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Related Concept Videos

Relaxation of Skeletal Muscles01:29

Relaxation of Skeletal Muscles

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The period of muscle contraction primarily influences the duration of stimulation at the neuromuscular junction (NMJ), the presence of free calcium ions in the sarcoplasm, and the availability of energy or ATP to support contractions.
When an action potential reaches the axon terminal, it depolarizes the membrane and opens voltage-gated sodium channels. Sodium ions enter the cell, further depolarizing the presynaptic membrane. This depolarization causes voltage-gated calcium channels to open....
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In skeletal muscles, acetylcholine is released by nerve terminals at the motor endplate—the point of synaptic communication between motor neurons and muscle fibers. The binding of acetylcholine to its receptors on the sarcolemma allows entry of sodium ions into the cell and triggers an action potential in the muscle cell. Thus, electrical signals from the brain are transmitted to the muscle. Subsequently, the enzyme acetylcholinesterase breaks down acetylcholine to prevent excessive...
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Overview of Skeletal Muscle01:15

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Skeletal muscles are composed of a bundle of muscle fibers and are attached to bones through tendons. Each skeletal muscle fiber is a single muscle cell. The sarcolemma, the plasma membrane of a skeletal muscle cell, consists of a lipid bilayer and glycocalyx that supports muscle fibers. The sarcolemma extends into the muscle cells to form tubular structures called transverse or T-tubules. Each side of the T-tubules consists of a membrane-bound structure called the sarcoplasmic reticulum,...
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Excitation-Contraction Coupling in Skeletal Muscles01:20

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Excitation-contraction coupling is a series of events that occur between generating an action potential and initiating a muscle contraction. It occurs at the triad, a structure found in skeletal muscle fibers that comprise a T-tubule and terminal cisternae of the sarcoplasmic reticulum on each side. These triads are visible in longitudinally sectioned muscle fibers. They are typically located at the A-I junction — the junction between the A and I bands of the sarcomere.
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Directly Acting Muscle Relaxants: Dantrolene and Botulinum Toxin01:26

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Directly acting muscle relaxants like dantrolene and botulinum toxin (BoNT) have distinct mechanisms and applications. Dantrolene, a hydantoin derivative, acts on the ryanodine receptor (RYR1) in skeletal muscle cells. RYR1 are calcium channels present at the sarcoplasmic reticulum membrane. In response to excitation, they release calcium ions from the sarcoplasmic reticulum to the cytosol. Calcium promotes actin-myosin-mediated contraction of muscles.
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Functional Characterization of Endogenously Expressed Human RYR1 Variants
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Core skeletal muscle ryanodine receptor calcium release complex.

Angela F Dulhunty1, Lan Wei-LaPierre2, Marco G Casarotto1

  • 1John Curtin School of Medical Research, Australian National University, Canberra, ACT, Australia.

Clinical and Experimental Pharmacology & Physiology
|October 4, 2016
PubMed
Summary

The skeletal muscle ryanodine receptor (RyR1) complex is vital for muscle contraction, linking external signals to internal calcium stores. Its disruption causes severe muscle disorders and developmental issues.

Keywords:
Ca2+ release complexcalsequestrinexcitation-contraction couplingjunctinryanodine receptorskeletal muscletriadin

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Area of Science:

  • Muscle physiology
  • Molecular biology
  • Biochemistry

Background:

  • The skeletal muscle ryanodine receptor (RyR1) complex is crucial for excitation-contraction (EC)-coupling.
  • This complex spans muscle fiber compartments, connecting the extracellular space to the sarcoplasmic reticulum (SR) calcium store.

Purpose of the Study:

  • To review current knowledge of protein interactions within the core RyR1 complex.
  • To summarize the contribution of these interactions to EC-coupling.
  • To identify ongoing challenges in the field.

Main Methods:

  • Literature review of existing research on EC-coupling proteins.
  • Analysis of protein interactions within the RyR1 complex.
  • Synthesis of findings on structural and functional influences on EC-coupling.

Main Results:

  • Essential EC-coupling proteins include DHPR α1S, DHPR β1a, and RyR1.
  • Accessory SR proteins like triadin, junctin, and calsequestrin modulate EC-coupling gain.
  • Mutations in these proteins lead to myopathies and perinatal death.

Conclusions:

  • The RyR1 complex's intricate protein interactions are fundamental to skeletal muscle function.
  • Understanding these interactions is key to addressing muscle diseases.
  • Further research is needed to address remaining challenges in EC-coupling.