CHAPTER 5 Excitable Tissue: Muscle A transverse M LINE is seen in the middle of the H

BAND, and this line PLUS the NARROW LIGHT AREAS ON

(Ganong) ki-yan-yoh  EITHER SIDE OF IT are sometimes called the PSEUDO-H ZONE
Skeletal muscle – is made up of individual muscle fibers that
are “building blocks” of the muscular system in the same sense Sarcomere – area between 2 adjacent Z lines
that neurons are bldg. blocks of the nervous system
- Most skeletal muscles begin and end in tendons Thick filaments (almost about twice the diameter of the thin
- Muscle fibers are arranged in parallel between the filaments) are made up of Myosin
tendinous ends .: the force of contraction of the units
is additive Thin filaments are made up of Actin, Tropomyosin and
Muscle fibers are – MULTInucleated, LONG, CYLINDRICAL and Troponin
surrounded by a cell membrane – SARCOLEMMA
NOTE: There are no syncytial bridges between cells Thick filaments (MYOSIN) are lined up to form the A BANDS,
- Are made up of myofibrils whereas the Thin filaments (ACTIN, TROPOMYOSIN,
o Myofibrils are divisible into individual TROPONIN) extend out of the A band and into less dense
filaments staining I BANDS
o Myofilaments – has several proteins that
together make up the contractile machinery The lighter H BANDS in the center of A BANDS are the region
of the skeletal muscle where, when the muscle is relaxed, the thin filaments (actin
Myosin – II, Actin, Tropomyosin & Troponin – the contractile troponin, tropomyosin) DO NOT overlap the thick filament
mechanism of skeletal muscle are dependent on these proteins (myosin)
- Troponin – has 3 sub units
o Troponin I The Z LINE allow for anchoring of the thin filament
o Troponin T
o Troponin C Each thick filament (myosin) is seen to be surrounded by 6 thin
Note: Other important proteins in muscle are involved in filaments (actin, troponin, and tropomyosin) in a regular
maintaining the proteins that participate in contraction in hexagonal pattern
appropriate structural relation to one another and to the
extracellular matrix Myosin II – the form of myosin found in muscle
- With 2 globular heads and a long tail
Striations - Heads of myosin – form cross bridges with actin
Differences in refractive indexes of the various parts of o Made up of light chains and;
the muscle fiber are responsible for the characteristic cross – o Amino terminal portions of the heavy chains
striations seen in skeletal muscle when viewed under a o Contain an actin-binding site and a catalytic
microscope.
site that hydrolyzes ATP
Myosin – contains heavy chains and light chains (indicated ^)
The LIGHT I BAND id divided by a DARK Z LINE, and the DARK A
Myosin molecules are arranged symmetrically on either side of
BAND has the LIGHTER H BAND in its center
the center of the sarcomere
- This arrangement creates the light areas in the
pseudo-H zone

M LINE - the site of reversal polarity of the myosin molecules in

each of the thick filaments
- At these points, there are slender cross-sections that
hold the thick filament in “proper array”
- Each thick filament contains several hundred myosin
molecules

