ANIMAL MOVEMENT
ciliates and ctenophores (see Figure 29.12B ) through
Movement is an important characteristic of
animals. Animal movement occurs in many forms in
animal tissues, ranging from barely discernible
streaming of cytoplasm to extensive movements of
powerful skeletal muscles. Most animal movement
depends on a single fundamental mechanism:
contractile proteins, which can change their form to
allow relaxation and contraction. Contractile machinery
is always composed of ultrafine fibrils arranged to
contract when powered by ATP. By far the most
important protein contractile system is the actomyosin
system, composed of two proteins, actin and myosin.
This is an almost universal biomechanical system found
from protozoa to vertebrates; it performs a long list of
diverse functional roles. Cilia and fl agella, however, are
composed of proteins other than actin and myosin, and
thus are exceptions to the rule. In this discussion we
examine the three principal kinds of animal movement:
ameboid, ciliary and flagellar, and muscular.
Ameboid Movement
Ameboid movement is a form of movement
especially characteristic of amebas and other unicellular
forms; it is also found in many wandering cells of
metazoans, such as white blood cells, embryonic
mesenchyme, and numerous other mobile cells that
move through tissue spaces.
Research with a variety of ameboid cells,
including pathogen fighting phagocytes in blood, has
produced a consensus model to explain extension and
withdrawal of pseudopodia (false feet) and ameboid
crawling. Optical studies of an ameba in movement
suggest that the outer layer of nongranular, gel-like
ectoplasm surrounds a more fl uid core of endoplasm
(see Figure 11.10, p. 222). Movement depends on actin
and other regulatory proteins. According to this
hypothesis (Stossel, 1994), as the pseudopod extends,
hydrostatic pressure forces actin subunits in the flowing
endoplasm into the pseudopod where they dissociate
from regulatory proteins and are then able to assemble
into a network to form the gel-like ectoplasm. At the
trailing edge of the gel, where the network disassembles,
freed actin interacts, in the presence of calcium ions,
with myosin to create a contractile force that pulls the
cell forward behind the extending pseudopod.
Locomotion is assisted by membrane-adhesion proteins
that attach temporarily to the substrate to provide
traction, enabling the cell to crawl steadily forward (see
Figure 11.12, p. 224).
Ciliary and Flagellar Movement
Cilia are minute, hairlike, motile processes that
extend from surfaces of cells of many animals. They are
a particularly distinctivefeature of ciliate protistans, but
except for nematodes in which motile cilia are absent
and arthropods in which they are rare, cilia are found in
all major groups of animals. Cilia perform many roles
either in moving small organisms such as unicellular
their aquatic environment or in propelling fl uids and
materials over epithelial surfaces of larger animals.
Cilia are of remarkably uniform diameter (0.2 to
0.5 _ m) wherever they are found. Electron microscopy
reveals that each cilium has at its base a basal body
(kinetosome) that is structurally similar to a centriole
(see Figure 3.14, p. 46). Each basal body gives rise to a
peripheral circle of nine double microtubules arranged
around two single microtubules in the center ( Figure
29.11 ) forming the structural support and machinery for
movement within each cilium. Each microtubule is
composed of a spiral array of protein subunits called
tubulin (see Figure 3.13B, p. 45). The microtubule
doublets around the periphery are connected to each
other and to the central pair of microtubules by a
complex system of microtubule-associated proteins
(MAPs). Also extending from each doublet is a pair of
arms composed of the protein dynein. The dynein arms,
which act as cross bridges between doublets, operate to
produce a sliding force between microtubules. During
ciliary movement, microtubules behave as sliding
filaments that move past one another much like the
sliding filaments of vertebrate skeletal muscle described
in the discussion on the sliding filament hypothesis, page
658. During ciliary flexion, dynein arms link to adjacent
microtubules, then swivel and release in repeated
cycles, causing microtubules on the concave side to
slide outward past microtubules on the convex side. This
process increases curvature of the cilium. During the
recovery stroke microtubules on the opposite side slide
outward to bring the cilium back to its starting position.
A flagellum is a whiplike structure longer than a
cilium and usually present singly or in small numbers at
one end of a cell. They are found in many single-celled
eukaryotes, in animal spermatozoa, and in sponges.
Flagella have the same basic internal structure as cilia,
although several exceptions to the 9 _ 2 arrangement
have been noted; for example, sperm tails of fl atworms
have but one central microtubule, and sperm tails of a
mayfly have no central microtubule. The main difference
between a cilium and a fl agellum is in their beating
pattern rather than in their structure. A fl agellum beats
symmetrically with snakelike undulations so that water is
propelled parallel to the long axis of the fl agellum. A
cilium, in contrast, beats asymmetrically with a fast
power stroke in one direction followed by a slow
recovery during which the cilium bends as it returns to its
original position ( Figure 29.12A ). Water is propelled
parallel to the ciliated surface ( Figure 29.12A and B ).
