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Muscle Strcuture

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mahima
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7 views

Muscle Strcuture

Uploaded by

mahima
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
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STRUCTURE OF

MUSCLE
 Skeletal muscle – 35-65% of carcass weight of
meat animals
 Epimysium- CT sheath covering the entire muscle
 Perimysium- CT sheath surroundinf bundles of MF
 Endomysium- surrounds individual muscle fibres
Muscle fiber/ Myofiber/ Muscle cell

 Structural unit of muscle fiber


 75-92% of total muscle volume

 Long, unbranched, multinucleated, thread like cells

 10-100 µm diameter

Sarcolemma
 Muscle cell membrane (elastic in nature)

 Motor nerve fiber endings terminate on sarcolemma at


myoneural junction
 Motor end plate- structures at myoneural junction form
a raised mound on the muscle surface
Myofibril

 Organelle unique to muscle


 Long thin rods (1-2 µm diameter) with their long
axis parallel to the long axis of the fiber
 Muscle fiber of 50 µm diameter has 1000-2000
myofibrils
 Cross striated myofibrils remain embedded in the
cytoplasm of muscle fiber
Myofibrillar cross section- highly organized array of
dots of two distinct sizes that comprises of
a. Thick filaments – arranged parallel to each other, in
exact alignment across entire surface of myofibril
b. Thin – aligned across myofibril, parallel to each
other and the thick filaments
Thick and thin filaments overlap at certain regions –
hence banded/ striated appearance (alternate light
and dark areas)
 Light band- singly refractive , isotropic, I band
 Dark band- doubly refractive, anisotropic, A band, denser
 Z disk- dark thin band that bisects I band
 Sarcomere- Repeating structural unit of myofibril, basic
unit where muscle contraction and relaxation occurs. It is
unit of myofibril between two Z disks (½ I Band +A
band+½ I band)
 Sarcomere length – 2.5 µm (resting stage)
 H zone- region A band where only thick filaments are
present
 Pseudo H zone- region of A band containing only rod
portion of myosin molecules, no heads present
 M line-
Myofilaments
Thick filaments- constitute A band
 14- 16 nm in diameter, 1.5 µm in length

 Predominant protein- myosin

Thin filaments-
 6-8 nm in diameter, 1 µm on either side of Z disk

 constitute I band and extend beyond I band into A

band
 Predominant protein- actin
Z disk ultrastructure
 An actin filament on one side of the Z disk lies
between two actin filaments on opposite side of Z
disk
 Actin filaments do not pass through the Z disk
 Z disk is made of Z filaments, connect with actin
filaments on either side of Z disk.
 1 actin filament connects to 4 Z filaments that pass
through Z disk and then connects with an actin
filament in the adjacent sarcomere
Proteins of myofibril
 More than 20 proteins where 6 constitute app 90%
of total myofibrillar proteins (MP)
 Myosin, actin, titin, tropomyosin, troponin and nebulin
 On basis of function-
 Contractile- actin , myosin
 Regulatory- tropomyosin, troponin
 Cytoskeletal- titin , nebulin ( integral to structure
of Z disk)
Contractile proteins
1. Actin- 20% of MP
Globular shaped app 5.5 nm in diameter
G shaped actin- monomeric form
G actin monomers polymerize to form F actin
2 strands of F actin are spirally coiled around one
another to form “super helix”
2. Myosin- Fibrous protein , 45% of MP
 Elongated rod shaped with a thickened portion at

one end (head)


 Head region is double headed and projects

laterally from the long axis of the filament


 Portion between head and tail is known as neck
 Myosin filaments are arranged in opposite directions on
either side of M line.
 Mysoin heads- active site which forms cross bridges with
actin filaments during contraction
 Myosin when subjected to proteolytic digestion splits into
two fractions ie. Light meromyosin and heavy
meromyosin
 Pseudo H zone- centre of the A band myosin filaments
contain only rod portion of myosin molecules, no heads
present
Regulatory proteins
Tropomyosin- 5 % of MP, Lies in close contact with actin
filament
Each strand lies alongside, within each groove of actin
super helix
Single molecule extends length of 7 G-actin mol .
Troponin- 5% of MP
 Present at well defined intervals in grooves of actin
filament
 Lies along the tropomysoin strands

 1 mol of troponin for every 7-8 G actin molecules

* refer previous slide for representation


Cytoskeletal proteins
 Titin- most abundant, 10% of MP.
rd
 3 filament

 Largest polypeptide known (25000 aa)

