Chapter VI – Contraction of the Skeletal Muscle

Figure 6.1 – A–E, Organization of skeletal muscle, from the gross to the
molecular level. F–I, Cross sections at the levels indicated.

I. Introduction
 40% of total body mass is composed of skeletal muscle
 10% of total body mass is smooth and cardiac muscle
 “Lever Systems of the Body”
 Muscles operate by applying tension to their points of
insertion into bones, and the bones in turn form various types
of lever systems

II. Physiological Anatomy of the Skeletal Muscle

 Striated voluntary muscle
 Elongated, cylindrical, unbranched, w/ striations (length up to
30 cm, and 10-100 μm in diameter)
 Multinucleated, peripheral nuclei
 Developed from myoblast
 Rapid contractions (compared to cardiac muscle)
 Composed of muscle cells, connective tissue, blood vessels,
and nerves
 Muscles attached to bone
 Composed of numerous fibers ranging from 10 – 80 m in
diameter
 Except for 2% of the fibers, each fiber is usually innervated by
only one nerve ending, located near the middle of the fiber

Figure 6.2 – Microscopic organization of skeletal fiber 

A. Sarcolemma (from Greek: Sarco – flesh, lemma – sheath

/cover)
 Thin Membrane Enclosing a Skeletal Muscle Fiber
 consists of:
o true cell membrane / plasma membrane and
o an outer coat made up of a thin layer of polysaccharide material that contains
numerous thin collagen fibrils
 Within the sarcolemma is the sarcoplasm (cytoplasm) of the muscle fiber)
 At each end of the muscle fiber, this surface layer of the sarcolemma fuses with a tendon
fiber.
 The tendon fibers, in turn, collect into bundles to form the muscle tendons that then connect
the muscles to the bones.

B. Myofibrils (Myo – muscle; fibrilla – small fibers)

 Composed of Actin and Myosin Filaments (protein structures)
 Each muscle fiber contains several hundreds to several thousand myofibrils
 filaments inside a myofibril do not extend the entire length of a muscle fiber
 myosin and actin filaments partially interdigitate and thus cause the myofibrils to
have alternate light and dark bands
 The alternating dark A bands and light I bands create the striations that can be seen in
both myofibrils and in whole skeletal and cardiac muscle fibers.

Filamentous bands
Light Bands Dark Bands
Contain only actin (thin) Contain only myosin (thick)
filaments filaments
I bands A bands
Isotropic to polarized light Anisotropic to polarized light  Figure 6.4 –
Z disc passes through Arrangement of filaments
center of each I band within a sarcomere

Figure 6.5 – Components of

a Sarcomere (TEM 21,600x)
 

C. Cross bridges
 Small projections from the sides of the myosin filaments
 interacts with actin filament causing contraction

D. Z-disk
 Narrow, plate-shaped regions of dense protein material
 Ends of filaments are attached
 Passes across the myofibril and from one another, attaching and aligning the myofibrils
across the muscle fiber

E. Titin Filamentous Molecules (Greek word Titan meaning “Gigantic”)

 Titin – side-by-side relationship of actin and myosin is maintained by this filamentous protein
 Molecular weight: 3,000,000 (one of the largest proteins in the body)
 Physically described as filamentous and springy
 Acts as framework holds the myosin and actin filaments in place so that the contractile
machinery of the sarcomere will work

F. Sarcomere
 Basic unit of myofibril
 that lies between 2 successive Z discs
 When muscle is contracted, length is about 2 µm

G. Sarcoplasm
 intracellular fluid between myofibrils
 contains large quantities of potassium, magnesium and phosphate plus multiple protein
enzymes

H. H zone
 Narrow region in center of each A band that contains thick filaments but no thin filaments.

I. M Line
 Region in center of H zone that contains proteins that hold thick filaments together at center of
sarcomere

J. Mitochondria
 Lies parallel to the myofibrils
 Supplies the contracting myofibrils with large amount of energy in the form of ATO formed by
the mitochondria

K. Sarcoplasmic Reticulum
 A specialized endoplasmic reticulum of skeletal muscle
 Important in regulating calcium storage, release and reuptake and therefore muscle
contraction
III. General Mechanism of Muscle Contraction

1 An action potential travels along a motor nerve to its ending on muscle fibers

2 At each ending, the nerve secretes a small amount of the neurotransmitter acetylcholine
(ACh).

3 ACh acts on a local area of the muscle fiber membrane to open ACh-gated cation
channels through protein molecules floating in the membrane

4 A The opening of acetylcholine-gated channels allows large quantities of sodium ions to

diffuse to the interior of the muscle fiber membrane.

