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PowerPoint® Lecture Slides prepared by Barbara Heard, Atlantic Cape Community College

C H A P T E R

© 2013 Pearson Education, Inc.

© Annie Leibovitz/Contact Press Images

9

Muscles and Muscle Tissue: Part A

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Muscle Tissue

  • Nearly half of body's mass
  • Transforms chemical energy (ATP) to directed mechanical energy  exerts force
  • Three types
  • Skeletal
  • Cardiac
  • Smooth
  • Myo, mys, and sarco - prefixes for muscle

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© 2013 Pearson Education, Inc.

Types of Muscle Tissue

  • Skeletal muscles
  • Organs attached to bones and skin
  • Elongated cells called muscle fibers
  • Striated (striped)
  • Voluntary (i.e., conscious control)
  • Contract rapidly; tire easily; powerful
  • Require nervous system stimulation

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© 2013 Pearson Education, Inc.

Types of Muscle Tissue

  • Cardiac muscle
  • Only in heart; bulk of heart walls
  • Striated
  • Can contract without nervous system stimulation
  • Involuntary

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© 2013 Pearson Education, Inc.

Types of Muscle Tissue

  • Smooth muscle
  • In walls of hollow organs, e.g., stomach, urinary bladder, and airways
  • Not striated
  • Can contract without nervous system stimulation
  • Involuntary

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© 2013 Pearson Education, Inc.

Table 9.3 Comparison of Skeletal, Cardiac, and Smooth Muscle (1 of 4)

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© 2013 Pearson Education, Inc.

Special Characteristics of Muscle Tissue

  • Excitability (responsiveness): ability to receive and respond to stimuli
  • Contractility: ability to shorten forcibly when stimulated
  • Extensibility: ability to be stretched
  • Elasticity: ability to recoil to resting length

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© 2013 Pearson Education, Inc.

Muscle Functions

  • Four important functions
  • Movement of bones or fluids (e.g., blood)
  • Maintaining posture and body position
  • Stabilizing joints
  • Heat generation (especially skeletal muscle)
  • Additional functions
  • Protects organs, forms valves, controls pupil size, causes "goosebumps"

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© 2013 Pearson Education, Inc.

Skeletal Muscle

  • Connective tissue sheaths of skeletal muscle
  • Support cells; reinforce whole muscle
  • External to internal
  • Epimysium: dense irregular connective tissue surrounding entire muscle; may blend with fascia
  • Perimysium: fibrous connective tissue surrounding fascicles (groups of muscle fibers)
  • Endomysium: fine areolar connective tissue surrounding each muscle fiber

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© 2013 Pearson Education, Inc.

Figure 9.1 Connective tissue sheaths of skeletal muscle: epimysium, perimysium, and endomysium.

Bone

Tendon

Epimysium

Epimysium

Perimysium

Endomysium

Muscle fiber

in middle of

a fascicle

Blood vessel

Perimysium

wrapping a fascicle

Endomysium

(between individual

muscle fibers)

Muscle

fiber

Perimysium

Fascicle

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© 2013 Pearson Education, Inc.

Table 9.1 Structure and Organizational Levels of Skeletal Muscle (1 of 3)

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© 2013 Pearson Education, Inc.

Table 9.1 Structure and Organizational Levels of Skeletal Muscle (2 of 3)

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© 2013 Pearson Education, Inc.

Table 9.1 Structure and Organizational Levels of Skeletal Muscle (3 of 3)

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© 2013 Pearson Education, Inc.

Microscopic Anatomy of a Skeletal Muscle Fiber

  • Long, cylindrical cell
  • 10 to 100 µm in diameter; up to 30 cm long
  • Multiple peripheral nuclei
  • Sarcolemma = plasma membrane
  • Sarcoplasm = cytoplasm
  • Glycosomes for glycogen storage, myoglobin for O2 storage
  • Modified structures: myofibrils, sarcoplasmic reticulum, and T tubules

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© 2013 Pearson Education, Inc.

Myofibrils

  • Densely packed, rodlike elements
  • ~80% of cell volume
  • Contain sarcomeres - contractile units
  • Sarcomeres contain myofilaments
  • Exhibit striations - perfectly aligned repeating series of dark A bands and light I bands

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© 2013 Pearson Education, Inc.

Figure 9.2b Microscopic anatomy of a skeletal muscle fiber.

