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CHAPTER

5
Cellular Movement
and Muscles

PowerPoint Lecture Slides prepared by


Stephen Gehnrich, Salisbury University

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Cytoskeleton and Motor Proteins

All physiological processes depend on movement


Intracellular transport
Changes in cell shape
Cell motility
Animal locomotion

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Cytoskeleton and Motor Proteins

All movement is due to the same cellular


machinery

Cytoskeleton
Protein-based intracellular network
Motor proteins
Enzymes that use energy from ATP to move

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Use of Cytoskeleton for Movement
Cytoskeleton elements
Microtubules
Microfilaments
Three ways to use the
cytoskeleton for
movement
Cytoskeleton road
and motor protein
carriers
To reorganize the
cytoskeletal network
Motor proteins pull on
the cytoskeletal rope

Figure 5.1
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Cytoskeleton and Motor Protein Diversity

Structural and functional diversity


Multiple isoforms of cytoskeletal and motor proteins
Various ways of organizing cytoskeletal elements
Alteration of cytoskeletal and motor protein function

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Microtubules

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Microtubules

Are tubelike polymers of the protein tubulin


Similar protein in diverse animal groups
Multiple isoforms
Are anchored at both ends
Microtubule-organization center (MTOC) () near the
nucleus
Attached to integral proteins (+) in the plasma
membrane

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Microtubules

Figure 5.2
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Function of Microtubules

Motor proteins can transport subcellular


components along microtubules
Motor proteins kinesin and dynein
For example, rapid change in skin color

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Movement of Pigment Granules

Figure 5.3
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Microtubules: Composition and Formation

Microtubules are polymers of the protein tubulin


Tubulin is a dimer of a-tubulin and b-tubulin
Tubulin forms spontaneously
For example, does not require an enzyme
Polarity
The two ends of the microtubule are different
Minus () end
Plus (+) end

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Microtubule Assembly

Activation of tubulin monomers by GTP


Monomers join to form tubulin dimer
Dimers form a single-stranded protofilament
Many protofilaments form a sheet
Sheet rolls up to form a tubule
Dimers can be added or removed from the ends of
the tubule
Asymmetrical growth
Growth is faster at + end
Cell regulates rates of growth and shrinkage

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Microtubule Assembly

Figure 5.4
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Microtubule Growth and Shrinkage

Factors affecting growth/shrinkage are


Local concentrations of tubulin
High [tubulin] promotes growth
Dynamic instability
GTP hydrolysis on b-tubulin causes disassembly
Microtubule-associated proteins (MAPs)
Temperature
Low temperature causes disassembly
Chemicals that disrupt the dynamics
For example, plant poisons such as taxol and colchicine

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Microtubule Dynamics

Figure 5.5
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Regulation by MAPs

Figure 5.6
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Pacific yew tree

Taxol

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Movement Along Microtubules

Motor proteins move along microtubules


Direction is determined by polarity and the type of
motor protein
Kinesin move in (+) direction
Dynein moves in () direction
Movement is fueled by hydrolysis of ATP
Rate of movement is determined by the ATPase
domain of motor protein and regulatory proteins
Dynein is larger than kinesin and moves five times
faster

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Vesicle Traffic in a Neuron

Figure 5.7
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Cilia and Flagella
Cilia
Numerous, wavelike motion
Flagella
Single or in pairs, whiplike movement
Composed of microtubules arranged into axoneme
Bundle of parallel microtubules
Nine pairs of microtubules around a central pair
Nine-plus-two
Asymmetric activation of dynein causes movement

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Cilia and Flagella

Figure 5.8
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Cilia and Flagella

Figure 5.8
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Microtubules and Physiology

Table 5.1
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Microfilaments

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Microfilaments

Polymers composed of the protein actin


Found in all eukaryotic cells
Often use the motor protein myosin
Movement arises from
Actin polymerization
Sliding filaments using myosin

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Microfilament Structure and Growth

G-actin monomers polymerize to form a polymer


called F-actin
Spontaneous growth
610 times faster at + end
Treadmilling
Assembly and disassembly occur simultaneously and
overall length is constant
Capping proteins
Increase length by stabilizing end and slowing
disassembly

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Microfilament Structure and Growth

Figure 5.9
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Microfilament (Actin) Arrangement

Arrangement of microfilaments in the cell


Tangled neworks
Microfilaments linked by filamin protein
Bundles
Cross-linked by fascin protein
Networks and bundles of microfilaments are
attached to cell membrane by dystrophin protein
Maintain cell shape
Can be used for movement