B This action causes a local depolarization that in turn leads to the opening of voltage-
gated sodium channels, which initiates an action potential at the membrane.

5 The action potential travels along the muscle fiber membrane in the same way that
action potentials travel along nerve fiber membranes

6 The action potential depolarizes the muscle membrane, and much of the action potential
electricity flows through the center of the muscle fiber.

Here it causes the sarcoplasmic reticulum to release large quantities of calcium ions
that have been stored within this reticulum.
7 The calcium ions (Ca++) initiate attractive forces between the actin and myosin
filaments, causing them to slide alongside each other, which is the contractile
process
8 After a fraction of a second, the calcium ions are pumped back into the sarcoplasmic
reticulum by a calcium membrane pump and remain stored in the reticulum until a new
muscle action potential comes along this removal of calcium ions from the myofibrils
causes the muscle contraction to cease.

Figure 6.6 Relaxed and Contracted states of a myofibril showing (top) sliding of the actin filaments
(pink)

A. Molecular
Mechanism of Muscle Contraction
 By sliding filament mechanism
 Mechanical forces generated by the interaction of myosin cross bridges with actin filaments cause
the actin filaments to slide inward among the myosin filaments (refer to Figure 6.6)
 Under resting conditions, these forces are inhibited
 When an action potential travels over the muscle fiber, the sarcoplasmic reticulum releases large
quantities of calcium ions which activate the forces between myosin and actin filaments then
contraction is initiated
Relaxed State ends of the actin filaments extending from 2
successive Z discs barely overlap one another

Contracted State Actin filaments have been pulled inward among the
myosin filaments, hence their ends overlap one
another to their maximum extent.

Also, the Z discs have been pulled by the actin

filaments up to the ends of the myosin filaments

B. Molecular Characteristics of the Contractile Filament

 Figure 6.7 Structure of myosin molecule

i. Myosin Filaments
 thick contractile protein filaments (16 nm in
diameter; approx. 1.6 m)
 Made up of 200 or more individual myosin
molecules
 Total length of each myosin filament is
uniform

ii. Myosin molecule

 consists of a tail and two myosin heads, which bind to myosinbinding sites on actin molecules of
thin filament during muscle contraction
 Molecular weight of about 480,000
 Composed of 6 polypeptide chains:
o 2 heavy chains (MW of 200,000 each) and
o 4 light chains (MW of 20,000 each)

iii. Myosin head

 each end of the two heavy chains is folded bilaterally into a globular peptide structure
 functions as an adenosine triphosphatase (ATPase) enzyme (cleaves ATPADP+PO43- and
use the energy derived from the ATP’s high-energy phosphate bond to energize the contraction
process)

iv. Body of the filament

 tails of the myosin molecule bundled together

v. Arm
 Part of the body of each myosin molecule hangs to the side along with the head

vi. Cross Bridges

 Protruding arms and heads together

vii. Hinges
 Flexible portion of the cross bridge
 Hinged arm: allows the heads to be either extended far outward from the body of the myosin
filament or brought close to the body
 Hinged heads: participate in the actual contraction process
 There are no cross bridge heads in the center of the myosin filament for a distance of about 0.2
micrometer because the hinged arm extend away from the center.

