STRUCTURE OF CONTRACTILE PROTEINS O1. Each actin (thin) filament is made of two *F* (filamentous) aetins helically wound to each other. 02 Each *F’ actin is a polymer of monomeric “G’ (Globular) actins. 03. Two filaments of another protein, tropomyosin also run close to the *F” actins throughout its length. 04. A complex protein Troponin is distributed at regular intervals on the tropomyosin. 05. In the resting state a subunit of troponin masks the active binding sites for myosin on the actin filaments, 06. Each myosin (thick) filament is also a polymerised protein. 07. Many monomeric proteins called Meromyosins constitute one thick filament (Myosin). 08, Each meromyosin has two important parts, a globular head with a short arm and a tail 09. The former being called the heavy meromyosin (HMM). 10, The latter, the light meromyosin (LMM) 11, The HMM component, i.e. the head and short arm projects outwards at regular distance and angle from each other from the surface of a myosin filament and is known as cross arm 12, The globular head is an active ATPase enzyme and has binding sites for ATP and active sites for actin, Actin binding sites ATP binding sites Cross arm (b) Figure 20.3 (a) An actin (thin) filament (b) Myosin monomer (Meromyosin) 13.The G-actin polymerises to form the F-actin in the presence of magnesium ion. 14-Tropomyosin is a fibrous molecule.(Fibre like, Thread Like) 15. At resting state it separates the actin and myosin by binding to the myosin binding site on actin filament and hence prevents the formation of cross bridges which in turn prevents the contraction of muscle fibre.16. At regular intervals of tropomyo a complex protein called troponin is present. 17.A troponin is a trimeric protein ie, it has three units which acts as the binding sites for three different components, 18. The three units of troponin are i) Troponin I : It inhibits actin-myosin interaction (between F-Actin & My’ other components. ii) Troponin Itis the binding site for tropomyosin iii) Troponin C ; Itis thing site for calcium in ) and binds to Distinguish between A band and I band myosin and actin filaments A-Band (Anisotropic band) I- Band (Isotropic band) parts of actin filaments. Zone Ithas wide H-zone. Tthas thin Z-line. It gives dark appearance and | It gives light appearance hence GRSeraNce hence also called dark band also called light band, 7 Itcontains myosin filaments and [It contains part of actin filaments Filaments Its length remains unchanged Shortens during muscle contrac Change in length tion, during muscle contraction. Motor Uni 01. Itis the functional unit of a muscle and is formed of all the muscle fibres being supplied by the branches of a single axon of a motor neuron, 02. On an average, there are 100 muscles fibres in a motor unit. But the number of muscle fibres in a motor unit may be as less as only one and two to three, it may be as high as 1900 muscle fibres per motor unit. 03. All the muscle fibres of a motor unit contract or relax simultaneously MECHANISM OF MUSCLE CONTRACTION 01. Mechanism of muscle contraction is best explained by the sliding filament theory 02. It states that contraction of a muscle fibre takes place by the sliding of the thin filaments over the thick filaments, 03. Muscle contraction is initiated by a signal sent by the central nervous system (CNS) via a motor neuron, 04, A motor neuron along with the muscle fibres connected to it constitute a motor unit 05. The junction between a motor neuron and the sarcolemma of the muscle fibre is called the neuromuscular junction or motor-end plate. 06, A neural signal reaching this junction releases a neurotransn which generates an action potential in the sarcolemma. 07. This spreads through the muscle fibre and causes the release of calcium ions into the sarcoplasm 08, Increase in Ca-- level leads to the binding of calcium with a subunit of troponin on actin filaments and thereby remove the masking of active sites for myosin 09, Utilising the energy from ATP hydrolysis, the myosin head now binds to the exposed active sites on actin to form a cross bridge er (Acetyl choline)Actin — filament Myosin _-® filament SSREEBOLLEIGR: ‘ATP Cross bridge Myosin head (Breaking of cross bridge) (Formation of eross bridge) Sliding/rotation Figure 20.4 Stages in cross bridge formation. rotation of head and breaking of cross bridge 10. This pulls the attached actin filaments towards the centre of ‘A’ band. 11, The *Z’ line attached to these actins are also pulled inwards thereby causing a shortening of the sarcomere, i.e., contraction, 12. Itis clear from the above steps, that during shortening of the muscle, i.., contraction, ‘Maximally Contracted ‘Two Sarcomeres Figure 20.5 Sliding-filament theory of muscle contraction (movement of the thin filaments and the relative size of the I band and I zones)the ‘I’ bands get reduced, whereas the ‘A’ bands retain the length. 