Diagram of part of a muscle fiber showing

the myofibrils. One myofibril extends from the cut end of the fiber.

Sarcolemma

Mitochondrion

Myofibril

Nucleus

Light

I band

Dark

A band

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© 2013 Pearson Education, Inc.

Striations

  • H zone: lighter region in midsection of dark A band where filaments do not overlap
  • M line: line of protein myomesin bisects H zone
  • Z disc (line): coin-shaped sheet of proteins on midline of light I band that anchors thin filaments and connects myofibrils to one another
  • Thick filaments: run entire length of an A band
  • Thin filaments: run length of I band and partway into A band
  • Sarcomere: region between two successive Z discs

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© 2013 Pearson Education, Inc.

Sarcomere

  • Smallest contractile unit (functional unit) of muscle fiber
  • Align along myofibril like boxcars of train
  • Contains A band with ½ I band at each end
  • Composed of thick and thin myofilaments made of contractile proteins

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© 2013 Pearson Education, Inc.

Figure 9.2c Microscopic anatomy of a skeletal muscle fiber.

Small part of one

myofibril

enlarged to show

the myofilaments

responsible for the

banding pattern.

Each sarcomere

extends from one Z

disc to the next.

Thin (actin)

filament

Z disc

H zone

Z disc

Thick

(myosin)

filament

I band

A band

I band

M line

Sarcomere

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© 2013 Pearson Education, Inc.

Figure 9.2d Microscopic anatomy of a skeletal muscle fiber.

Enlargement of

one sarcomere (sectioned length-

wise). Notice the

myosin heads on

the thick filaments.

Z disc

Sarcomere

M line

Z disc

Thin

(actin)

filament

Elastic

(titin)

filaments

Thick

(myosin)

filament

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© 2013 Pearson Education, Inc.

Myofibril Banding Pattern

  • Orderly arrangement of actin and myosin myofilaments within sarcomere
  • Actin myofilaments = thin filaments
  • Extend across I band and partway in A band
  • Anchored to Z discs
  • Myosin myofilaments = thick filaments
  • Extend length of A band
  • Connected at M line

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© 2013 Pearson Education, Inc.

Ultrastructure of Thick Filament

  • Composed of protein myosin
  • Each composed of 2 heavy and four light polypeptide chains
  • Myosin tails contain 2 interwoven, heavy polypeptide chains
  • Myosin heads contain 2 smaller, light polypeptide chains that act as cross bridges during contraction
  • Binding sites for actin of thin filaments
  • Binding sites for ATP
  • ATPase enzymes

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© 2013 Pearson Education, Inc.

Ultrastructure of Thin Filament

  • Twisted double strand of fibrous protein
    F actin
  • F actin consists of G (globular) actin subunits
  • G actin bears active sites for myosin head attachment during contraction
  • Tropomyosin and troponin - regulatory proteins bound to actin

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© 2013 Pearson Education, Inc.

Longitudinal section of filaments within one

sarcomere of a myofibril

Thick filament

Thin filament

In the center of the sarcomere, the thick filaments

lack myosin heads. Myosin heads are present only

in areas of myosin-actin overlap.

Thick filament.

Thin filament

Each thick filament consists of many myosin

molecules whose heads protrude at opposite�ends of the filament.

A thin filament consists of two strands of actin

subunits twisted into a helix plus two types of

regulatory proteins (troponin and tropomyosin).

Portion of a thick filament

Portion of a thin filament

Myosin head

Tropomyosin

Troponin

Actin

Actin-binding sites

ATP-

binding

site

Heads

Tail

Flexible hinge region

Myosin molecule

Actin subunits

Actin subunits

Active sites

for myosin

attachment

Figure 9.3 Composition of thick and thin filaments.

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© 2013 Pearson Education, Inc.

Structure of Myofibril

  • Elastic filament
  • Composed of protein titin
  • Holds thick filaments in place; helps recoil after stretch; resists excessive stretching
  • Dystrophin
  • Links thin filaments to proteins of sarcolemma
  • Nebulin, myomesin, C proteins bind filaments or sarcomeres together; maintain alignment

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© 2013 Pearson Education, Inc.

Sarcoplasmic Reticulum (SR)

  • Network of smooth endoplasmic reticulum surrounding each myofibril
  • Most run longitudinally
  • Pairs of terminal cisterns form perpendicular cross channels
  • Functions in regulation of intracellular Ca2+ levels
  • Stores and releases Ca2+

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© 2013 Pearson Education, Inc.

