Outline Cellular Movement and Muscles:
Movement of pigment
Cytoskeleton and Motor Proteins
- All Physio processes depend on
movement:
o Intracellular transport
o Cell shape
o Cell motility
o Animal locomotion
- All mvmt depend on same machinery
Cytoskeleton
- Protein based intracellular network
Motor Proteins
- Enzymes that use energy from ATP to
move
Cytoskeleton use for movement
- Cytoskeleton elements
o Microtubules
o Microfilaments
- 3 ways to use cytoskeleton for
movement:
o Cytoskel and motor protein carriers
o To reorganize cytoskeletal network
o Motor proteins pull on cytoskeletal
rope
Cytoskeleton and Motor Protein Diversity
- Structural and functional diversity
o Many isoforms of cytoskeletal and
motor proteins
o Various ways of organizing
cytoskeletal elements
o Alteration of cytoskeletal and
motor protein function
Microtubules
- Tubelike polymers of protein tubulin
o Multiple isoforms
- Anchored at both ends
o Microtubule organization center
(MTOC) (-) near nucleus
o Attached to integral proteins (+) in
plasma membrane
- Motor proteins transport subcellular
components along microtubules
o Motor proteins like kinesin and
dynein
Eg.
granules
**8/102**
Microtubules: Composition and Formation
- Microtubules are polymers of the protein
tubulin
o Tubulin
Dimer of tubulin and
tubulin
Forms spontaneously (no
enzyme needed)
o Polarity
2 ends are different
( - ) & (+ ) end
Microtubule Assembly
- Activation of Tubulin by GTP
- Monomer + monomer = dimer
- Dimers form single stranded
protofilament
- Protofilament form sheet
- Sheet rolls up to form a tubule
- Dimers added or removed from ends
o Asymmetrical growth
o Growth is faster at + end
- Cell regulates rates of growth and
shrinkage
13 / 102
Microtubule Growth and Shrinkage
- Factors affecting growth/shrinkage
o Concentration of tubulin
o High tubulin promotes growth
- Dynamic instability
o GTP hydrolysis on tubulin
causes disassembly
- Microtubule associated proteins (MAPs)
- Temperature
o Low temp = disassembly
- Chemicals disrupt dynamics
o Eg. Taxol and colchicines (plant
poisons)
Movement along microtubules
- Motor proteins move along microtubules
- Direction determined by polarity and
motor protein type
o Kinesin move in (+) direction
o Dynein move in (-) direction (larger
than kinesin and 5x faster)
 - Movement fueled by hydrolysis of ATP o Assembly and disassembly occur
- Rate of movement determined by ATPase simultaneously and overall length
of motor protein and regulatory proteins is constant
- Capping Proteins
19/102 o Increase length by stabilizing end
and slowing disassembly
Cilia
27/102
- Numerous wavelike motion

Flagella
Microfilament (Actin Arrangement)
- Single or in pairs whiplike movement
Arrangement of Microfilaments in the cell
C & F composed of microtubules arranged into
axoneme - Tangled networks
o Microfilaments linked by filamin
- Bundle of parallel microtubules
- 9 pairs of microtubules around central protein
- Bundles
pair
o Cross-linked by fascin protein
o 9+2
Networks and bundles of microfilaments are
Asymmetric activation of dynein causes
attached to cell membrane by dystrophin
movement
protein
Microtubules and Physiology
- Maintain cell shape
Cellular Process Physio fxn - used for movement
Cytokinesis Devt & Growth
Movement by Actin Polymerization
(mitosis)
Axon Structure Nervous system - 2 types of amoeboid movement
Vesicle Transport Hormones and cell o Filapodia are rodlike extensions of
signaling cell membrane
Pigment Adaptive coloration Neural connections
dispersion Microvilli of digestive
Flagellar Reproduction epithelia
movement o Lamellapodia are sheetlike
Ciliary Respiration, digestion extensions of c. membrane
movement Leukocytes
Macrophages
Microfilaments 34/102
- Polymers composed of actin Actin + Myosin = Motor Protein
- In eukaryotic cells
- Uses motor protein myosin Myosin
- Movement arises from:
o Actin polymerization - Actin based movements involve motor
o Sliding filaments using myosin protein myosin
o Sliding Filament Model
Microfilament Structure and Growth - Myosin is an ATPase
o Converts energy from ATP to mech.