viii. ATP Activity of Myosin Head

 myosin head functions as an ATPase enzyme which allows the head to cleave ATP and use the
energy derived from ATP’s high-energy phosphate bond to energize the contraction process

ix. Actin Filaments

 thin contractile protein filaments (8 nm in diameter; 1-2 m in length)
 Composed of two helical strands of F-actin molecules and two strands of tropomyosin molecules
that fit in the grooves between the actin strands.
 Attached to one end of each tropomyosin molecule is a troponin complex that initiates
contraction
Figure 6.8 Portion of Actin Filament 

x. Regulatory Protein – Tropomyosin

 Component of Actin filament
 Molecular weight of 70,000 and a
length of 40 nanometers.
 Wrapped spirally around the sides
of the F-actin helix.
 In resting stage: lie on top of the active site of the actin strands, so that attraction cannot
occur between actin and myosin filaments to cause contraction
 Contraction occurs only when an appropriate signal causes a conformational change in
tropomyosin that uncovers active sites on the actin molecule and initiates contraction.
 when skeletal muscle fiber is relaxed, tropomyosin covers myosin-binding sites on actin
molecules, thereby preventing myosin from binding to actin

xi. Regulatory Protein – Troponin

 Component of Actin filament
 Troponin I- strong affinity for actin
 Troponin T- for tropomyosin
 Troponin C- for Calcium ions, believed to initiate contraction process

Moves tropomyosin
muscle contraction
Ca bind to
2+
Troponin changes away from myosin-
begins as myosin
troponin shape binding sites on
binds to actin
actin molecules

Figure 6.9 Combination of many myosin molecules to form a

myosin filament. Also shown are thousands of myosin cross-
bridges and interaction between the heads of the cross-
bridges with adjacent actin filament

*** ADP molecule

 One ADP molecule is attached to each one of the G-actin molecules
 G-actin molecules serves as the active sites in the actin filaments with which the cross bridges
of the myosin filaments interact to cause muscle contraction
 each strand of the double F-actin helix is composed of polymerized G-actin molecules.

Figure 6.10 7 Actin filament composed of two helical strands

of F-actin molecules and two strands of tropomyosin molecules that
fit in the grooves between the actin strands. Attached to one end of
each tropomyosin molecule is a troponin complex that initiates
contraction

C. Interaction of Myosin Filament, Actin Filaments, and Calcium Ions to Cause Contraction

i. Inhibition of the Actin Filament by the Troponin-Tropomyosin Complex

  A pure actin filament without the presence of the troponin-tropomyosin complex (but in the
presence of magnesium ions and ATP) binds instantly and strongly with the heads of the
myosin molecules.
 Then, if the troponin-tropomyosin complex is added to the actin filament, the binding
between myosin and actin does not take place. Therefore, it is believed that the active sites
on the normal actin filament of the relaxed muscle are inhibited or physically covered by the
troponin-tropomyosin complex.
 Consequently, the sites cannot attach to the heads of the myosin filaments to cause
contraction. Before contraction can take place, the inhibitory effect of the troponin-
tropomyosin complex must itself be inhibited.

ii. Activation of the Actin Filament by Calcium Ions

 In the presence of large amounts of Calcium ions, the inhibitory effect of the troponin-
tropomyosin on the actin filaments is itself inhibited.
 MOA – still unkown
 Possible explanation:
o When calcium ions combine with Troponin C, each molecule of which can bind
strongly with up to 4 calcium ions, the troponin complex supposedly undergoes a
conformational change that tugs on the tropomyosin molecule and moves it deeper
into the groove between the two actin strands.
o This action uncovers the active sites of the actin, thus allowing contraction to
proceed.

iii. “Walk Along Theory” of Contraction

 Interaction of the Activated Actin Filament and the Myosin Cross-Bridges
 actin filament is activated by the calcium ions
 the heads of the cross-bridges from the myosin filaments become attracted to the active
sites of the actin filament and initiate contraction.
 *Although the precise manner is still partly theoretical, one hypothesis for which
considerable evidence exists is
the walk-along (or ratchet)
theory of contraction.

Figure 6.11 – “Walk-along” mechanism 

iv. ATP
a. Energy Source for Contraction
b. When a muscle contracts,
work is performed, and energy
is required.
c. Fenn effect – Use of ATP to be catabolized/hydrolyzed to form ADP (release of Phosphate
Anion) and duration of muscular contraction is directly proportional.

1. Before contraction begins, the heads of the cross bridges bind with ATP.
2. When the troponin-tropomyosin complex binds with calcium ions, active sites of actin filament are
uncovered, and myosin heads then bind with these sites.
3. The bond between the head of the cross bridge and the active site of the actin filament causes a
conformational change in the head.

