MUSCLE Return to original shape after stretching

General Function: GENERAL TYPES

Contraction

Action of microfilaments + associated proteins

Conversion of chemical to mechanical energy

Majority are mesodermal (mesenchyme) in origin

Except smooth muscle of the iris (ectoderm)

Differentiation via increase in length + myofibrilar

synthesis
Distinguished based on:
Organelles differ from other cellular counterparts
Morphological (overall general feature)
o Sarcolemma (plasmalemma)
Physiological (general function)
Sarcoplasmic reticulum (SER)

Sarcoplasm (cytoplasm)
SKELETAL MUSCLES
Other functions:
Muscle fibers
Produce body movements
Long, cylindrical
Stabilization of body positions
multinucleated (periphery of the cell under the
Control of organ volumes
cell membrane)
Sphincter muscles
Nuclei location distinct in skeletal muscle- found at the
Movement of substances in the body
periphery
Blood, lymph, food and fluids, sperm
_ Hypertrophy
Heat production
Increase in size cell volume or size
Shivering (involuntary action of skeletal muscles)
Dependent on age, sex, nutrition and physical activity
MUSCLE PROPERTIES
Histogenesis of Skeletal Muscle
Excitability

Respond to chemicals released from nerve cells

Conductivity

Ability to propagate electrical signals over a membrane

Contractility

Ability to shorten and generate force

Extensibility

Stretching without getting damaged

Elasticity
 Skeletal Muscle Organization MYOFILAMENTS

Arranged in bundles Thick and thin filaments

Causes the banding patterns in A and I bands
Muscle coverings: (connective tissues) H Zone
Lighter portion of the A band
1. Epimysium Thick filaments only
M Line (G. mitte middle)
surrounding the entire bundle
Bisects the region of the H zone
Continuous with tendon (myotendinous junction) Lateral connections between thick filaments
Myomesin
2. Perimysium _ Myosin-binding proteins
_ Holds thick filaments in place
surrounding a fascicle _ Creatinine kinase catalysis of transfer of
phosphate groups from
3. Endomysium phosphocreatine to ADP supplying ATP for muscle
contraction
Surrounding an individual fiber
Titin Springs the myofilaments back after contraction
With basal lamina secreted by individual muscle
fibers

SKELETAL MUSCLE FIBERS

Striations are caused by alternating bands

Endomysium stained with antilaminin. Note that the basal a) A bands
lamina of the endomysium is formed by the underlying Anisotropic - birefringent in polarized light
muscle fiber Darker bands
Thick myofilaments
Myotendinous Junction- part of a tendon (T) inserted into the b) I bands
endomysium and perimysium of a muscle Isotropic do not alter polarized light
Lighter bands
Connective tissues
Thin myofilaments
Transmits mechanical forces generated by c) Z line/disc
Zwischenscheibe
contracting muscles Bisects the I bands
Terminal ends of a unit of sarcomere
Penetrated by blood vessels
Sarcomere= Single contractile apparatus of a muscle
Larger blood vessels and lymphatic vessels in

epi- and perimysium

Capillaries extend up to the endomysium

Myofibrils are cylindrical bundles of thick and thin

myofilaments that fill most of each muscle fiber

 B THICK FILAMENTS
Myosin
Larger and more complex protein
Two identical heavy chain + two pairs of light chains

Myosin heavy chain

_ Thin, rod-like molecules
_ Myosin tails (twisted heavy chains)
_ Myosin heads
- ATP binding and hydrolysis (ATPase activity) site
MYOFILAMENTS - Actin binding
Thin filaments Myosin light chain
o F-actin -Associated with the myosin heads
Tropomyosin
Forms troponin TRANSVERSE TUBULE SYSTEM
Thick filaments T-tubules
Myosin Invaginations of the sarcolemma
Actin and myosin constitute 55% of total Provides uniform contraction to muscle
protein of striated muscle
Both actin and myosin are contractile proteins

A. THIN FILAMENTS
Long filamentous polymers (F-actin)
2 strands of G-actin (globular) monomers
Assymetric
Produce filament polarity
Twisted orientation (double helix)

Tropomyosin
Long thin molecule containing two polypeptide
chains
Assembles to form a long polymer located in the
groove between the two twisted actin strands
Troponin
3 subunits:
TnT (attachment to tropomyosin)
TnC (binds calcium ions)
TnI (inhibits actin-myosin interaction)

Troponin and tropomyosin are considered to be regulatory

proteins

INNERVATION
Action of the muscle
Motor end-plate
A.k.a. neuromuscular junction
Unmyelinated axon terminating on the muscle cell
surface
Site of innervation
 during contraction

