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    Muscle Physiology: Dr. Shrinidhi

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    Rahul kumar
    This document provides an overview of muscle physiology, including the three main types of muscle tissue - skeletal, smooth, and cardiac muscle. It describes the structure and organization of skeletal muscle from the tissue level down to the molecular level components. The sliding filament theory of muscle contraction is explained in detail. Different muscle fiber types are compared in terms of their characteristics such as size, force production, fatigue resistance and contraction speed.

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    Muscle Physiology: Dr. Shrinidhi

    Uploaded by

    Rahul kumar
    20 views68 pages
    This document provides an overview of muscle physiology, including the three main types of muscle tissue - skeletal, smooth, and cardiac muscle. It describes the structure and organization of skeletal muscle from the tissue level down to the molecular level components. The sliding filament theory of muscle contraction is explained in detail. Different muscle fiber types are compared in terms of their characteristics such as size, force production, fatigue resistance and contraction speed.

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    This document provides an overview of muscle physiology, including the three main types of muscle tissue - skeletal, smooth, and cardiac muscle. It describes the structure and organization of skeletal muscle from the tissue level down to the molecular level components. The sliding filament theory of muscle contraction is explained in detail. Different muscle fiber types are compared in terms of their characteristics such as size, force production, fatigue resistance and contraction speed.

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    20 views68 pages

    Muscle Physiology: Dr. Shrinidhi

    Uploaded by

    Rahul kumar
    This document provides an overview of muscle physiology, including the three main types of muscle tissue - skeletal, smooth, and cardiac muscle. It describes the structure and organization of skeletal muscle from the tissue level down to the molecular level components. The sliding filament theory of muscle contraction is explained in detail. Different muscle fiber types are compared in terms of their characteristics such as size, force production, fatigue resistance and contraction speed.

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    © All Rights Reserved
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    of 68

    MUSCLE PHYSIOLOGY

    DR. SHRINIDHI MBBS, MD


    Disclaimer: These slides should be used as a guide for understanding the concepts only. They are not the notes and they are not an alternative to textbooks.
    MUSCLE TISSUE TYPES
    ▪ Skeletal
    ▪ Attached to bones
    ▪ Nuclei multiple and peripherally located
    ▪ Striated, Voluntary and involuntary (reflexes)
    ▪ Smooth
    ▪ Walls of hollow organs, blood vessels, eye, glands, skin
    ▪ Single nucleus centrally located
    ▪ Not striated, involuntary, gap junctions in visceral smooth
    ▪ Cardiac
    ▪ Single nucleus centrally located
    ▪ Striations, involuntary, intercalated disks
    Classification of Muscles
    Functional
    Syncytium

    Cardiac Single-Unit

    Automaticity

    Striated Smooth
    Muscle Muscle
    Motor Unit
    Composition

    Skeletal Multi-Unit
    Motor Nerve
    Required
    STRUCTURE OF SKELETAL MUSCLE

    ▪ Forms 40% of body weight

    ▪ Locomotion

    ▪ Striated or voluntary

    ▪ Multinucleated
    SKELETAL MUSCLE & ITS CONNECTIVE TISSUE…………
    ▪ Epimysium
    ▪ surrounds entire muscle
    ▪ Perimysium
    ▪ separates muscle into bundles
    of muscle fibers (fascicles)
    ▪ contains blood vessels
    ▪ Endomysium
    ▪ separates muscle fascicles into individual muscle cells (myofibers)
    ▪ contains capillaries
    Epimysium, perimysium, and endomysium all come together at the ends of muscles to form TENDONS
    MICROANATOMY OF SKELETAL MUSCLE
    ▪ Muscle fiber- 10 to 80μ in diameter each is composed of
    1000s of myofibrils