The head then tilts toward the arm of the crossbridge and providing the power stroke for pulling the
actin filament.

The energy that activates the power stroke is the energy already stored, like a “cocked” spring, by
the conformational change that occurred in the head when the ATP molecule was cleaved earlier.
4. Once the head of the cross-bridge tilts, it releases ADP and Phosphate anions that were previously
attached to the head is allowed.

At the site of release of the ADP, new molecule of ATP binds. This binding of a new ATP causes
detachment of the head from the actin
5. After the head has detached from the actin, the new molecule of ATP is cleaved to begin the next
cycle, leading to a new power stroke. That is, the energy again “cocks” the head back to its
perpendicular condition, ready to begin the new power stroke cycle
6. When the “cocked” head binds with a new active site on the actin filament, it becomes un- cocked
and once again provides a new power stroke.
This cycle repeats until the actin filaments pull the Z membrane up against the ends of the myosin filaments or
until the load on the muscle becomes too great for further pulling to occur.

v. The Amount of Actin and Myosin Filament Overlap

 Determines tension developed by the contracting muscle
 As the sarcomere shortens and actin filament begins to overlap the myosin filament, the
tension increases progressively until the sarcomere length decreases to about 2.2
micrometers.
 With further shortening, the sarcomere maintains full tension.

Figure 6.12 – Length-tension diagram for a single fully contracted

sarcomere showing the maximum strength of contraction when the
sarcomere is 2.0 to 2.2 micrometers in length. At the upper right are the
relative positions of the actin and myosin filaments at different
sarcomere lengths from point A to point D 

 Figure 6.13 – Relationship of muscle length to tension in the muscle

both before and during muscle contraction

vi. Effect of Muscle Length on Force Contraction in the whole intact muscle

 sarcomeres in different parts of the muscle do not always contract the same amount
 thus, the curve in the figure above has different dimensions from those shown for the individual
muscle fiber, but it exhibits the same general form for
the slope in the normal range of contraction
 Active Tension – increase in tension that occurs
during contraction, decreases as the muscle is
stretched beyond its normal length.

Figure 6.14  Relationship of load of velocity of

contraction in a skeletal muscle with a cross-sectional
area of 1 sq. cm and a length of 8cm

vii. Relation of Velocity of contraction to load

 A skeletal muscle contracts rapidly when it
contracts against no load to a state of full
contraction in about 0.1 second for the average muscle.
 When loads are applied, the velocity of contraction becomes progressively less as the load
increases.
 When the load has been increased to equal the maximum force that the muscle can exert,
the velocity of contraction becomes zero, and no contraction results, despite activation of
the muscle fiber.
 This decreasing velocity of contraction with load occurs because a load on a contracting
muscle is a reverse force that opposes the contractile force caused by muscle contraction.
 Therefore, the net force that is available to cause the velocity of shortening is
correspondingly reduced

IV. Energetics of Muscle Contraction

 1. Work defined as Force over distance
2. muscle contracts against a load is an example of work
3. SI unit is Joule with the following formula: Joule = Newton (force) x meter (displacement)
4. However, for this discussion, we would make necessary “substitutions” in terms to be used but
same principles still apply
5. W = L x D (Work = Load x Distance/Displacement)

 Sources of Muscle Contraction

Definition of Terms:
ATP (Adenosine Triphosphate)
 Used in a cascade of chemical reactions that ultimately lead to:
1. trigger the walk-along mechanism whereby the cross-bridges pull the actin filaments,
2. pumps calcium ions from the sarcoplasm into the sarcoplasmic reticulum after the contraction is over
3. pumping sodium and potassium ions through the muscle fiber membrane to maintain an appropriate
ionic environment for the propagation of muscle fiber action potentials

 ATP in a muscle fiber is approx. 4mM (4 milli-Molar; Molar = g/MW / L of solution) is sufficient to
maintain full contraction for only 1 to 2 seconds at most
 The ATP catalyzed to ADP + PO43-, which transfers energy from the ATP molecule to the contracting
machinery of the muscle fiber
 ADP is re-phosphorylated to form new ATP within another fraction of a second
 Below are sources for re-phosphorylation which is also the sources for sustained muscle
contraction
Twitch
 A single action potential causes a brief contraction followed by relaxation