T Tubules

  • Continuations of sarcolemma
  • Lumen continuous with extracellular space
  • Increase muscle fiber's surface area
  • Penetrate cell's interior at each A band–I band junction
  • Associate with paired terminal cisterns to form triads that encircle each sarcomere

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© 2013 Pearson Education, Inc.

Figure 9.5 Relationship of the sarcoplasmic reticulum and T tubules to myofibrils of skeletal muscle.

Part of a skeletal

muscle fiber (cell)

Myofibril

Sarcolemma

I band

A band

I band

Z disc

H zone

Z disc

M

line

Sarcolemma

Triad:

• T tubule

• Terminal

cisterns of

the SR (2)

Tubules of

the SR

Myofibrils

Mitochondria

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© 2013 Pearson Education, Inc.

Triad Relationships

  • T tubules conduct impulses deep into muscle fiber; every sarcomere
  • Integral proteins protrude into intermembrane space from T tubule and SR cistern membranes and connect with each other
  • T tubule integral proteins act as voltage sensors and change shape in response to voltage changes
  • SR integral proteins are channels that release Ca2+ from SR cisterns when voltage sensors change shape

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© 2013 Pearson Education, Inc.

Sliding Filament Model of Contraction

  • Generation of force
  • Does not necessarily cause shortening of fiber
  • Shortening occurs when tension generated by cross bridges on thin filaments exceeds forces opposing shortening

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© 2013 Pearson Education, Inc.

Sliding Filament Model of Contraction

  • In relaxed state, thin and thick filaments overlap only at ends of A band
  • Sliding filament model of contraction
  • During contraction, thin filaments slide past thick filaments  actin and myosin overlap more
  • Occurs when myosin heads bind to actin  cross bridges

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© 2013 Pearson Education, Inc.

Sliding Filament Model of Contraction

  • Myosin heads bind to actin; sliding begins
  • Cross bridges form and break several times, ratcheting thin filaments toward center of sarcomere
  • Causes shortening of muscle fiber
  • Pulls Z discs toward M line
  • I bands shorten; Z discs closer; H zones disappear; A bands move closer (length stays same)

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© 2013 Pearson Education, Inc.

Figure 9.6 Sliding filament model of contraction.

Slide 2

1

Fully relaxed sarcomere of a muscle fiber

Z

H

Z

I

I

A

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© 2013 Pearson Education, Inc.

Figure 9.6 Sliding filament model of contraction.

Slide 3

2

Fully contracted sarcomere of a muscle fiber

Z

Z

I

I

A

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© 2013 Pearson Education, Inc.

The Nerve Stimulus and Events at the Neuromuscular Junction

  • Skeletal muscles stimulated by somatic motor neurons
  • Axons of motor neurons travel from central nervous system via nerves to skeletal muscle
  • Each axon forms several branches as it enters muscle
  • Each axon ending forms neuromuscular junction with single muscle fiber
  • Usually only one per muscle fiber

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© 2013 Pearson Education, Inc.

Events of Excitation-Contraction (E-C) Coupling

  • AP propagated along sarcomere to
    T tubules
  • Voltage-sensitive proteins stimulate Ca2+ release from SR
  • Ca2+ necessary for contraction

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© 2013 Pearson Education, Inc.

Role of Calcium (Ca2+) in Contraction

  • At low intracellular Ca2+ concentration
  • Tropomyosin blocks active sites on actin
  • Myosin heads cannot attach to actin
  • Muscle fiber relaxed

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© 2013 Pearson Education, Inc.

Role of Calcium (Ca2+) in Contraction

  • At higher intracellular Ca2+ concentrations
  • Ca2+ binds to troponin
  • Troponin changes shape and moves tropomyosin away from myosin-binding sites
  • Myosin heads bind to actin, causing sarcomere shortening and muscle contraction
  • When nervous stimulation ceases, Ca2+ pumped back into SR and contraction ends

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© 2013 Pearson Education, Inc.

Cross Bridge Cycle

  • Continues as long as Ca2+ signal and adequate ATP present
  • Cross bridge formation—high-energy myosin head attaches to thin filament
  • Working (power) stroke—myosin head pivots and pulls thin filament toward M line

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© 2013 Pearson Education, Inc.