    ▪ Each myofibril is in turn made up of myofilaments

    ▪ Myofilaments

    (i) Contractile- myosin II, actin

    (ii) Modulatory- tropomyosin, troponin


    ORGANIZATION OF MYOFILAMENTS :
    LIGHT MICROSCOPIC STRUCTURE

    ▪ Cross striations due to alternate dark and light bands

    ▪ Light band- Isotropic band- I band- thin filaments

    ▪ Dark band- Anisotropic band- A band- birefringent

    ▪ H zone- lighter zone in A band

    ▪ Z line- in the center of I band

    ▪ M line- in the center of A band

    ▪ Sarcomere- between two z lines- basic unit of muscle


    The thick myosin filament……………..
    ▪ Myofilaments- thick & thin filaments

    ▪ Myosin-10 to 14nm wide & 1.6μm long

    1500 in each myofibril

    Myosin filament made of around 200molecules of myosin

    ▪ Myosin molecule- composed of 6 polypeptide chains- 2 heavy & 4 light chains

    A tail, an arm and 2 globular heads

    Arm and head form cross-bridge

    Two hinges

    Head has sites for ATP and actin binding


    ACTIN……
    ▪ Actin filament - 7nm wide and 1.0μm long
    ▪ Extend on both sides of z-lines
    ▪ F-actin forms a double helix
    ▪ Made of 300 G-actin molecules (MW 42,000)
    ▪ G-actin has active sites for interaction with myosin heads
    ▪ Actin core

    ▪ Tropomyosin

    ▪ Filamentous protein blocks myosin binding site


    on actin, 40nm length and MW of 70,000.

    ▪ Troponin

    ▪ T – attaches troponin complex to tropomyosin

    ▪ I – along with tropomyosin inhibits myosin


    binding site on actin

    ▪ C – binds free intracellular calcium to produce


    a conformational change in tropomyosin
    OTHER STRUCTURAL PROTEINS

    ▪ Titin

    ▪ keeps thick myofilaments centered in sarcomere

    ▪ extends from M line to Z line, largest MW protein known

    ▪ Nebulin

    ▪ determines length of thin myofilaments, “molecular ruler”


    I-band, A-band, and M-line regions of the sarcomere
    OTHER STRUCTURAL PROTEINS……
    ▪ Alpha Actinin – anchors thin myofilaments to the Z-line
    ▪ Beta Actinin – determines length of thin filaments
    ▪ Myomesin – binds titin, aligns thick filaments into hexagonal array
    ▪ Desmin – cytoskeletal protein, connects adjacent sarcomeres
    ▪ C-, H-, and X- proteins – form rings around thick filaments, maintains thick
    filament structure during contraction
    ▪ Cap-Z and tropomodulin – associated with opposite ends of growing thin
    filaments, regulates length
    ▪ Dystrophin – anchors actin filaments to sarcolemma, defective in MD
    ▪ Myotilin – interacts with alpha actinin and Z-lines, sarcomeric organization
    Sarcolemma-
    ▪ Consists of an inner plasma membrane and outer collagenous layer
    ▪ Invaginates at numerous points to form T-tubules
    ▪ Carries action potential
    Sarcoplasm-
    ▪ Consists of myofibrils
    ▪ Numerous mitochondriae lying parallel to myofibrils
    Sarcoplasmic reticulum-
    ▪ L-tubules
    ▪ Storage of calcium ions
    SARCOTUBULAR SYSTEM
    T - tubule- inward extension of sarcolemma
    opens to exterior
    contain ECF
    run transverse to myofibrils
    transmit action potential
    L – tubule - sarcoplasmic reticulum
    run parallel to myofibrils
    terminate in terminal cisternae
    stores calcium ions
    Triads - 2 terminal cisternae abutting a t-tubule
    Steps involved in excitation-
    contraction coupling
    Action potential

    Neuromuscular
    transmission

    End plate potential

    Muscle Action potential


    Propagation of muscle AP
    along sarcolemma

    AP reaches triad
    via T-tubule

    Depolarisation
    of T-tubule

    Dihydropyridine receptor acts as voltage


    sensor
    Opening of Ryanodine receptors

    Ca2+ influx from


    Sarcoplasmic reticulum
    into cytoplasm

    Binding of Ca2+ to Tn C

    Conformational change in
    troponin and tropomyosin
    Exposure of binding sites
    on actin

    Interaction of actin and


    myosin

    Contraction
    Active pumping of Ca2+ back into
    sarcoplasmic reticulum

    Tropomyosin covers binding


    sites of actin

    Relaxation
    THEORIES OF CONTRACTION
    1) Viscoelastic (new elastic body theory) theory- 1840s to1920s - muscle

    acts like a stretched spring contained in a viscous medium.