Glycogen
 Glucose polysaccharide in occurring in most animal cells as opposed to starch in plants
 Storage unit for glucose

 Phosphocreatinine
a. Used to reconstitute the ATP and carries a high energy phosphate bond similar to bonds of the ATP.
b. Instantly cleaved and its released energy caused bonding of a new phosphate ion to ADP to
reconstitute the ATP.
c. However, the amount of the phosphocreatinine in the muscle fiber is small
d. capable of causing maximal muscle contraction for only 5-8 seconds

 Glycolysis
 Rapid enzymatic breakdown of glucose from the glycogen in the muscles liberates energy that is
used to convert ADP to ATP
 Inputs: 2 ATP Glucose
 Outputs: 4 ATP, Pyruvate, Lactate
 ATP generated from the reaction can be used to directly energize additional/prolong muscle
contraction and also to reform the stores of phosphocreatine

 Importance of Glycolysis
 Reaction can occur without any oxygen so muscle contraction can be sustained seconds to a minute
without oxygen (Anaerobic Respiration)
 The rate of formation of ATP is about 2.5 times as rapid as ATP formation in response to cellular
foodstuff reacting to oxygen.
 Prolonged glycolysis leads to overproduction of lactic acid (as a result of anaerobic respiration) which
in turn cause muscular discomfort and fatigue (pangangawit)

 Oxidative Metabolism (Aerobic Respiration)

 Combining oxygen with the end products of glycolysis and with various cellular foodstuffs to liberate
ATP
 More than 95 percent of all energy used by the muscles for sustained, long – term contraction is
derived from the oxidative metabolism.
V. Characteristics of Whole Muscle Contraction
Figure 6.15  Isotonic vs Isometric Contraction
A. Isometric
 When the muscle does not shorten during contraction
 The muscle contracts against a force transducer without the
decreasing the muscle length.
 Example: Planking- back and abdominal muscle

B. Isotonic
 When it does shorten but the tension on the muscle remains
constant throughout the contraction.
 The muscle shortens against a fixed load.
 The characteristics of isotonic contraction depend on the load
against which the muscle contracts, as well as the inertia.
 Example: Crunches-Abdominal Muscle, Push up, Triceps Brachii

C. Slow vs Fast Muscle Fibers

1) Muscle that reacts rapidly including the anterior tibialis are composed of fast fiber with only small
number of the slow variety.
2) Conversely, muscles such as soleus that respond slowly but with prolonged contraction are composed
mainly of slow fibers. Below is the difference between the fast and slow fibers of the muscle.

SLOW FIBERS FAST FIBERS

Type I, Red Muscle Type II, White Muscle
Smaller Larger for greater strength of contraction
Innervated by the smaller nerve fibers Extensive sarcoplasmic reticulum is present
More extensive blood vessel system and more Less extensive blood supply.
capillaries to supply extra amounts of oxygen.
Increased numbers of mitochondria to support high Fewer mitochondria. Large amount of glycolytic
levels of oxidative metabolism. enzyme is present.
Contains large amounts of myoglobin, an iron- Deficit of myoglobin
containing protein similar to hemoglobin red blood
cells. It gives a reddish appearance to the slow
fibers.
Twitch Duration: 100 ms (milliseconds) Twitch Duration: 7.5 ms

Figure 6.16  Motor Unit

VI. Mechanics of Muscle Contraction

1. Motor Unit
 A group of muscles innervated by a single nerve fiber.
 muscle fibers that react rapidly and whose control must be exact
have more nerve fibers for fewer muscle fibers.
 A motor unit = motor neuron + group of muscles (innervated).
 A single motor may branch to innervate several muscle fibers that
function together as a group.
 Although each muscle fiber is innervated by a single motor neuron,
an entire muscle may receive an input from hundreds of different
motor neurons

2. Summation
 The adding together of individual twitch contractions to increase the intensity of overall muscle
contraction
 Occurs in two ways:
o increasing the number of motor neuron units contracting simultaneously, multiple fiber
summation, and different motor units are driven asynchronously by the spinal cord as a
result the contraction alternates among the motor units one after the other;
 o increasing the frequency of contraction, frequency summation and can lead to
tetanization.