- G- actin monomers polymerize to form F-
Energy
actin
- 17 classes of myosin
- Spontaneous growth
o Many isoforms in each class
o 6-10 times faster at + end
o All isoforms have similar structure
- Treadmilling
Head (ATPase activity)
 Tail (bind to subcellular
components)
Neck (regulation of ATPase) Muscle Cells (Myocytes)

Sliding Filament Model (40/102) - Myocytes (muscle cells)

o Contractile cells unique to animals
- Pulling rope sort of - Contractile elements within myocytes
o Actin Rope o Thick Filaments
o Myosin Arm Polymers of myosin
Myosin II hexamers

- 2 Processes:
o Chemical Reaction
Myosin binds to actin (cross o Thin Filaments
bridge) Polymers of alpha actin
o Structural Change Ends capped by
Myosin bends (power stroke) tropomodulin and CapZ to
- Cross bridge cycle stabilize
o Formation of cross bridge, power Troponin and tropomyosin on
stroke, release and extension outer surface
- ATP to release and reattach to actin
o Absence of ATP causes rigor mortis Muscle Cells
LOL
Myosin cannot release actin - 2 main types of muscle cells are based on
arrangement of actin and myosin
Actino Myosin Activity o Striated (striped appearance)
Skeletal and cardiac
2 Factors affecting mvmt Actin and myosin arranged
in parallel
- Unitary Displacement o Smooth (do not appear striped)
o Distance Myosin steps during each Actin and myosin are not
cross bridge cycle arranged in any particular
o Depends on:
way
Myosin neck length
Location of binding sites on Striated and Muscle Types (49/102)
actin IMPT!!!!!!!!!!!!!!!!
Helical structure of
actin Striated Muscle Structure
- Duty Cycle
o Cross bridge cyle time (usually 0.5) - Thick and thin filaments arranged into
o Use of multiple myosin dimmers to sarcomeres
maintain contact - Repeated in parallel in series
o Side by side across myocyte
Actin and Myosin Function Causes striated appearance
o End to end along myocyte
Cell Process Physio fxn
Vesicle Transport Hormones and Cell Sarcomeres
signaling
Microvilli Digestion - Z disk
o Border of each sarcomere
Amoeboid movement Cardiovascular physio
o Thin filaments attached to z-disk
Skeletal muscle Locomotion
contraction and extend from it towards middle
Cardiac muscle Pump blood of sarcomere
contraction - A band
o Middle region of sarcomere
Smooth muscle Blood vessels
o Occupied by thick filaments
contraction
 - I band
o On either side of Z disk
o Occupied by thin filament
52/102
Sarcomeres
- Thick filament surrounded by 6 thin
filaments
- 3D org. of thin and thick filaments is
maintained by other proteins
o Nebulin
Along length of thin filament
o Titin
Keeps thick filament
centered in sarcomere
Attaches thick filament to Z
disk
Muscle Actinomyosin Activity is Unique
- Myosin II cannot drift away from actin
- Duty Cycle of Myosin II is 0.05 (NOT 0.5)
o Head is attached for a short time
o Doesnt impede other myosins
from pulling the thin filament
- Unitary Displacement is Short
o Filament sliding with each
movement of the myosin head
Contractile Force
- Depends on overlap of thick and thin
filaments
o More overlap ; more force
o Amt. of overlap depends on
sarcomere length
Measured by distance
between z disks
- Maximal force occurs at optimal length
o Decreased force = shorter/longer
lengths
Myofibril
- In muscles, sarcomeres are arranged into
myofibrils
o Single, linear continuous stretch of
interconnected sarcomeres
o Extends length of muscle cell
o Parallel arrangement
more myofibrils in parallel =
generate more force
Contraction and Relaxation in Vertebrate
Striated Muscle
Regulation of Contraction
- Excitation Contraction Coupling (EC
coupling)
o Depolarization of sarcolemma
o Elevation of intracellular Ca 2+
o Contraction
Sliding filaments
Ca2+ Allows myosin to bind to actin
- At rest, cytoplasmic ca2+ is low
o Troponin tropomyosin cover
myosin binding sites on actin
- As cytoplasmic ca2+ increases
o Ca2+ binds to TnC (calcium
binding site on troponin)
o Troponin tropomyosin moves,
exposing myosin binding site on
actin
o Myosin binds to actin and cross
bridge cycle begins
o Cycles continue as long as Ca2+
present
o Cell relaxes when sarcolemma
repolarizes and intracellular Ca2_
returns to resting levels
Troponin and Tropomyosin
65/102
Troponin tropomyosin isoforms
- Properties of isoforms affect contraction
o fTnC has higher affinity for Ca2_
than s/cTnC
mucles with fTnC respond to
smaller increases in
cytoplasmic Ca2+
- Isoforms differ in affect of temp. and pH
Myosin and Isoforms
- Properties of isoforms affect contraction
o Isoforms of myosin II in muscle
o Isoforms can change over time
67/102 MYOSIN ISOFORMS IMPT!!!!!!!!!!!!!