Cross Bridge Cycle

  • Cross bridge detachment—ATP attaches to myosin head and cross bridge detaches
  • "Cocking" of myosin head—energy from hydrolysis of ATP cocks myosin head into high-energy state

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© 2013 Pearson Education, Inc.

Figure 9.12 The cross bridge cycle is the series of events during which myosin heads pull thin filaments
toward the center of the sarcomere.

Slide 1

Actin

Ca2+

Thin filament

Myosin

cross bridge

Thick

filament

Myosin

ATP

hydrolysis

In the absence of ATP, myosin heads will not detach, causing rigor mortis.

*This cycle will continue as long

as ATP is available and Ca2+ is

bound to troponin.

Cross bridge formation. Energized myosin head attaches to an actin myofilament, forming

a cross bridge.

Cocking of the myosin head. As ATP is hydrolyzed to ADP and Pi, the myosin head returns to its prestroke high-energy, or “cocked,” position. *

Cross bridge detachment. After ATP attaches to myosin, the link between myosin and actin weakens, and the myosin head detaches (the cross bridge “breaks”).

The power (working) stroke. ADP and Pi are released and the myosin head pivots and bends, changing to its bent

low-energy state. As a result it pulls the actin filament toward the M line.

1

2

3

4

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© 2013 Pearson Education, Inc.

Figure 9.12 The cross bridge cycle is the series of events during which myosin heads pull thin filaments
toward the center of the sarcomere.

Slide 2

Actin

Thin filament

Myosin

cross bridge

Thick

filament

Myosin

Cross bridge formation. Energized myosin head attaches to an actin myofilament, forming a cross bridge.

1

© 2013 Pearson Education, Inc.

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© 2013 Pearson Education, Inc.

Figure 9.12 The cross bridge cycle is the series of events during which myosin heads pull thin filaments
toward the center of the sarcomere.

Slide 3

The power (working) stroke. ADP and Pi are released and the myosin head pivots and bends, changing to its bent low-energy state. As a result it pulls the actin filament toward the M line.

2

© 2013 Pearson Education, Inc.

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© 2013 Pearson Education, Inc.

Figure 9.12 The cross bridge cycle is the series of events during which myosin heads pull thin filaments
toward the center of the sarcomere.

Slide 4

Cross bridge detachment. After ATP attaches to myosin, the link between myosin and actin weakens, and the myosin head detaches (the cross bridge “breaks”).

3

© 2013 Pearson Education, Inc.

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© 2013 Pearson Education, Inc.

Figure 9.12 The cross bridge cycle is the series of events during which myosin heads pull thin filaments
toward the center of the sarcomere.

Slide 5

Cocking of the myosin head. As ATP is hydrolyzed to ADP and Pi, the myosin head returns to its prestroke high-energy, or “cocked,” position. *

4

ATP

hydrolysis

*This cycle will continue as long

as ATP is available and Ca2+ is

bound to troponin.

© 2013 Pearson Education, Inc.

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© 2013 Pearson Education, Inc.

Figure 9.12 The cross bridge cycle is the series of events during which myosin heads pull thin filaments
toward the center of the sarcomere.

Slide 6

A&P Flix™: The Cross Bridge Cycle

PLAY

Actin

Ca2+

Thin filament

Myosin

cross bridge

Thick

filament

Myosin

ATP

hydrolysis

In the absence of ATP, myosin heads will not detach, causing rigor mortis.

*This cycle will continue as long

as ATP is available and Ca2+ is

bound to troponin.

Cross bridge formation. Energized myosin head attaches to an actin myofilament, forming

a cross bridge.

Cocking of the myosin head. As ATP is hydrolyzed to ADP and Pi, the myosin head returns to its prestroke high-energy, or “cocked,” position. *

Cross bridge detachment. After ATP attaches to myosin, the link between myosin and actin weakens, and the myosin head detaches (the cross bridge “breaks”).

The power (working) stroke. ADP and Pi are released and the myosin head pivots and bends, changing to its bent

low-energy state. As a result it pulls the actin filament toward the M line.

1

2

3

4

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© 2013 Pearson Education, Inc.

Homeostatic Imbalance

  • Rigor mortis
  • Cross bridge detachment requires ATP
  • 3–4 hours after death muscles begin to stiffen with weak rigidity at 12 hours post mortem
  • Dying cells take in calcium  cross bridge formation
  • No ATP generated to break cross bridges

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