3. Tetanization
 when the frequency reaches a critical level, the successive contraction eventually become so rapid
that they fuse together and the whole muscle contraction appears to be completely smooth and
continuous due to enough calcium ions are maintained in the sarcoplasm without allowing any
relation between the action potential

 Size principle allows the gradation of muscle force during weak contraction to occur in small steps,
where the steps become progressively greater when large amounts of force are required.

 Note: The maximum strength of tetanic contraction of a muscle operating at a normal muscle length
averages between 3 and 4 Kg per cm2, or 50 psi (pounds per square inch)

 A quadriceps muscle can have up to 16 square inches of muscle belly, as much as 800 pounds of
tension may be applied to the patellar tendon. Thus, one can readily understand how it is possible
for muscles to pull their tendons out of their insertions in bones.

Figure 6.15 Frequency summation and Tetanization

4. Staircase Effect (Treppe)

i. The phenomenon of successive increase of strength in
muscle contraction to a plateau
ii. Put into other words, when a muscle begins to
contract after a “long period of rest”, its initial strength of
contraction may be as little as one-half its strength 10 to
50 muscle twitches later.
iii. Believed to be caused primarily by increasing calcium
ions in the cytosol with each successive muscle
action potential and failure of the sarcoplasm to
recapture the ions immediately

5. Skeletal Muscle Tone

 The amount of remaining tautness of the muscles even when the muscles are at rest
 Skeletal muscle tone results entirely from a low rate of nerve impulses coming from the spinal cord.
 These nerve impulses are controlled partly by signals:
o transmitted from the brain to the appropriate spinal cord anterior motoneurons
o originate in muscle spindles located in the muscle.

6. Muscle Fatigue
 It is the prolonged and strong contraction of a muscle.
 fatigue results mainly from inability of the contractile and metabolic processes of the muscle fibers
to continue supplying the same work output
 we can infer that this is the pathologic result of the accumulation of lactic acid in the muscles (the
end product of glycolysis to produce ATP)

VII. Remodeling of Muscle

1. Muscle Hypertrophy
 Muscle hypertrophy is the increase of the total mass of a muscle
 Increase in the number of actin and myosin filaments in each muscle fiber, causing enlargement of
the individual muscle fibers; this condition is called simply fiber hypertrophy
 Another type of hypertrophy occurs when muscles are stretched to greater than normal length

2. Muscle Fibers Hyperplasia

 Under rare conditions of extreme muscle force generation, the actual number of muscle fibers has
been observed to increase in addition to the fiber hypertrophy process. When it does occur, the
mechanism is linear splitting of previously enlarged fibers

3. Muscle Atrophy
 The total decrease in the mass of a muscle
 When a muscle remains unused for many weeks, the rate of degradation of the contractile proteins
is more rapid than the rate of replacement.
  The pathway that appears to account for much of the protein degradation in a muscle undergoing
atrophy is the ATP-dependent ubiquitin-proteasome pathway
 Proteasomes are large protein complexes that degrade damaged or unneeded proteins by
proteolysis, a chemical reaction that breaks peptide bonds
 Ubiquitin is a regulatory protein that basically labels which cells will be targeted for proteosomal
degradation

4. Muscle Denervation
 When a muscle loses its nerve supply, it no longer receives the contractile signals that are required
to maintain normal muscle size. Therefore, atrophy begins almost immediately
 In the final stage of denervation atrophy, most of the muscle fibers are destroyed and replaced by
fibrous and fatty tissue
 The fibers that do remain are composed of a long cell membrane with a lineup of muscle cell nuclei
but with few or no contractile properties and little or no capability of regenerating myofibrils if a
nerve does regrow
 Contracture – The fibrous tissue that replaces the muscle fibers during denervation atrophy also
has a tendency to continue shortening for many months

VIII. Footnotes and Clinical Correlations

A. Muscle efficiency – percentage of energy input that is converted into work instead of heat

 The percentage of the input energy to muscle <25%, with the remainder becoming heat.
 The low efficiency is due to one-half of the energy in food is lost during the formation of ATP
 Only 40 – 45% of the energy in ATP itself can later be converted into work
 Maximum efficiency can be realized only when the muscle contracts at a moderate velocity.
 If the muscle contracts slowly/ immobile, maintenance heat are released during contraction
 If contraction is too rapid, Energy is used to overcome friction within the muscle itself, and this
too reduces the efficiency of contraction.
 Maximum efficiency is approx. 30%