    2) Continuous filament theory- during contraction actin and myosin

    combine to form a single filament. This undergoes folding and shortening

    due to thermal agitation or loss of water molecules

    3) Sliding filament theory…… the most accepted one


    SLIDING FILAMENT THEORY

    ▪ 1954 by A.F.Huxley and H.E.Huxley independently

    ▪ Two overlapping sets of filaments sliding past each other.

    ▪ Thin filaments at each end of sarcomere move towards center between


    thick filaments.

    ▪ Globular heads of myosin form cross-bridges with actin monomers-


    cross-bridge theory
    ▪ Huxley (1969) - Cross-bridges  attach to thin filament  pull
    towards center  detach  attach further down  Ratchet

    theory or Walk-along theory


    Molecular events associated with
    contraction and relaxation of
    skeletal muscle
    ATP attaches to myosin head

    ATP split into ADP+Pi

    Myosin head cocks up

    Attaches to actin monomer

    Head tilts towards arm


    Powerstroke - Actin is pulled
    ADP & Pi released

    ATP attaches to head

    Head releases from actin

    ATP is cleaved
    To ADP & Pi
    Head cocks up
    EVENTS DURING MUSCLE CONTRACTION

    1. Chemical changes

    2. Mechanical changes

    3. Thermal changes

    4. Electrical changes
    CHEMICAL CHANGES

    ▪ ATP attaches to myosin head splits to ADP+Pi myosin


    head cocks up attaches to actin power-stroke ADP &
    Pi discarded new ATP attaches to myosin head myosin
    head released from actin

    ▪ ATP yields 11.5kcal/mol


    SOURCES OF ATP

    1. ATP present in sarcoplasm  suffice for 1-2sec

    2. Creatine phosphate  suffice for 5-8sec.

    Lohman’s reaction CP + ADP = Creatine + ATP

    3. Glycolysis- suffice for 1min

    4. Oxidation of cellular foodstuff- for longer periods


    MECHANICAL CHANGES

    ▪ Isotonic contraction- shortening of muscle but

    volume remains the same

    ▪ Isometric contraction- no change in the length


    THERMAL CHANGES
    1. Resting heat- A.V.HILL- 300cal/min in 70kg man with 30kg of skeletal
    muscles.

    2. Activation heat- energy required for Ca2+ influx, binding to troponin &
    pumping out of Ca2+- 10cal/gm

    3. Shortening heat- proportional to amount of shortening

    4. Maintenance heat

    5. Relaxation heat

    6. Recovery heat- restitution of ATP and glycogen


    ELECTRICAL CHANGES

    ▪ RMP of -90mv

    ▪ AP moves along sarcolemma

    ▪ Velocity of AP conduction- 5m/sec


    TYPES OF SKELETAL MUSCLE FIBRES
    Kenenisa Bekele
    MUSCLE FIBER TYPE COMPARISON CHART

    Slow-Twitch Fast-Twitch Fast-Twitch


    Characteristic
    Type I Type IIA Type IIX or IIB
    Powerlifting, Powerlifting,
    Marathons, distance
    sprinting, sprinting,
    running, swimming,
    Activities jumping, strength jumping,
    cycling, power walking,
    and agility strength and
    endurance training
    training agility training
    Muscle Fiber
    Small Large Large
    Size
    Force
    Low High Very High
    Production
    Slow-Twitch Fast-Twitch Fast-Twitch
    Characteristic
    Type I Type IIA Type IIX or IIB

    Resistance to Fatigue Slow Quick Very Quick

    Contraction Speed Slow Quick Very Quick

    Mitochondria High Medium Low


    Capillary density High Medium Low
    Myoglobin High Medium Low

    ATPase Level Low Medium High

    Oxidative Capacity High Medium Low


    ▪ Nonathletic individuals have close to a 50/50 balance of fiber types.

    ▪ Training can never make slow-twitch fibers as powerful as fast-twitch, nor can

    training make fast-twitch fibers as fatigue resistant as slow-twitch fibers.

    ▪ Type I fibers in the quadriceps femoris muscles of the legs, can vary from

    <20% (in sprinters) to as high as 95% (in marathon runners). These differences

    are believed to be primarily the result of differences in genetics.


    Disclaimer: These slides should be used as a guide for understanding the concepts only. They are not the notes and they are not an alternative to textbooks.

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