Thin filaments – are polymers made up of two chains of actin

- Each thin filament has 300-400 actin molecules
- 40 – 60 tropomyosin molecules
- Troponin – molecules are small globular units located
at intervals along the tropomyosin molecules
 o Each of the three troponin subunits has - The sarcoplasmic reticulum is an important store of
unique functions Ca2+and also participates in muscle metabolism.
o Troponin T – bind the troponin component to
Tropomyosin DYSTROPHIN – GLYCOPROTEIN COMPLEX
o Troponin I – inhibits the interaction of Dystrophin protein (427,000 Da) – large
myosin with actin - Forms a rod that connects the thin actin filaments to
o Troponin C – contains binding sites for Ca2+ the transmembrane protein B-dystroglycan (beta) in
Additional Structural Proteins the sarcolemma by smaller proteins in the cytoplasm
Actinin – binds actin to the Z lines Syntrophins
Titin – largest known protein (molecular mass of near - B – dystroglycan is connected to Merosin in the
3,000,000 Da) extracellular matrix by A-dystroglycan (alpha)
- Connects Z lines to the M lines o Merosin – refers to the laminins that contain
- Provides scaffolding for the sarcomere the a (alpha) subunit in their trimeric make
- Has 2 Kinds of folded domains that provide muscle up)
with elasticity - The dystroglycans are in turn associated with a
o 1st – stretched muscle – there is relatively complex of four transmembrane glycoproteins
little resistance as the domain folds o α-, β, γ-, sarcoglycan
o 2nd – muscle further stretched – there is rapid - Dystrophin-Glycoprotein complex – adds strength to
increase in resistance that protects the the muscle by providing a scaffolding for the fibrils and
structure of the sarcomere connecting them to the extracellular environment.
Desmin – adds structure to the Z line in part by binding the Z o Disruption of the tightly choreographed
line to the plasma membrane structure can lead to several pathologies or
muscular dystrophies
NOTE: Although these proteins are important in muscle
structure/function, by no means do they represent an ELECTRICAL CHARACTERISTICS OF SKELETAL MUSCLE
exhaustive list. The electrical events in skeletal muscle and the ionic
fluxes that underlie them share distinct similarities w/ nerves
SARCOTUBULAR SYSTEM (TRIADS) with quantitative differences in timing and magnitude
Muscle fibrils are surrounded by structures made up RESTING MEMBRANE POTENTIAL is about -90 mV
of membrane that appear as vesicles and tubules (when ACTION POTENTIAL lasts 2-4 ms and is conducted along the
viewed under microscope) fiber at about 5m/s
- These are the Sarcotubular system ABSOLUTE REFRACTORY PERIOD – 1-3 ms long
- This is made up of a The after-polarizations, with their related changes in
o T system threshold to electrical stimulation, are relatively prolonged
o Sarcoplasmic reticulum
ION DISTRIBUTION & FLUXES
T system – of transverse tubules, which is continuous with Distribution of ions is similar to nerve cell membranes
sarcolemma of the muscle fiber forms a grid perforated by DEPOLARIZATION (same as nerves) –largely manifestation of
individual muscle fibrils Na+ influx
- The spaces between two layers of T system is an REPOLARIZATION – is largely a manifestation of K+ efflux
extension of the extracellular space
- The T system, which is continuous with the CONTRACTILE RESPONSES
sarcolemma, provides a path for rapid transmission of Muscle fiber membrane depolarization normally
the ACTION POTENTIAL from the cell membrane to all starts at the motor end plate, the specialized structure under
the fibrils in the muscle the motor nerve ending
- The Action potential is transmitted along the muscle
Sarcoplamic Reticulum – forms an irregular curtain around of fiber and initiates the contractile response
each fibril, has an enlarged Terminal Cisterns in close contact
with the T system at the junctions between A and I BANDS THE MUSCLE TWITCH
- At these points of contact, the arrangement of the Muscle Twitch – a single action potential that causes a brief
central T system with a cistern of the sarcoplasmic contraction followed by relaxation
reticulum in either side has led to the use of the term - The teach starts about 2 ms after the start of
TRIADS to describe the system depolarization of the membrane, before
repolarization is completed
 - The duration of the “twitch” varies with the type of
muscle being tested Excitation-contraction coupling – the process by which
- Fast muscle fibers (fine, rapid, precise movements) – depolarization of muscle fibers initiate contraction
7.5 ms (TWITCH DURATION)
- Slow muscle fibers (strong, gross, sustained) – have a The action potential is transmitted to all the fibrils in the fiber
twitch durations up to 100 ms via the T System (previously mentioned)