B. Recovery of Muscle Contraction in Poliomyelitis (Development of Macro-motor Units)

 Remaining nerve fibers (that weren’t undamaged) branch off to form new axons that then
innervate many of the paralyzed muscle fibers.
 Macromotor units (product of this recovery process) can contain as many as five times the
normal number of muscle fibers for each motoneuron coming from the spinal cord.
 The formation of large motor units decreases the fineness of control one has over the muscles
but allows the muscles to regain varying degrees of strength.

C. Rigor Mortis
 Contracture – muscles contract and become rigid, even without action potentials hours
following death
 results from loss of all the ATP, which is required to cause separation of the cross- bridges
from the actin filaments during the relaxation process.
 muscles remain in rigor until the muscle proteins deteriorate about 15 to 25 hours later, which
presumably results from autolysis caused by enzymes released from lysosomes.
 Occur faster in elevated temperatures

D. Muscular Dystrophy
 several inherited disorders that cause progressive weakness and degeneration of muscle
fibers, which are replaced by fatty tissue and collagen.
 Duchenne muscular dystrophy (DMD)
o Recessive trait
o mutation of the gene that encodes for a protein called dystrophin
o dystrophin links actins to proteins in the muscle cell membrane
IX. Assessment

1. The following statements is/are true:

I. Calcium ions are not involved in the contraction of the muscle
II. Motor Unit = Muscles + Nerve Fiber
III. Sodium ions present in the ECF directly activate the actin filament
IV. Ca++ is stored in the sarcoplasmic reticulum

A. I only C. III and IV

B. II only D. IV only

2. It is otherwise called the decrease in the mass of muscle.

A. Livor mortis
B. Rigor Mortis
C. Muscular Atrophy
D. Fatigue

3. Which of the following statements accurately describe Actin:

I. Concentrated in the “Thin” Filaments
II. Are Isotropic to Polarized Light
III. Are Anisotropic to Polarized Light
IV. Innervated by the smaller nerve fibers
A. III and IV C. I and II
B. II and III D. I and III

4. Which of the following statements accurately describe Myosin:

I. Concentrated in the “Thin” Filaments
II. One of two contractile proteins found in the myofibrils
III. Are Anisotropic to Polarized Light
IV. Twitch duration approximately last 7.5 ms

A. I and IV C. III only

B. II and III D. I and III

5. Which of the following best describes how ATP is used in the muscles:
A. ATP  ADP + PO43- + q C. ADP + PO43-  Ach
B. Ca2+ + Na+ + ATP  ADP + PO43- D. NOTA

6. The following are sources of ATP except for continued contraction except:
A. Photosynthesis C. Glycolysis
B. Phosphocreatine D. Aerobic Respiration

7. Examples of Isotonic Contraction:

A. Squats D. None of the Above
B. Stair Climbing E. A and B
C. Tug-of-War

8. Examples of Isometric Contraction except:

A. Weightlifting C. Leg Extensions
B. Wall Sit D. Planking

9. Ca2+ binds to which of the following Troponin sub-species:

A. Troponin I C. Troponin N
B. Troponin C D. Troponin T

10. Skeletal Muscles fibers are enveloped by:

A. Sarcasm
B. Sarcolemma
C. Sarcoplastic Reticulum
D. Sarcocytes
X. References:

Tortora, Gerard J. et al, “Principles of Anatomy & Physiology” 15th Ed © 2017 John Wiley & Sons, Inc
Hall, J. E & Hall, M. E. “Guyton and Hall Textbook of Medical Physiology” 14th Ed © 2021 Elsevier
Barrett, K. E. et al “Ganong’s Review of Medical Physiology” 26th Ed © 2019 by McGraw-Hill Education
Costanzo, L. S. “Board Review Series Physiology” 7th Ed © 2019 Wolters Kluwer

>>> Answers:
1. D 6. A
2. C 7. C
3. C 8. A
4. B 9. B
5. A 10. B