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Exercise Science & Sport Studies
Physiological Principles of Conditioning for Sports
Dr. Moran
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• Class Textbook
Physiological Aspects of Sport Training and Performance
J. Hoffman
http://www.amazon.com/exec/obidos/ASIN/0736034242/interactiveda162-20/102-3304755-7467337
• Class Website
http://web.cortland.edu/moranm/EXS558/EXS558.html
– Download weekly readings (.PDF)
– Research source links
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Neuromuscular System Outline
I.
Muscle Types
II.
Skeletal Muscle Design
a. Myofibrils (Actin and Myosin)
III. Sliding Filament Theory
IV. Factors Influencing Muscle Force Production
V.
Excitation-Contraction Coupling
VI. Muscle Fiber Types
a. Slow
b. Fast (Oxidative-Glycolytic)
c. Fast Glycolytic
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Types of Muscle
Skeletal
w Voluntary muscle; controlled consciously
w Over 600 throughout the body
Cardiac
w Controls itself with assistance from the
nervous and endocrine systems
w Only in the heart
Smooth
w Involuntary muscle; controlled unconsciously
w In the walls of blood vessels and internal
organs
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Design of Skeletal Muscle
• Epimysium (connective tissue)
surrounds whole muscle
• Fasicles (groups of fibers) surrounded
by perimysium
• Myofibrils surrounded by endomysium
•Responsible for contraction
• Sarcolemma surrounds cellular
contents of each muscle fiber
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Myofibrils
• Composed of myofilaments
• Consist mainly of two proteins
• MYOSIN (thick)
-Features globular heads acting as ATPase (determines rate of contraction)
- M-line in middle of myosin molecule, heads on each side move toward
M-line (bipolar)
• ACTIN (thin):
-two intertwined subunits (forms groove)
-no ATPase (“molecular motor”)
-terminated at Z-line
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Sarcomere: Z-line to Z-line
M line: “naked” region – which way muscle pulls depends on which side is
better anchored (ex: curl vs chin up)
Level of Filament Overlap dictates Force Production
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Sliding Filament Theory
(Huxley 1969)
• Wrapped around ACTIN is Tropomyosin
• Associated with tropomyosin is Troponin
• Troponin consists of three subunits:
TnI – bound to actin
TnT – bound to tropomyosin
TnC – bound to calcium
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Sliding Filament Theory
(con’t)
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
When calcium is released from SR, it binds to TnC
Causes conformational shift (transmitted to rest of troponin
and to tropomyosin)
Causes conformational shift in ACTIN ( exposes active
sites)
MYOSIN’s ATPase cleaves bound ATP (myosin-ADP-Pi)
Myosin-ADP-Pi binds to active site (release of ADP-Pi)
Actomyosin complex formed
“Power stroke” occurs at myosin cross-bridge heads
(shortening)
Following flexion of cross-bridge, ATP binds to myosin
Release myosin cross-bridge from ACTIN (relaxation)
Process repeats or stops when intercellular calcium ↓
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ACTIN and MYOSIN do not change length!
Shortening occurs asynchronously to provide continuous muscle action
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Factors Affecting Force Development
1.
# of cross-bridge formations
- based upon probability
- faster the movement of
ACTIN, ↓ probability of crossbridge formation
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Factors Affecting Force Development
2.
Overlap of ACTIN-MYOSIN
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Motor Unit
* The more delicate
the movement the less
fiber per motor unit as
opposed to gross
movements
Nerve fiber + muscle it innervates = motor unit
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Excitation/Contraction Coupling
- Electrical impulse conducted down axon of motor neuron
- Release of Ach (acetylcholine) at nerve terminal
- ACh crosses cleft and binds with AChR at endplate
- Opens sodium channels and depolarizes (excites) endplate:
endplate potential (EPP)
- EPP causes depolarization (action potential) of entire sarcolemma
surface, including T-tubules
- At specialized regions of T-tubule system there is a close proximity
between its membrane and SR (terminal cisternae)
- In this region T-tubular membrane has dihydropyridine (DHP)
receptors, that act as voltage sensors, sense depolarization
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Excitation/Contraction Coupling (con’t)
- In same region, membrane of SR has ryanodine receptors (Ca2+ channels)
- Depolarization causes conformational change in ryanodine receptors
which causes Ca2+ influx
- Cascade Effect: release of Ca2+ causes additional Ca2+ channels to
open
- Results in sharp in cystolic Ca2+ which then binds to troponin to
stimulate muscle contraction
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Overview
Muscle Fiber Action
w Muscle action is initiated by a nerve
impulse.
w The nerve releases ACh, which allows
sodium to enter and depolarize the cell. If
the cell is sufficiently depolarized, an
action potential occurs which releases
stored Ca2+ ions.
w Ca2+ ions bind with troponin, which lifts the
tropomyosin molecules off the active sites
on the actin filament. These open sites
allow the myosin heads to bind to them.
(continued)
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Overview (continued)
Muscle Fiber Action
w Once myosin binds with actin, the myosin
head tilts and pulls the actin filament so
they slide across each other.
w Muscle action ends when calcium is
pumped out of the sarcoplasm to the
sarcoplasmic reticulum for storage.
w Energy for muscle action is provided when
the myosin head binds to ATP. ATPase on
the myosin head splits the ATP into a
usable energy source.
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Slow-Twitch (Type I) Muscle Fibers
w High aerobic (oxidative) capacity and fatigue resistance
w Low anaerobic (glycolytic) capacity and motor unit
strength
w Slow contractile speed (110 ms to reach peak tension)
and myosin ATPase
w 10–180 fibers per motor neuron
w Low sarcoplasmic reticulum development
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Fast-Twitch (Type IIa) Muscle Fibers
w Moderate aerobic (oxidative) capacity and fatigue
resistance
w High anaerobic (glycolytic) capacity and motor unit
strength
w Fast contractile speed (50 ms to reach peak tension)
and myosin ATPase
w 300–800 fibers per motor neuron
w High sarcoplasmic reticulum development
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Fast-Twitch (Type IIb) Muscle Fibers
w Low aerobic (oxidative) capacity and fatigue resistance
w High anaerobic (glycolytic) capacity and motor unit
strength
w Fast contractile speed (50 ms to reach peak tension)
and myosin ATPase
w 300–800 fibers per motor neuron
w High sarcoplasmic reticulum development
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Muscle Biopsy
w Hollow needle is inserted into muscle to take a sample.
w Sample is mounted, frozen, thinly sliced, and examined
under a microscope.
w Allows study of muscle fibers and the effects of acute
exercise and exercise training on fiber composition.
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“Eccentric exercise-induced morphological changes
in the membrane systems involved in excitationcontraction coupling in rat skeletal muscle”
Takehura H. et al. (2001)
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