical monomers . Tropomyosin,
along with troponin play an important role in regulation of musclecontraction . As
tropomyosin binds to actin it follows its helical structure .

[6]

This figure describes the relative position of accesory proteins and actin in a
thin filament. Troponin complex is bound to actin and tropomyosin, which lies in
the groove of the actin helix.
When a muscle is relaxed, tropomyosin is blocking the myosin binding sites
on the thin filament. During the process of contraction, Ca2+ molecules bind to the
C-subunit on Troponin which causes the molecule to change its structure, this then
pulls away from the myosin binding site and brings tropomyosin a long with it.
This then reveals the binding site and allows for the binding of myosin to the thin
filament and the beginning of contraction.
9. Electromechanical contraction in muscles When the nerve impulse from
brain and spinal cord are carried along motor neuron to muscle fibre Ca++ ions are
released in the terminal axon.
 Increases calcium ion concentration stimulates the release of
neurotransmitter (Acetylcholine) in the synaptic cleft.
  The neurotransmitter binds to the receptor on the sarcolemma and
depolarization and generate action potential across muscle fibre for muscle
contraction.
 The action potential propagates over entire muscle fibre and move to the
adjacent fibres along transverse tubules.
 The action potential in transverse tubules causes the release of calcium ion
from sarcoplasmic reticulum, which stimulate for muscle contraction.
 The sequences of muscle contraction explained by sliding filament model
are as follows

Steps of muscle contraction

1. Blocking of myosin head:
 Actin and myosin overlaps each other forming cross bridge. The cross
bridge is active only when myosin head attached like hook to the actin
 filament. When muscle is at rest, the overlapping of actin filament to the
myosin head is blocked by tropomyosin. The actin myofilament is in OFF
position.
2. Release of calcium ion:
 Nerve impulse causing depolarization and action potential in the
sarcolemma trigger the release of calcium ions.
 The calcium ion then binds with the troponin complex on the actin
myofilament causing displacement of tropomyosin from its blocking site.
 As soon as the actin binding site is exposed, myosin cross bridge with actin.
 The actin myofilament is in ON position.
3. Cross bridge formation:
 The cross bridge between actin and myosin acts as an enzyme (Myosin
ATPase), which hydrolyses ATP stored in myosin head into ADP and
inorganic phosphate and release energy.
 This released energy is used for movement of myosin head toward actin
filament. The myosin head tilts and pull actin filament along so that myosin
and actin filament slide each other. The opposite end of actin myofilament
within a sarcomere move toward each other, resulting in muscle contraction.
 After sliding the cross bridge detached and the actin and myosin filament
come back to original position.