MOLECULAR BASIS OF CONTRACTION This triggers the release of CA2+ from the Terminal Cisterns
- Brought about by the sliding of the thin filaments over (the lateral sacs of the sarcoplasmic reticulum to the T system).
the thick filaments The depolarization of the T Tubule membrane activated the
- NOTE: the shortening is NOT d/t changes in the actual sarcoplasmic reticulum via the Dihydropyridine receptor
lengths of thick and thin filaments, but by their (DHPR), named for the drug dihydropyridine (which blocks
increased overlapping within the muscle them)
- The WIDTH of A BANDS – constant
- Z lines – move closer together when muscle contract Dihydropyridine receptors (DHPR) – are voltage gated Ca2+
and farther apart when it relaxes channels in the T tubule membrane
- The sliding during muscle contraction occurs when the In cardiac muscle, influx of Ca2+ via these channels
myosin heads bind firmly to actin, bend at the junction trigger the release of Ca2+ stored in the sarcoplasmic reticulum
of the head with the neck and then detach (summary (calcium induced calcium release) by activating Ryanodine
wth) Receptor (RyR).
- This Power stroke – depends on the simultaneous
hydrolysis of ATP Ryanodine Receptor (RyR) – is a ligand gated Ca2+
Myosin II molecules – are dimers that have 2 heads BUT ONLY channel with Ca2+ as its natural ligand.
1 attaches to actin at any given time
In skeletal muscle, Ca2+ entry from the ECF by this route is
In a resting muscle, Troponin I is bound to actin and NOT required for Ca2+ release. Instead, the DHPR that serves
Tropomyosin and covers the sites where myosin heads interact as the voltage sensor unlocks release of Ca2+ from the nearby
with actin. Also here (at rest), the myosin head contains Tightly sarcoplasmic reticulum via physical interaction with the RyR.
Bound ADP The released Ca2+ is quickly amplified through calcium induced
calcium release.
-ACTION POTENTIAL- Ca2+ is reduced in the muscle by the SERCA PUMP
Cytosolic Ca2+ - is increased and Free Ca+ binds to (Sarcoplasmic or Endoplasmic Reticulum Ca2+ ATPase)
Troponin C
- This binding weakens the Troponin I interaction with SERCA pump – uses energy from ATP hydrolysis to remove
actin and exposes the actin binding site for myosin Ca2+ from the cytosol back into the terminal cisterns (where it
allow for formation of myosin/actin cross bridges is stored until released by the next action potential.
- Upon the formation of cross-bridge, ADP, is released,
causing a formational change in the myosin head that Once Ca2+ concentration outside the reticulum has been
moves the thin filament (actin etc) to the thick lowered sufficiently, chemical interaction between myosin and
filament (myosin), compromising the cross-bridge actin ceases and the muscle relaxes.
“power stroke” NOTE: ATP is for bot contraction (myosin head) and relaxation
- ATP quickly binds to the free site on myosin, which (SERCA). If transport of Ca2+ into the reticulum is inhibited,
leads to the detachment of the myosin head form the relaxation does not occur even though there are no more
thin filament action potentials; resulting to a sustained contraction –
- ATP is then hydrolyzed and the inorganic phophase Contracture
(Pi) is then released, causing a “re-cocking” of the
myosin head and completing the cycle
o Many myosin heads cycle at or near the same
time, and they cycle repeatedly, producing
gross muscle contraction
- NOTE: Each power stroke shortens the sarcomere by
about 10 nm. Each thick filament has about 500
myosin heads and each head cycles about 5 times per
sec DURING RAPD CONTRACTION
TYPES OF CONTRACTION
The types of contraction are possible because of elastic and
viscous elements in series with contractile mechanism, it is
possible for contraction to occur without an appreciable
decrease in the length of the whole muscle called Isometric
(Same measures or length)

Contraction against a constant load with a decrease in muscle

length is Isotonic (same tension)

Note: that because work is the product of force times distance,

isotonic do work, whereas isometric does not. .: Muscle can do
negative work while lengthening against a constant weight

SUMMATION OF CONTRACTIONS
The electrical response of a muscle fiber to repeated
stimulation is like that of nerve. The fiber is electrically
refractory only during the rising phase and part of the falling
phase of the spike potential. At this time, the contraction
initiated by the first stimulus is just beginning. However,
because the contractile mechanism does not have a refractory
period, repeated stimulation before relaxation has occurred
produces additional activation of the contractile elements and
a response that is added to the contraction already present.

The tension of the developed summation is considerably

greater than that during of the single muscle twitch.

Tetanus – the rapid repetitive stimulation, activation of the

contractile mechanism occurs repeatedly before any relaxation
has occurred, and the individual responses fuse into one
continuous contraction
- Complete Tetanus – when no relaxation occurs
between stimuli
 o The tension developed is about 4 times
developed by the individual twitch
contractions
- Incomplete Tetanus – when periods of incomplete
relaxation takes place between summated stimuli

NOTE: the stimulation frequency at which summation of

contraction occurs is determined by the twitch duration of the
particular muscle. Ex. if the twitch duration is 10 ms,
frequencies less than 1/10 ms (100/s) cause discrete responses
interrupted by complete relaxation, and frequencies greater
than 100/s cause summation.