Muscular Movement
Contractile tissue is most highly developed in
muscle cells called fibers. Although muscle fibers
themselves can do work only by contraction and cannot
actively lengthen, they can be arranged in so many
different confi gurations and combinations that almost
any movement is possible.

Figure 29.11
A, Longitudinal and cross section of a cilium showing
the microtubules and microtubule-associated proteins (MAPs)
of the 9 _ 2 arrangement typical of both cilia and fl agella. The
central pair of microtubules end near the level of the cell
surface. The peripheral microtubules continue inward for a
short distance to compose two of each of the triplets in the
basal body (kinetosome).
B, Electron micrograph of section through several
cilia. (_133,000)
Figure 29.12
A, Flagellum beats in wavelike undulations, propelling
water parallel to the main axis of itself. Cilium propels water in
direction parallel to the cellsurface.
B, Movement of cilia in comb plates of a ctenophore.
Note how the waves of beating comb plates pass down a comb
row, opposite the direction of the power stroke of individual
cilia. The movement of one comb plate lifts the plate below it
and so triggers the next lower plate and so on.
Types of Vertebrate Muscle
Vertebrate muscle is broadly classified on the
appearance of muscle cells (fibers) when viewed with a
light microscope. Both skeletal muscle and cardiac
muscle appear transversely striped (striated), with
alternating dark and light bands ( Figure 29.13 ),
although unlike skeletal muscle, cardiac muscle is
uninucleate and with branching cells. A third type of
vertebrate muscle is smooth (or visceral) muscle, which
lacks the characteristic alternating bands of the striated
type.
Skeletal muscle is typically organized into
sturdy, compact bundles or bands ( Figure 29.13A ). It is
called skeletal muscle because it is attached to skeletal
elements and is responsible for movements of the trunk,
appendages, respiratory organs, eyes, mouthparts, and
other structures. Skeletal muscle fibers are extremely
long, cylindrical, multinucleate cells that usually reach
from one end of the muscle to the other. They are
packed into bundles called fascicles (L. fasciculus,
small bundle), which are enclosed by tough connective
tissue (see Figure 29.14 ). The fascicles are in turn
grouped into a discrete muscle surrounded by a thick
connective tissue layer. Most skeletal muscles taper at
their ends, where they connect to bones by tendons.
Other muscles, such as the ventral abdominal muscles,
are flattened sheets.
Figure 29.13
Photomicrographs of types of vertebrate muscle.
A, Skeletal muscle (human) showing several striated
fi bers (cells) lying side by side. Note that nuclei are peripheral.
B, Smooth muscle (human) showing absence of
striations. Note elongate nuclei in the long fibers.
C, Cardiac muscle (monkey) is striated, similar to
skeletal muscle. Note the vertical bars, called intercalated
discs, joining separate fi bers end to end.
Figure 29.14
Organization of skeletal muscle from gross to
molecular level. A skeletal muscle (left) is composed of
thousands of multinucleated muscle fi bers (center), each
containing thousands of myofi brils (right). Each myofibril
contains numerous myosin and actin fi laments that interact to
slide past each other during contraction to shorten the muscle.
The sarcoplasmic reticulum is a network of modified
endoplasmic reticulum tubules surrounding the myofi brils and
serves as a reservoir for stored calcium that is released during
each membrane depolarization, and initiates filament sliding
during muscle contraction.
In most fi shes, amphibians, and to some extent
lizards and snakes, muscles are organized into
segments that alternate with the vertebrae. Skeletal
muscles of other vertebrates, by splitting, fusion, and
shifting, have developed into specialized muscles best
suited for manipulating jointed appendages that have
evolved for locomotion on land. Skeletal muscle
contracts powerfully
and quickly but fatigues more rapidly than does smooth
muscle. Skeletal muscle is sometimes called voluntary
muscle because it is stimulated by motor neurons (see
p. 727) under conscious control.
 those of giant barnacles and of Alaska king crabs living
Muscles can only contract or shorten and relax to along the Pacific coast of North America. Such large
their original length; they provide movement only in muscle cells lend themselves well to physiological
one direction, and are therefore often grouped as studies and are understandably popular with muscle
an antagonistic set of muscles. Antagonistic physiologists.
muscles are functional opposites that oppose
In the limited space available to treat the great
eachothers action. For example, the biceps brachii diversity of muscle structure and function in the
on one side of the upper arm is opposed in its invertebrate assemblage, we have selected for
action by the triceps brachii on the opposite side of discussion two functional extremes: the specialized
the arm. By contracting against each other, they adductor muscles of molluscs and the fast fl ight
balance and smooth rapid movements in two muscles of insects.
different directions.