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Microfilament (Actin) Arrangement

Figure 5.10
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Movement by Actin Polymerization

Two types of amoeboid movement


Filapodia are rodlike extensions of cell membrane
Neural connections
Microvilli of digestive epithelia
Lamellapodia are sheetlike extensions of cell
membrane
Leukocytes
Macrophages

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Movement by Actin Polymerization
Filapodia

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Movement by Actin Polymerization
Filapodia

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Movement by Actin Polymerization
Lamellapodia

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Actin Polymerization and Fertilization

Figure 5.11
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Actin + Myosin = motor protein

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Myosin

Most actin-based movements involve the motor


protein myosin
Sliding filament model
Myosin is an ATPase
Converts energy from ATP to mechanical energy
17 classes of myosin (IXVII)
Multiple isoforms in each class
All isoforms have a similar structure
Head (ATPase activity)
Tail (can bind to subcellular components)
Neck (regulation of ATPase)

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Myosin

Figure 5.12
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Sliding Filament Model

Analogous to pulling yourself along a rope


Actin the rope
Myosin your arm
Alternating cycle of grasp, pull, and release
Your hand grasps the rope
Your muscle contracts to pull rope
Your hand releases, extends, and grabs further along
the rope

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Sliding Filament Model

Two processes
Chemical reaction
Myosin binds to actin (cross-bridge)
Structural change
Myosin bends (power stroke)
Cross-bridge cycle
Formation of cross-bridge, power stroke, release, and
extension
Need ATP to release and reattach to actin
Absence of ATP causes rigor mortis
Myosin cannot release actin

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Sliding Filament Model

Figure 5.13
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Actino-Myosin Activity

Two factors affect movement


Unitary displacement
Distance myosin steps during each cross-bridge cycle
Depends on
Myosin neck length
Location of binding sites on actin
Helical structure of actin
Duty cycle
Cross-bridge time/cross-bridge cycle time
Typically ~0.5
Use of multiple myosin dimers to maintain contact

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Myosin Activity

Figure 5.14
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Actin and Myosin Function

Table 5.2
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Muscle Structure
and Regulation of Contraction

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Muscle Cells (Myocytes)

Myocytes (muscle cells)


Contractile cell unique to animals
Contractile elements within myocytes
Thick filaments
Polymers of myosin
~300 myosin II hexamers
Thin filaments
Polymers of a-actin
Ends capped by tropomodulin and CapZ to stabilize
Proteins troponin and tropomyosin on outer surface

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Thick and Thin Filaments

Figure 5.15
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Muscle Cells

Two main types of muscle cells are based on the


arrangement of actin and myosin
Striated (striped appearance)
Skeletal and cardiac muscle
Actin and myosin arranged in parallel
Smooth (do not appear striped)
Actin and myosin are not arranged in any particular way

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Striated and Smooth Muscle

Figure 5.16
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Striated Muscle Types

Table 5.3
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Striated Muscle Cell Structure

Thick and thin filaments arranged into sarcomeres


Repeated in parallel and in series
Side-by-side across myocyte
Causes striated appearance
End-to-end along myocyte

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Sarcomeres

Structural features of sarcomeres


Z-disk
Forms border of each sarcomere
Thin filaments are attached to the Z-disk and extend from
it towards the middle of the sarcomere
A-band
Middle region of sarcomere occupied by thick filaments
I-band
Located on either side of Z-disk
Occupied by thin filament

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Sarcomeres

Figure 5.17
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Sarcomeres

Each thick filament is surrounded by six thin


filaments
Three-dimensional organization of thin and thick
filaments is maintained by other proteins
Nebulin
Along length of thin filament
Titin
Keeps thick filament centered in sarcomere
Attaches thick filament to Z-disk

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Three-Dimensional Structure of Sarcomere

Figure 5.18
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Muscle Actinomyosin Activity is Unique

Myosin II cannot drift away from actin


Structure of sarcomere
Duty cycle of myosin II is 0.05 (not 0.5)
Each head is attached for a short time
Does not impede other myosins from pulling the thin
filament
Unitary displacement is short
Small amount of filament sliding with each movement
of the myosin head

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Contractile Force

Contractile force depends on overlap of thick and


thin filaments
More overlap allows for more force
Amount of overlap depends on sarcomere length as
measured by distance between Z-disks
Maximal force occurs at optimal length
Decreased force is generated at shorter or longer
lengths