Excitation of Vertebrate Striated Muscle
- Skeletal muscle and cardiac muscle differ
in excitation and EC coupling
 - Differences:
o Cause of depolarization
o Time change in membrane
potential
o Propagation of AP
o Cellular origin of Ca2+
Action Potential
- APs along sarcolemma signal contraction
o Na+ enters cell when Na+
channels open
Depolarization
o Voltage gated Ca2+ channel open
Increased Ca2+
o Na+ channels close
o K+ leave cell when K+ channels
Induction of Ca2+ Release from SR
open
Repolarization
o Reestablishment of ion gradients
by Na+/K+ ATPase and Ca2+
ATPase
Initial Cause of Depolarization
- Myogenic (beginning in muscle)
o Spontaneous
- Pacemaker cells
o Cells depolarize fastest
o Unstable resting membrane
potential
- Neurogenic (beginning in the nerve)
o Excited by neurotransmitter from
motor nerves
Skeletal muscle
o Can have multiple (tonic) or single
(twitch) innervations sites
79/102 & 80/102!!!!!!!!!!!!!!!!! IMPT
T tubules and Sarcoplasmic Reticulum
Relaxation
- Transverse Tubules (T-tubules)
o Invaginations of sarcolemma
o Enhance penetration of AP into
myocyte
o Developed in larger, faster
twitching muscles
o Less developed in cardiac muscle
- Sarcoplasmic Reticulum (SR)
o Stores Ca2+ bound to protein
sequestrin
o Terminal cisternae increase storage
- T tubules and terminal cisternae are
adjacent to one another
Ca2+ Channels and Transporters
- Channels allow Ca2+ enter cytoplasm
o Ca2+ channels in cell membrane
Dihydropyridine receptor
(DHPR)
o Ca2+ channels in SR membrane
Ryanodine receptor (RyR)
- Transporters remove Ca2+ from
cytoplasm
o Ca2+ transporters in cell
membrane
Ca2+ ATPase
Na+/Ca2+ exchanger
(NaCaX)
o Ca2+ Transporters in SR
membrane
Ca2+ ATPase (SERCA)
- AP along sarcolemma conducted down T-
Tubules
o Depolarization depends on DHPR
o Ca2+ enters cell from extracellular
fluid
In heart; increase in Ca2+
causes RyR to open; allowing
release 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
- Repolarization of Sarcolemma
- Remove Ca2+ from cytoplasm
o Ca2+ ATPase in sarcolemma and
SR
o Na+/Ca2+ exchanger (NaCaX) in
sarcolemma
o Parvalbumin
Cytosolic Ca2+ binding
protein buffers Ca2+
- Ca2+ dissociates from troponin
- Tropomyosin blocks myosin binding sites
- Myosin can no longer bind to actin
- 82/102
Summary of Striated Muscles
83/ 102!!!!!!!!!!!!!!!!
Smooth Muscle
- Slow, prolonged contractions
- Often found in wall of tubes in body
o Blood vessels, intestine, airway etc
- Differences from Skeletal Muscle:
o No sarcomeres ( no striations)
Thick and thin filaments are
scattered in cell
Attached to cell membrane
at adhesion plaques
o No T-Tubules and minimal SR
o Often connected by gap junctions
Function as a single unit
o Different mechanism of EC
coupling
Control of Smooth Muscle Contraction
- Regulated by nerves hormones and
physical conditions
o At rest the protein caldesmon is
bound to actin and blocks myosin
binding
Smooth muscle does not
have troponin
o Stimulation of cell increases
intracellular Ca2+
o 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
89/102!!!!!!!!!!!!! PWIDI
Diversity of Muscle Fibers
- Different protein isoforms affect EC
coupling
o Ion channels
o Ion pumps
o Ca2+ binding proteins
o Speed of myosin ATPase
- Variation in other properties of muscle
cells
o Myoglobin content
o Number of mitochondria
- Skeletal muscle cells can be classified as
fast, slow, white, red, oxidative, glycolytic
Changing Fiber Types:
- Developmental (from embryo to adult)
o Increased proportion of fast muscle
isoforms
- Physiological response
o Exercise
o Can change both cardiac and
skeletal muscle
- Changes due to hormonal and
nonhormonal mechanisms
o Thyroid hormones repress
expression of B-myosin II gene and
induce alpha myosin II gene
Alpha myosin II exhibits the
fastest action-myosin ATPase
rates
o For example, direct stimulation of
cell can alter gene expression
94/102!!!
Trans differentiation of Muscle Cells
- Trans differentiation
o Cells used for novel functions
o 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
o Electric Organs
Invertebrate Muscles
- Variation in Contraction Force due to
graded excitatory postsynaptic potentials
(EPSP)
o Innervations by multiple neurons
o EPSPs can summate to give
stronger contraction
 o Some nerve signals can be
inhibitory
Asynchronous insect Flight muscles
- Wing beats 250 1000Hz
o Fastest vertebrate contraction =
100Hz (toadfish)
- Asynchronous muscle contractions
o Contraction is not synchronized to
nerve stimulation
o Stretch activation
Sensitivity of myofibril to
Ca2+ changes during
contraction/ relaxation cycle
Intracellular Ca2+ remains
high
Contracted muscle is
Ca2+ insensitive
o Muscle relaxes
Stretched muscle is Ca2+
sensitive
o Muscle contracts
Mollusc (Bivalve) Catch Muscle
- Muscle that holds shell closed
- Capable of long duration contractions
with little energy consumption
o Protein twitchin may stabilize actin-
myosin cross-bridges
Cross bridges do not
continue to cycle
Phosphorylation/dephophoryl
ation of twitchin regulates its
function