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Human Physiology
Dr. Ahmed Ramadan
2
Motor unit of skeletal muscle
In cardiac muscle and single unit type of smooth muscle , they pass electrical stimuli to each other through gap junction or nexus
Definition
But in skeletal muscle , fibers are not stimulated by adjacent muscle fibers but by motor neurons (somatic)
Types of skeletal muscle fibers
Slow – twitch fibers (S fibers) Fast – twitch fibers (F fibers)
The least fatigable equipped for sustained performance Quickly fatigued
Fatigue
Mainly responsible for brief and rapid contractions
densities of capillaries and mitochondria
concentrations of fat droplets (high - energy substrate reserves)
Content Rich in glycogen but contain little myoglobin
Red pigment (myoglobin) for short-term 02 storage
Rich in oxidative enzymes
Predominate
"Red" muscles "White" muscles
in
Example Soleus muscle maintain the body in an upright position (standing) Gastrocnemius muscle involved in running activity
Contractile apparatus of striated muscle
Z lines or Z plates (plate-like proteins) subdivide each myofibril striated compartments called Sarcomeres
When observed by microscopy light and dark bands and lines (hence the name "striated muscle") created by the thick myosin filaments and thin actin filaments
Actin filaments (Roughly 2000 actin filaments) are bound medially to the Z plate
Sarcomere I band A band
The region of the sarcomere proximal to the Z plate and contains only actin filaments The region where the actin and myosin filaments overlap
The H zone contains myosin filaments only (1000 per sarcomere) which thicken towards the middle of the sarcomere to form the M line (M plate)
Thick & thin filaments
Each myosin filament consists of a bundle of myosin -Il molecules
Each molecule has two globular heads connected by flexible necks to the filamentous tail of the molecule
Myosin Each of the heads has a motor domain with a nucleotide - binding pocket (for ATP or ADP + Pi) and an actin binding site
Conformational changes in the head - neck segment allow the myosin head to ‘tilt’ when interacting with actin
A globular protein molecule (G actin)
Actin Four hundered G actin join to form F-actin
Two F actin combines to form an actin filament
Tropomyosin Joined end - to - end (40 nm each) lie adjacent to the actin filament and a troponin (TN) molecule is attached every 40 nm
Contraction cycle
1) Each of the two myosin heads (M) of a myosin - Il molecule binds one ATP molecule in their nucleotide binding pocket
The resulting M-ATP complex (myosin ATP complex) lies 90 ° angle to the rest of the myosin filament
In this state, myosin has only a weak affinity for actin binding
2) Due to the influence of the increased cytosolic Ca2+ Conc. (on the troponin - tropomyosin complex) actin (A) activates myosin's ATPase resulting in hydrolysis of ATP (ATP
ADP + Pi) and the formation of an A-M-ADP-Pi complex
Detachment of Pi (inorganic phosphate) from the complex results in a conformational change of myosin that the actin - myosin association constant by four powers of ten
3) The myosin heads consequently tilt to a 40 ° angle causing the actin and myosin filaments to slide past each other
The release of ADP from myosin ultimately brings the myosin heads to their final position, at 45 ° angle
The remaining A-M complex is stable and can again be transformed into a weak bond when the myosin heads bind ATP a new ("softening effect" of ATP)
4) If a new ATP is bound to myosin subsequent weakening of actin - myosin bond allows realignment of the myosin head from 45 ° to 90 °, the position preferred by the M-ATP complex
If the cytosolic Ca2+ concentration remains > 10-6 mol / L the cycle will begin anew.
This depends mainly on whether subsequent action potentials arrive
G Vs F Actin Actin / Troponin / Tropomysin Contraction
ATP binding site
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