13. The myosin, releasing the ADP and Pi goes back to its relaxed state. 14, A new ATP binds and the cross-bridge is broken 15. The ATP is again hydrolysed by the myosin head and the cycle of cross bridge formation and breakage is repeated causing further sliding, 16, The process continues till the Ca» ions are pumped back to the sarcoplasmic cistemae in the masking of actin filament. 17. This causes the return of *Z” lines back to their original position, i.e., relaxation 18. The reaction time of the fibres can vary in different muscles. 19, Repeated activation of the muscles can lead to the accumulation of lactic acid due to anaerobic breakdown of glycogen in them, ca g fatigue 20, The sarcomere shortens, but the lengths of thin and thick myofilaments do not change. 21. The ‘H” zone narrows and even disappears when the thin myofilaments meet at the centre of the sarcomere. 22, Thus the length of the sarcomere decreases during contraction. Size of I band also decreases. yoglobin 01. Muscle contains a red coloured oxygen storing pigment (protein) called myoglobin 02. Myoglobin content is high in some of the muscles which gives a reddish appearance 03, Such muscles are called the Red fibres. Differences between red muscle fibres and white muscle fibres Red Muscle Fibres White Muscle Fibres ‘These muscle fibres are dark red which is due to the Th muscle fibres are lighter in colour as they have very less Myoglobin presence of red haemoprotein | quantity myoglobin. called myoglobin Mitochondria | Mitochondria are more in| Mitochondria are less number. number. Sarcoplasmic Reticu- | Red muscles have less White muscles have more lum sarcoplasmic reticulum, sarcoplasmie reticulum, They carry out considerable | They depend mainly on aerobic oxidation without ac- | anacrobic oxidation (glycoly- Lactic acid cumulating much lactic acid, | sis) for energy production and accumulate lactic acid in large amount during strenuous work. Red muscle fibres can con-_ | White muscle fibres soon get Fatigue tract fora longer period fatigued without fatigue. Rate of contraction These muscle fibres have slow rate of contraction for long periods. “These muscle fibres have a fast rate of contraction for short periods. Examples Extensor muscles of the hu- man back Eye ball muscles,04. These muscles also contain plenty of mitochondria which can utilise the large amount of oxygen stored in them for ATP production. 08. These muscles, therefore, can also be called aerobic muscles. 06. Some of the muscles possess very less quantity of myoglobin and therefore, appear pale or whitish. These are the White fibres. 07. Number of mitochondria are also few in them, but the amount of sarcoplasmic reticulum is high. They depend on anaerobic process for energy. Muscle Fatigue and oxygen debt 1. The reduction in the force of contraction of a muscle after prolonged stimulation is called muscle fatigue 02.The repeated contraction of the skeletal muscle anaerobically leads to the mulation of lactic acid in the muscle 03.The glycogen present in the body breaks anaerobically to produce lactic acid whose accumulation causes pain and fatigue. 04, The lactic acid accumulated in myocytes then diffuses into blood and transport to liver 05.During strenuous exercise, the muscle does not get sufficient oxygen to meet its energy needs immediately 06.0 it contracts anaerobically and accumulates lactic acid produced by anaerobic glycolysis, 07.During recovery, the oxygen consumption of muscle exceeds. 08.The extra oxygen consumed during recovery is called oxygen debt of the muscle. 09.Itis used in oxidising the accumulated lactic acid aerobically and in restoring the depleted creatine phosphate and ATP in the muscle fibre. 10. A small part of oxygen debt also goes to myoglobin which binds and stores oxygen for future use. 11. For extra oxygen, deep and rapid breathing oceurs carrying more oxygen into the lungs and eventually to the tissues. Rigor Mortis 01. The rigidity of muscles that occurs after death is called rigor-mortis. It is due to complete depletion of ATP and Phosphocreatine as Cellular metabolism stop. 02.Rigor montis disappears some fifteen to twenty five hours after death as proteins are degraded