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LengthForce Relationship

Figure 5.19
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Myofibril

In muscle cells, sarcomeres are arranged into


myofibrils
Single, linear continuous stretch of interconnected
sarcomeres (i.e., in series)
Extends the length of the muscle cell
Have parallel arrangement in the cell
More myofibrils in parallel can generate more force

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Myofibrils in Muscle Cells

Figure 5.20
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Contraction and Relaxation
in Vertebrate Striated Muscle

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Regulation of Contraction

Excitation-contraction coupling (EC coupling)


Depolarization of the muscle plasma membrane
(sarcolemma)
Elevation of intracellular Ca2+
Contraction
Sliding filaments

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Ca2+ Allows Myosin to Bind to Actin

At rest, cytoplasmic [Ca2+] is low


Troponin-tropomyosin cover myosin binding sites on
actin
As cytoplasmic [Ca2+] increases
Ca2+ binds to TnC (calcium binding site on troponin)
Troponin-tropomyosin moves, exposing myosin-
binding site on actin
Myosin binds to actin and cross-bridge cycle begins
Cycles continue as long as Ca2+ is present
Cell relaxes when the sarcolemma repolarizes and
intracellular Ca2+ returns to resting levels

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Troponin and Tropomyosin

Figure 5.21
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Regulation of Contraction by Ca2+

Figure 5.22
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Ionic Events in Muscle Contraction

Figure 5.23
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TroponinTropomyosin Isoforms

Properties of isoforms affect contraction


For example, fTnC has a higher affinity for Ca2+ than
s/cTnC
Muscle cells with the fTnC isoform respond to smaller
increases in cytoplasmic [Ca2+]
Isoforms differ in the affect of temperature and pH

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Myosin Isoforms

Properties of isoforms affect contraction


Multiple isoforms of myosin II in muscle
Isoforms can change over time

Table 5.4
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Excitation and EC coupling
in Vertebrate Striated Muscle

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Excitation of Vertebrate Striated Muscle

Skeletal muscle and cardiac muscle differ in


mechanism of excitation and EC coupling
Differences include
Initial cause of depolarization
Time course of the change in membrane potential
(action potential)
Propagation of the action potential along the
sarcolemma
Cellular origins of Ca2+

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Action Potentials

APs along sarcolemma signal contraction


Na+ enters cell when Na+ channels open
Depolarization
Voltage-gated Ca2+ channel open
Increase in cytoplasmic [Ca2+]
Na+ channels close
K+ leave cell when K+ channels open
Repolarization
Reestablishment of ion gradients by Na+/K+ ATPase
and Ca2+ ATPase

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Time Course of Depolarization

Figure 5.24
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Initial Cause of Depolarization

Myogenic (beginning in the muscle)


Spontaneous
For example, vertebrate heart
Pacemaker cells
Cells that depolarize fastest
Unstable resting membrane potential
Neurogenic (beginning in the nerve)
Excited by neurotransmitters from motor nerves
For example, vertebrate skeletal muscle
Can have multiple (tonic) or single (twitch)
innervation sites

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Neurogenic Muscle

Figure 5.25
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T-Tubules and Sarcoplasmic Reticulum

Transverse tubules (T-tubules)


Invaginations of sarcolemma
Enhance penetration of action potential into myocyte
More developed in larger, faster twitching muscles
Less developed in cardiac muscle
Sarcoplasmic reticulum (SR)
Stores Ca2+ bound to protein sequestrin
Terminal cisternae increase storage
T-tubules and terminal cisternae are adjacent to one
another

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T-Tubules and SR

Figure 5.28
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Ca2+ Channels and Transporters

Channels allow Ca2+ to enter cytoplasm


Ca2+ channels in cell membrane
Dihydropyridine receptor (DHPR)
Ca2+ channels in the SR membrane
Ryanodine receptor (RyR)
Transporters remove Ca2+ from cytoplasm
Ca2+ transporters in cell membrane
Ca2+ ATPase
Na+/Ca2+ exchanger (NaCaX)
Ca2+ transporters in SR membrane
Ca2+ ATPase (SERCA)

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Ca2+ Channels and Transporters

Figure 5.27
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Induction of Ca2+ Release From SR

AP along sarcolemma conducted down T-tubules


Depolarization opens DHPR
Ca2+ enters cell from extracellular fluid
In heart, [Ca2+] causes RyR to open, allowing release of
Ca2+ from SR
Ca2+ induced Ca2+ release
In skeletal muscle, change in DHPR shape causes RyR to
open, allowing release of Ca2+ from SR
Depolarization induced Ca2+ release