Bivalve molluscan muscles contain fi bers of two
types. One kind is striated muscle that can contract
Smooth muscle lacks the striations typical of
rapidly, enabling the bivalve to snap shut its valves when
skeletal muscle ( Figure 29.13B ). The cells are much
disturbed. Scallops use these fast muscle fi bers to
smaller, tapering strands, each containing a single,
swim in their awkward manner (see Figure 16.25B, p.
central nucleus. The cells interdigitate with each other
347). The second muscle type is smooth muscle,
such that the tapered end of one cell lies close to the
capable of slow, long-lasting contractions. Using these
central nuclear region of the next. Smooth muscle cells
fibers, a bivalve can keep its valves tightly shut for hours
are organized into sheets of muscle encircling cavities
or even days. Such adductor muscles use little metabolic
and tubular structures of the body, such as the walls of
energy and receive remarkably few neural signals to
the alimentary canal, blood vessels, respiratory
maintain the activated state. The contracted state has
passages, and urinary and genital ducts. Smooth muscle
been likened to a catch mechanism involving a low rate
is typically slow acting and can maintain prolonged
of cross-bridge cycling (see p. 661) between contractile
contractions with very little energy expenditure. It is
proteins within the muscle fiber with a low energy
under the control of the autonomic nervous system (see
expenditure. However, research continues to clarify the
p. 738), hormones and local mechanisms; thus, unlike
mechanism, and similar mechanisms have been
skeletal muscle, its contractions are involuntary and
discovered in some types of vertebrate smooth muscle.
unconscious. Smooth muscle functions by sustained
contraction or relaxation. For example, smooth muscles
Insect flight muscles are virtually the functional
push material through a tube, such as the intestine, by
antithesis of the slow, holding adductor muscles of
active contractions or they change the diameter of a tube
bivalves. The wings of some small fl ies operate at
to regulate fl uid or air fl ow, such as in a blood vessel or
frequencies greater than 1000 beats per second. The
airway.
fibrillar muscle, which contracts at these frequencies
far greater than even the most active of vertebrate
Cardiac muscle, the seemingly tireless muscle
muscles shows unique characteristics. It has very
of the vertebrate heart, combines certain characteristics
limited extensibility; the wing leverage system is
of both skeletal and smooth muscle ( Figure 29.13C ). It
arranged so that the muscles shorten only slightly during
is fast acting and striated like skeletal muscle, but
each downbeat of the wings. Furthermore, muscles and
contraction is under involuntary autonomic and hormonal
wings operate as a rapidly oscillating system in an
control like smooth muscle. External control mechanisms
elastic thorax (see Figure 21.11, p. 447). Since the
serve only to modulate the intrinsic rate of contraction;
muscles recoil elastically and are activated by stretch
the heartbeat originates within specialized cardiac
during fl ight, they receive excitatory neural signals only
muscle, and the heart continues to beat even if removed
periodically rather than one signal per contraction; one
from the body (heart excitation is described on p. 694).
reinforcement signal for every 20 or 30 contractions is
Cardiac muscle is composed of closely opposed, but
enough to keep the system active. Insect fl ight muscles
separate, uninucleate cell fi bers joined to each other by
are described in more detail in Chapter 21 (pp. 446
junctional complexes (see Chapter 3, p. 46) within
447).
vertical bars called intercalated discs.
Structure of Striated Muscle
Types of Invertebrate Muscle
As mentioned on page 655, striated muscle is so
Smooth and striated muscles are also
named because of periodic bands, plainly visible under
characteristic of invertebrate animals, as well as another
the light microscope, that pass across the widths of
type called oblique striated muscle. There are many
muscle cells. Each cell, or fiber, is a multinucleated tube
variations of all three types and even instances in which
containing numerous myofibrils, packed together and
structural and functional features of vertebrate smooth
invested by a plasma membrane, the sarcolemma (
and striated muscle are combined. Striated muscle
Figure 29.14 ). The myofi bril contains two types of fi
appears in invertebrate groups as diverse as cnidarians
laments, composed of the protein myosin, and the
and arthropods. The thickest muscle fibers known,
protein actin. These are the contractile proteins of the
approximately 3 mm in diameter and 6 cm long, are
muscle. Actin fi laments are held together by a dense The actin filament complexes extend outward
structure called the Z line. The functional unit of the from both sides of the Z line and overlap with myosin
myofi bril, the sarcomere, extends between successive bundles toward the center of each sarcomere ( Figures
Z lines. These anatomical relationships are diagrammed 29.15B and 29.16 ).
in Figure 29.14 .
