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1.muscular System - Dipita Guha
1.muscular System - Dipita Guha
1.muscular System - Dipita Guha
Around 40% of the body is skeletal muscle. They are also known as striated muscles.
Most of them end and begin in tendons (fibrous tissue attaching a muscle to a bone).
As seen in Fig. 1, each skeletal muscle (A) is composed of muscle bundles (fasciculus) (B) each of which
is surrounded by a type of connective tissue known as perimysium. The fasciculus in turn, is composed of
several fibres (C) (each 10 – 80 μm diameter and
enclosed by the sarcolemma). Each of these fibres
in turn is composed of thousands of myofibrils
(D). Each (D) consists of several myofilaments
(E) that are made up of several myosin and actin
filaments (main protein polymers responsible for
contraction). Myosin (thick) and actin (thin) are
present as interdigitation giving rise to an
alternative dark and light banding pattern as
observed in (D). Differences in the refractive
indexes of various parts of muscle fibres give rise
to the appearance of cross-striations. I (isotropic)
band contains actin whereas the A (anisotropic)
band is made up of myosin. Within the A band
there is a pale region named the H band which is
not superimposed with actin. A transverse M line
is also present in the middle of the H band. The
small projections from the myosin filaments are
known as cross bridges (as seen in L). Their
interaction with actin filaments aid in contraction.
Each myofibril is made up of several units known
as sarcomere (~2 μm) each of which is the length
between two consecutive Z discs. Thus, [1
sarcomere = Z disc – A {pale H (M line)} band –
I band – Z disc]. This complicated yet organized
structure of skeletal muscles, enable its
contraction and relaxation.
Fig. 1. Hierarchical organization of skeletal
muscle.
1
[BIOLOGY FOR ENGINEERS]
Proteins involved: myosin (mostly myosin-II), actin, tropomyosin, troponin. There are others but these
are the fundamental ones. Tropinin in turn has 3 subunits – troponin I, troponin T and troponin C.
Tropomyosin molecules form long filaments that are present between actin chains. At almost regular
intervals, these filaments are interspersed with troponin molecules. The ‘T’ component binds the other
components to tropomyosin. ‘I’ binds to actin and inhibits interaction of myosin with actin and ‘C’ has
binding sites for Ca+2 so as to initiate contraction (Fig. 2).
Steps: action potential travels along motor neuron at nerve end, a neurotransmitter (eg. acetylcholine)
is secreted triggers opening of gated channels of muscle fibre membrane Na+ flows into these cells
sarcoplasmic reticulum (endoplasmic reticulum of muscle cells) releases lot of Ca+2 Ca+2 binds to
troponin C ‘I’s’ interaction with actin weakens actin and myosin slide alongside each other
[contraction]. For [relaxation], Ca+2 released from ‘C’ ‘I’ strongly interacts with actin no sliding.
The sliding filament mechanism: during contraction, the width of the A bands remain constant whereas
the Z lines move closer to each other. On the other hand, these lines move farther when relaxed (Fig. 3).
The energy required for this process is delivered by the hydrolysis of ATP.
Fig. 2. Arrangement of the major proteins Fig. 3. Sliding action of actin on myosin
Present in the heart and is rich in excitatory and conductive muscle fibres.
Striations similar to skeletal muscles (Fig. 4).
2
[BIOLOGY FOR ENGINEERS]
Another unique feature is the specialized tissue (pacemaker tissue) of heart which generates repetitive
action potentials thereby allowing the heart to beat even after the nerves have been cut.
References:
Arthur.C.Guyton, John E Hall, Textbook of Medical Physiology, 13/e, W.B. Saunders Company, 2016.
William F. Ganong, Review of Medical Physiology, 22/e, McGraw Hill, 2005.
https://bioengineering.illinois.edu/news/article/muscle-powered-biobots-walk-command
http://news.mit.edu/2012/mechanical-engineers-create-light-activated-skeletal-muscle-0830
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4858326/