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Ca2+ Induced Ca2+ Release

Figure 5.29
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Depolarization Induced Ca2+ Release

Figure 5.30
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Relaxation

Repolarization of sarcolemma
Remove Ca2+ from cytoplasm
Ca2+ ATPase in sarcolemma and SR
Na+/Ca2+ exchanger (NaCaX) in sarcolemma
Parvalbumin
Cytosolic Ca2+ binding protein buffers Ca2+
Ca2+ dissociates from troponin
Tropomyosin blocks myosin binding sites
Myosin can no longer bind to actin

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Relaxation

Figure 5.27
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Summary of Striated Muscles

Table 5.5
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Smooth Muscle

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Smooth Muscle

Slow, prolonged contractions


Often found in the wall of tubes in the body
Blood vessels, intestine, airway, etc.

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Smooth Muscle

Key differences from skeletal muscle


No sarcomeres (no striations)
Thick and thin filaments are scattered in the cell
Attached to cell membrane at adhesion plaques
No T-tubules and minimal SR
Often connected by gap junctions
Function as a single unit
Different mechanism of EC coupling

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Smooth Muscle

Figure 5.31
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Control of Smooth Muscle Contraction

Regulated by nerves, hormones, and physical


conditions (e.g., stretch)
At rest, the protein caldesmon is bound to actin and
blocks myosin binding
Smooth muscle does not have troponin
Stimulation of cell increases intracellular Ca2+
Ca2+ binds to calmodulin
Calmodulin binds caldesmon and removes it from actin
Cross-bridges form and contraction occurs
Calmodulin also causes phosphorylation of myosin
Increase in myosin ATPase activity

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Control of Smooth Muscle Contraction

Figure 5.32
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Muscle Diversity
in Vertebrates and Invertebrates

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Diversity of Muscle Fibers

Different protein isoforms affect EC coupling


Ion channels
Ion pumps
Ca2+-binding proteins
Speed of myosin ATPase
Variation in other properties of muscle cells
Myoglobin content
Number of mitochondria
Skeletal muscle cells can be classified as fast,
slow, white, red, oxidative, glycolytic

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Changing Fiber Types

Developmental (from embryo to adult)


Increased proportion of fast muscle isoforms
Physiological response
For example, exercise
Can change both cardiac and skeletal muscle

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Changing Fiber Types

Changes due to hormonal and nonhormonal


mechanisms
For example, thyroid hormones repress expression of
b-myosin II gene and induce a-myosin II gene
a-myosin II exhibits the fastest actino-myosin ATPase
rates
For example, direct stimulation of cell can alter gene
expression

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Nonhormonal Mechanisms

Figure 5.33
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Trans-Differentiation of Muscle Cells

Trans-differentiation
Cells used for novel functions
For example, heater organs of billfish eye
Specialized muscle cells
Few myofibrils (little actin and myosin)
Abundant SR and mitochondria
Futile cycle of Ca2+ in and out of the SR
High rate of ATP synthesis and consumption
Electric organs

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Heater Organ

Figure 5.34
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Invertebrate Muscles

Variation in
contraction force due
to graded excitatory
postsynaptic potentials
(EPSP)
Innervation by
multiple neurons
EPSPs can summate
to give stronger
contraction
Some nerve signals
can be inhibitory
Figure 5.35
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Asynchronous Insect Flight Muscles

Wing beats: 2501000 Hz


Fastest vertebrate contraction 100 Hz (toadfish)

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Asynchronous Insect Flight Muscles

Asynchronous muscle contractions


Contraction is not synchronized to nerve stimulation
Stretch-activation
Sensitivity of the myofibril to Ca2+ changes during
contraction/relaxation cycle
Intracellular [Ca2+] remains high
Contracted muscle is Ca2+ insensitive
Muscle relaxes
Stretched muscle is Ca2+ sensitive
Muscle contracts

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Asynchronous Insect Flight Muscles

Figure 5.36
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Mollusc (Bivalve) Catch Muscle

Muscle that holds shell closed


Capable of long duration contractions with little
energy consumption
Protein twitchin may stablilize actin-myosin cross-
bridges
Cross-bridges do not continue to cycle
Phosphorylation/dephophorylation of twitchin regulates
its function

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Mollusc (Bivalve) Catch Muscle

Figure 5.37
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