Sliding Filament Hypothesis of Muscle Contraction
Each myosin filament is composed of many
myosin molecules packed together in an elongate In the 1950s the English physiologists A. F.
bundle ( Figure 29.15 ). Each myosin molecule contains Huxley and H. E. Huxley independently proposed the
two polypeptide chains, each having a club-shaped head sliding filament hypothesis to explain striated muscle
( Figure 29.15A ). They are lined up in two bundles to contraction. According to this hypothesis, the actin and
form a myosin filament. The two myosin bundles are myosin fi laments become linked together by molecular
held end to end at the center of each sarcomere so that cross bridges, which act as levers to pull the filaments
the double heads of each myosin molecule face outward past each other. During contraction, the club-shaped
from the center of the filament and point toward the Z heads on the myosin filaments form cross bridges that
lines to which the actin fi laments are attached ( Figure move rapidly back and forth, alternately attaching to and
29.15B ). The myosin heads act as binding sites for releasing from receptor sites on the actin filaments, and
high-energy ATP and during muscle contraction they drawing actin filaments past the myosin filaments in a
form molecular cross bridges that interact with the actin ratchetlike action. As contraction continues, the Z lines
filaments. are pulled closer together ( Figure 29.16 ). Thus the
sarcomere shortens. Because all sarcomere units
shorten together, the whole muscle contracts. Relaxation
Human muscle tissue develops before birth, and a is a passive process. When cross bridges between the
newborn childs complement of skeletal muscle actin and myosin filaments release, the sarcomeres are
fibers is similar to that of an adult. Although an free to lengthen. This requires some force, which is
adult male weight lifter and a young boy have a supplied by recoil of elastic fibers within the connective
tissue layers of the muscle (see p. 196) and by
similar number of muscle fibers, the weight lifter
antagonistic muscles or the force of gravity.
may be several times the boys strength because
repeated high-intensity, short-duration exercise has
induced the synthesis of additional actin and
myosin filaments. Each fiber has hypertrophied,
becoming larger and stronger. This type of exercise
favors hypertrophy of fast glycolytic fibers (see p.
661) that fatigue quickly. Endurance exercise such
as long-distance running produces a very different
response. Fast oxidative and intermediate fiber
types are stimulated (see p. 661), and develop
more mitochondria and myoglobin and become
adapted for a high rate of oxidative
phosphorylation. These changes, together with the
development of more capillaries serving the fibers,
lead to increased capacity for long-duration activity
rather than increasing the strength of contraction.

Actin fi laments are composed of a backbone of

a double strand of the protein actin, twisted into a double
helix. In addition, two actin-binding proteins, tropomyosin
and troponin, form part of the actin fi lament complex.
They are important in regulating the interaction of actin
and myosin during muscle contraction. Two thin strands
of tropomyosin lie near the grooves between the actin
strands. Each tropomyosin strand is itself a double helix
as shown in Figure 29.15C . Troponin, a complex of
three globular proteins, is located at intervals along the
actin filament. Troponin acts as a calcium-dependent
Figure 29.15
switch that controls the contraction process. Molecular structure of actin and myosin fi laments of skeletal
muscle.
 A, The myosin molecule is composed of two
polypeptides coiled together and expanded at their ends into a
globular head.
B, The myosin fi lament is composed of a bundle of
myosin molecules with the globular heads extended outward
toward the actin fi laments on both sides.
C, The actin fi lament consists of a double strand of
actin surrounded by two tropomyosin strands. A globular
protein complex, troponin, occurs in pairs at every seventh
actin unit. Troponin is a calcium-dependent switch that controls
the interaction between actin and myosin.
