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Sliding Filament.

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Presentation on theme: "Sliding Filament."— Presentation transcript:

1 Sliding Filament

2 Thick & thin filaments Myosin tails aligned together & heads pointed away from center of sarcomere

3 Interaction of thick & thin filaments
Cross bridges connections formed between myosin heads (thick filaments) & actin (thin filaments) cause the muscle to shorten (contract) sarcomere sarcomere

4 thick filament (myosin) So that’s where those 10,000,000 ATPs go!
Where is ATP needed? binding site thin filament (actin) myosin head ADP thick filament (myosin) 1 2 ATP So that’s where those 10,000,000 ATPs go! Well, not all of it! form cross bridge release cross bridge 1 1 1 3 shorten sarcomere Cleaving ATP  ADP allows myosin head to bind to actin filament 1 4

5 Closer look at muscle cell
Sarcoplasmic reticulum Transverse tubules (T-tubules) Mitochondrion multi-nucleated

6 Muscle cell organelles
Ca2+ ATPase of SR Sarcoplasm muscle cell cytoplasm contains many mitochondria Sarcoplasmic reticulum (SR) organelle similar to ER network of tubes stores Ca2+ Ca2+ released from SR through channels Ca2+ restored to SR by Ca2+ pumps pump Ca2+ from cytosol pumps use ATP There’s the rest of the ATPs! But what does the Ca2+ do? ATP

7 Muscle at rest Interacting proteins
at rest, troponin molecules hold tropomyosin fibers so that they cover the myosin-binding sites on actin troponin has Ca2+ binding sites

8 The Trigger: motor neurons
Motor neuron triggers muscle contraction release acetylcholine (Ach) neurotransmitter

9 Nerve trigger of muscle action
Nerve signal travels down T-tubule stimulates sarcoplasmic reticulum (SR) of muscle cell to release stored Ca2+ flooding muscle fibers with Ca2+

10 Ca2+ triggers muscle action
At rest, tropomyosin blocks myosin-binding sites on actin secured by troponin Ca2+ binds to troponin shape change causes movement of troponin releasing tropomyosin exposes myosin-binding sites on actin

11 Coupling Excitation to Contraction
Calcium ions (Ca2+) link action potentials to contraction. At rest, Ca2+ is stored in the sarcoplasmic reticulum. Spaced along the plasma membrane (sarcolemma) of the muscle fiber are inpocketings of the membrane that form tubules of the "T system". These tubules plunge repeatedly into the interior of the fiber. The tubules of the T system terminate near the calcium-filled sacs of the sarcoplasmic reticulum. Each action potential created at the neuromuscular junction sweeps quickly along the sarcolemma and is carried into the T system.

12 How Ca2+ controls muscle
Sliding filament model exposed actin binds to myosin fibers slide past each other ratchet system shorten muscle cell muscle contraction muscle doesn’t relax until Ca2+ is pumped back into SR requires ATP ATP ATP

13 Myosin head (low- energy configuration
Thick filament Thin filaments Thin filament Myosin head (low- energy configuration ATP ATP Thick filament Myosin binding sites Thin filament moves toward center of sarcomere. Actin Myosin head (low- energy configuration ADP Myosin head (high- energy configuration P i ADP ADP + P i P i Cross-bridge

14 Ca low concentration: binding sites are covered and contraction stops
Role of Ca and Regulatory Proteins Fig Tropomyosin Ca2+-binding sites Actin Troponin complex (a) Myosin-binding sites blocked Ca low concentration: binding sites are covered and contraction stops Ca hi concentration: muscle contracts Ca2+ Myosin- binding site (b) Myosin-binding sites exposed

15 Put it all together… 1 2 3 ATP 7 4 6 ATP 5

16 How it all works… Action potential causes Ca2+ release from SR
Ca2+ binds to troponin Troponin moves tropomyosin uncovering myosin binding site on actin Myosin binds actin uses ATP to "ratchet" each time releases, "unratchets" & binds to next actin Myosin pulls actin chain along Sarcomere shortens Z discs move closer together Whole fiber shortens  contraction! Ca2+ pumps restore Ca2+ to SR  relaxation! pumps use ATP ATP ATP

17 Fully contracted muscle
Fig Sarcomere 0.5 µm Z M Z Relaxed muscle Contracting muscle Fully contracted muscle Contracted Sarcomere

18


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