shortening of the sarcomere shortens the

entire muscle fiber

Partially Contracted Muscle Fully Contracted muscle

H zone narrower H zone and I band
Z discs closer to one disappear
another Shortest sarcomere
Neuromuscular Junction: Titin molecules length
MUSCLE CONTRACTION AND RELAXATION become more
1. Arrival of nerve signal compressed
2. Acetylcholine (Ach) release
3. Binding of Ach to receptors
4. Opening of ligand-gated ion channel: creation of
end-plate potential
5. Opening of voltage-gated ion channels; creation of
action potentials
6. Action potentials propagated down T-tubules
7. Calcium release
8. Binding of Calcium to troponin
9. Shifting of tropomyosin; exposure of active sites on
actin Rigor Mortis
10. Activation and cocking of myosin head Takes place in skeletal muscles 3-4 hours after
11. Formation of myosin-actin cross bridge death
12. Power stoke; sliding of thin filament over thick Caused by the continuous leaking of Ca2+
filament molecules in the sarcolemma
13. Binding of new ATP; breaking of cross bdirge After breathing stops, ATP production
14. Cessation of nervous stimulation and Ach release stops as well
15. Ach breakdown by acetylcholinase (Ache) Crossbridges are retained due to Ca2+
16. Resorption of Calcium ions by sarcoplasmic Lasts for 24 hours
reticulum Disappears after due to the digestion of
17. Loss of Calcium ions from troponin crossbridges by proteolytic enzymes of lysosomes
18. Return of tropomyosin to position blocking active
sites of actin. Myasthenia gravis
Autoimmune disease
Sarcomere Antibodies blocks ACh receptors
Overlapping thick and thin filaments Inhibition of a neuromuscular junction
Contraction Self-limiting
Increased amount of the overlapping thin and However, the replacement of accepted receptors
thick filaments are again blocked by antibodies
Caused by the sliding of the myofilaments
Induced by action potential of the NS producing results to muscle weakness
its own muscular action potential cardiac muscles are not affected since only the
Relaxation autonomic nervous system signals the heart
Mechanism of Acetylcholinesterase (AChE)
o Breaks down ACh within the synaptic cleft Strabismus
Weakness in one eyelid muscle
o Ceases the muscle Action potential
o Ca2+ channels close
MUSCLE METABOLISM
Switch in the consumption of energy by muscles
sliding movement of the thin myofilaments
High ATP consumption during contraction
towards the M line
Moderate amount during relaxed state
Caused by the pull of the thick filaments
Energy consumption for active transport
Makes the sarcomere shorter in length
Ca2+ pump of the sarcoplasmic reticulum
o Closer Z discs
length of both filaments are maintained
Available ATP is not for long term use
Supply of ATP for a continuous activity of the muscle may be Aerobic Respiration
derived from the following: Requires oxygen to produce ATP
Oxygen sources:
1. Creatine phosphate/phosphocreatine Muscle fibers (myoglobin)
2. Aerobic cellular respiration Circulating oxygen with blood (hemoglobin)
3. Anaerobic cellular respiration _ Both myo- and hemoglobin are gas carriers
Enables greater amount of energy for
Creatine Phosphate prolonged muscle activity:
Phosphocreatine ~36 ATP for every molecule of glucose
Unique to muscle tissues ~100 ATP for every molecule of fatty acid
Overproduced ATP during relaxation period
converts it to creatine phosphate
o Creatine kinase (CK)
- Transfers one phosphate group from ATP
to creatine
Creatine
- Small amino acid synthesized in the liver, kidney and
pancreas
-Produced creatine are then transferred to muscle fibers

Both ATP and creatine phosphate are enough to produce MUSCLE TYPES
energy for 15 sec

SKELETAL MUSCLE
Three types of skeletal muscles
Type 1 (slow, red oxidative fibers)
Type 2a (fast, intermediate oxidative-glycolytic
fibers)
Type 2b (white glycolytic fibers)
Characterized based on physiological,biochemical and
histochemical properties

Anaerobic respiration Types of Skeletal Muscle Fibers

Takes place after consumption of creatine 1. Red fibers (slow fibers; "slow-twitch" fibers)
phosphate More myoglobin & mitochondria
Do not require oxygen Slow contraction and steady
Glycolytic pathway Predominate in postural muscles; limb muscles
Converts pyruvate to lactic acid (depend on tonus)
Lactic acid can be converted back to glucose depend on cellular respiration for ATP production
Anaerobic respiration + creatine phosphate resistant to fatigue
400-m race 2. White fibers (fast fibers; "fast-twitch" fibers)
Less myoglobin & fewer mitochondria
React quickly; forceful contraction
Rich in glycogen
Depend on glycolysis for ATP production
Fatigue easily
Dominant in muscles used for rapid movement
3. Intermediate fibers
Between red and white
Subclass of white

CARDIAC MUSCLE
The myofibrils of each cell = branched.
interlock with those of adjacent fibers by adherens
junctions.
enable the heart to contract force fully without
ripping the fibers apart.
Cardiac vs. Skeletal
More sarcoplasm and mitochondria
Larger transverse tubules (Z discs) than at A-l
band junctions
Less well-developed SR
Limited intracellular Ca+2 reserves
o more Ca+2 enters cell from extracellular
fluid during contraction

MUSCLE REGENeRATION

Skeletal muscle fibers cannot divide after 1st year

growth is enlargement of existing cells
repair
o satellite cells & bone marrow produce some
new cells
o if not enough numbers---fibrosis occurs
most often
Cardiac muscle fibers cannot divide or regenerate
all healing is done by fibrosis (scar formation)
Smooth muscle fibers (regeneration is possible)
cells can grow in size (hypertrophy)
some cells (uterus) can divide (hyperplasia)
new fibers can form from stem cells in Blood Vessel
walls
AGING

Skeletal muscle starts to be replaced by fat

beginning at 30
use it or lose it

Slowing of reflexes & decrease in maximal strength

Change in fiber type to slow oxidative fibers

(due to lack of use or aging)