Control of Contraction
Muscle contracts in response to nerve
stimulation. If the nerve supply to a muscle is severed,
the muscle atrophies, or wastes away. Skeletal muscle
fi bers are innervated by motor neurons whose cell
bodies are located in the central nervous system (brain
and spinal cord) (see p. 734). Each cell body gives rise
to a motor axon that leaves the central nervous system
to travel by way of a peripheral nerve trunk to a muscle
where it branches repeatedly into many terminal
branches. Each terminal branch innervates a single
muscle fi ber. Depending on the type of muscle, a single
motor axon may innervate as few as three or four
muscle fibers (where very precise control is needed,
such as the muscles that control eye movement) or as
many as 2000 muscle fibers (where precise control is
not required, such as large leg muscles). A motor neuron
and all muscle fi bers it innervates is called a motor
unit. The motor unit is the functional unit of skeletal
muscle control. When a motor neuron fi res, the action
potential passes to all fi bers of the motor unit and each
is stimulated to contract simultaneously. Total force
exerted by a muscle depends on the number of motor
units activated. Precise control of movement is achieved
by varying the number of motor units activated at any
one time. A smooth and steady increase in muscle
tension is produced by increasing the number of motor
units brought into play; this is called motor unit
recruitment.
The Neuromuscular Junction
The place where a motor axon terminates on a
muscle fi ber is called the neuromuscular ( or
myoneural) junction ( Figure 29.17 ). At the junction is
a tiny gap, or synaptic cleft, that thinly separates a
nerve terminal and muscle fi ber. Close to the junction,
the neuron stores a chemical, acetylcholine, in minute
vesicles known as synaptic vesicles. Vesicles of
acetylcholine are released into the synaptic cleft when a
nerve signal or action potential (see Chapter 33, p. 728)
reaches a synapse. Acetylcholine is a chemical mediator
or neurotransmitter that diffuses across the synaptic
cleft and acts on the muscle fi ber membrane, or
sarcolemma, by binding to receptor sites and generating
an electrical depolarization (see p. 728). The
depolarization spreads rapidly over the muscle-fi ber
sarcolemma. Thus the synapse is a special chemical
bridge that couples together the electrical activities of
nerve and muscle fi bers. The mechanism of
transmission of an electrical signal from nerve fi ber to
muscle is very similar to signal transmission between
two nerve fi bers described on page 731 and in Figures
33.7 and 33.8 (p. 731 and p. 732).
Built into vertebrate skeletal muscle is an
elaborate conduction system that serves to carry the
depolarization from the neuromuscular junction to the
densely packed fi laments within the fi ber. Along the
surface of the sarcolemma are numerous invaginations
of the membrane that project into the muscle fi ber as a
system of tubules, called T-tubules ( Figure 29.17 ). The
membrane depolarization passes down these T-tubules
and into the muscle fi ber. The T-tubules are closely
associated with the sarcoplasmic reticulum, a system
of modifi ed endoplasmic reticulum (p. 42) that runs
parallel to the actin and myosin fi laments. The
sarcoplasmic reticulum stores calcium and its release
around the actin and myosin fi laments enables the
muscle fi ber to contract.
Excitation-Contraction Coupling

How does electrical depolarization of the

sarcolemma and T-tubules activate the contractile
machinery? In resting, unstimulated muscle, shortening
does not occur because thin tropomyosin strands
surrounding the actin fi laments lie in a position that
prevents the myosin heads from attaching to actin.
When muscle is stimulated and the action potential is
Transmitted down the T-tubules, the electrical
depolarization stimulates the sarcoplasmic reticulum
surrounding the fi brils to release calcium ions ( Figure
29.18 ). The calcium binds to the actin-binding protein,
troponin. Troponin immediately undergoes changes in
shape that causes tropomyosin to move out of its
blocking position, exposing active sites on the actin fi
laments. Myosin heads then bind to these sites, forming
cross bridges between adjacent myosin and actin
filaments. This sets in motion an attach-pull-release
cycle, or cross-bridge cycling, that occurs in a series of
steps as shown in Figure 29.18 . Release of bond
energy from ATP hydrolysis activates the myosin head,
which swings 45 degrees, at the same time releasing a
molecule of ADP. This is the power stroke
that pulls the actin fi lament a distance of about
10 nm, and it
comes to an end when phosphate is released
and another ATP
molecule binds to the myosin head, freeing it
from the active
site. Thus each cycle requires expenditure of
energy in the
form of ATP ( Figure 29.18 ).
Shortening continues as long as nerve action
potentials arrive
at the neuromuscular junction and free calcium
remains available
around the actin and myosin fi laments. The
cross-bridge
cycling can repeat again and again, 50 to 100
times per second,
pulling actin and myosin fi laments past each
other. While the
distance each sarcomere can shorten is very
small, this distance
is multiplied by the thousands of sarcomeres
lying end to end in
a muscle fi ber. Consequently, a strongly
contracting muscle may
shorten by as much as one-third its resting
length.
When stimulation stops, calcium is quickly
pumped back
into the sarcoplasmic reticulum. Troponin
resumes its original
confi guration; tropomyosin moves back into its
blocking position
on actin, and the muscle relaxes.