 Extend longitudinally in each half sarcomere from M

line to Z disk
 Portion of titin in

A band is inelastic
and that in I band
is elastic
 Binds to the outside shaft of the thick filament and C
protein that encircles and stabilizes the thick
filament
 Provides scaffold for alignment of filaments during
myofibril and sarcomere formation
 Mature myofibrils- maintains structure and integrity
of myofibrils
 Nebulin – 4% of MP
 Located close and parallel to actin filament
 Extends along the length of the thin filament from A
band to Z disk
 Developing muscle- organization of thin filaments
 Mature muscle- serves as scaffold for stability of
thin filaments, anchors thin filaments to Z disk
 C protein- 2% , H protein- 1%, Myomesin-2%,
Mprotein-1%, skelemin-1%- stabilize the rod
portion of myosin molecules
 Aplha actinin (2%), Cap z (1%)- integral
components of Z disk
Sarcoplasmic reticulum and T tubules
 SR is a membranous system of tubules and cisternae
that forms closely meshed network around each
myofibril
 T tubules- associated with sarcolemma

Elements of SR
 Longitudinal tubules- thin tubules oriented in the
direction of myofibrillar axis
 Fenestrated collar- In the H zone region the longitudinal
tubules converge forming a perforated sheet
 Terminal cisternae- At junction of A and I band the
longitudinal tubules converge and join with a pair of
larger, transversly oriented tubular elements
 Longitudinal tubules extend from fenestrated collar
to terminal cisternae in both directions
 T tubule runs transversely across the sarcomere at
A-I band junction and lies between two tubular
elements of the terminal cisternae pair
 Triad- structure formed by a T-tubule and terminal
cisternae on either sides. This is located at A-I
junction. It is responsible for regulation of excitation-
contraction coupling, whereby a stimulus excites the
muscle and causes it to contract.
 Mitochondria- located in sarcoplasm, power house
of the cell
 Lysosomes- small vesicles located in the sarcoplasm.
Contain enzymes capable of digesting cell.
Cathepsins (proteolytic enzyme) is of major
importance
 Golgi complex- secretory cells
 Smooth muscle- only a small proportion of meat,
has single nucleus, centrally located. SR is less
developed, myofilaments less ordered. Actin and
myosin are present in same proportion as in skeletal
muscle but no striations.

 Cardiac muscle- unique property of rhythmic


contractability, centrally placed nucleus, less
branched fibers, striated appearance. T-tubules are
larger in diameter, occur at Z disk. Terminal
cisternae is absent. Intercalated disk are present
across the entire fiber
Connective tissue
 CT surrounding muscles, muscle bundles and muscle
fibers is fibrous, k/a connective tissue proper
 Bone, cartilage- supportive CT

ground substance plus embedded cells


CT proper
extracellular fibers
Ground substance
 Viscous solution containing soluble glycoproteins
referred to as proteoglycans (core protein attached
to glycosaminoglycans)
 Contains substrates and end products of CT
metabolism such as tropocollagen and tropoelastin
 Glycosaminoglycans – hyaluronic acid and
chondroitin sulphate
Extracellular fibers
 Collagen and elastin
 Collagen- most abundant protein in animal body ,
significantly influences met tenderness
 20-25% of total body protein
 Principal structural protein of CT
 Glycprotein that contain small amounts of glucose and
galactose
 Glycine- most abundant aa , 1/3 rd of total aa
 Hydroxyproline and proline – another 1/3rd ,
hydroxyproline is constant (13-14%) component of
collagen, does not occur in other animal proteins
 Tropocollagen – structural unit of collagen fibril
 Tropocollagen molecules are composed of three α
chains to form a triple helix
 Accordingly 12 types of collagen out of which type
I, III, IV, V and VII are associated with CT of skeletal
muscle.
 Insolubility and high tensile strength of collagen
fibers is due to intermolecular cross linkages which
increases and becomes more stable with age. Hence
meat from aged animals is tougher.
Elastin
 Less abundant CT, rubbery protein present in
arterial walls and ligaments, framework of diff
organs
 Glycine- most abundant aa
 Desmosine and isodesomine are 2 unique aa
present in elastin
 Insolubility – presence of high content of non polar
aa.
Connective tissue cells
 Fibroblasts- synthesize precursors of extracellular
components of CT ie. Tropocllagen, tropoelastin and
ground substance
 Mesenchymal cells- precursors of fibroblasts and
adipoblasts
 Adipose cells- deposition of fat

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