Neuromuscular junction and motor unit

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Neuromuscular junction and motor unit

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A study is conducted on a peripheral neuromuscular disease. In the study, the disease was found to occur secondary to autoimmune destruction of neuromuscular junction motor end-plate receptors. Which of the following is true regarding the type of these receptors and their associated signaling molecule?  

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Acetylcholinesterase (AChE) inhibitors

for neuromuscular junction disease p. 479

Neuromuscular disorders

paraneoplastic syndromes p. 219

Neuromuscular junction diseases p. 480

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In order for a skeletal muscle to contract, your brain sends a signal, in the form of an action potential in an upper motor neuron.

The upper motor neuron is part of the cerebral cortex, and it activates a lower motor neuron, which is located in the anterior horn of the spinal cord.

From here, the action potential is sent through an axon down to its ending branches, called axon terminals, to muscle fibers which they innervate.

The place where an axon terminal meets the muscle fiber is the neuromuscular junction.

The neuromuscular junction has three main parts: a presynaptic membrane, which is the membrane of an axon terminal; a postsynaptic membrane, which is the membrane of a skeletal muscle fiber and is also called a motor end-plate; and a synaptic cleft, which is the gap between the presynaptic and postsynaptic membrane.

When an action potential reaches the axon terminal, it stimulates voltage-gated calcium channels in the membrane to open and extracellular calcium ions flow into the lower motor neuron.

Inside the axon terminal are synaptic vesicles that contain neurotransmitters called acetylcholine.

The calcium that enters the axon terminal binds to the vesicles, which allows them to fuse with the cell membrane of the axon terminal, releasing the acetylcholine into the synaptic cleft.

The acetylcholine then diffuses over to the motor end plate on the muscle fiber - and because it’s a short distance, that diffusion happens really quickly.

Here, two acetylcholine molecules will bind to one ligand-gated ion channel, also called nicotinic receptor.

When that happens, these ligand-gated ion channels, which are selective for positively charged ions, open up.

When they open, lots of sodium ions rush into the skeletal muscle fiber, and a few potassium ions leak out of the cell.

But overall there’s an increase in positive charge on the inside of the muscle fiber and therefore on the inside of the membrane, relative to the outside of the membrane - and this is called depolarization.

This local depolarization on the postsynaptic membrane is called an end-plate potential and it makes the resting potential of the cell membrane which is usually around -100mV, more positive, or in this case, less negative.

Summary

The neuromuscular junction is a site where a motor neuron meets a skeletal muscle fiber. It is where a nerve impulse is transmitted from a motor neuron to a muscle fiber. A neuromuscular junction is made up of a nerve terminal, which contains the neurotransmitter acetylcholine, and a muscle fiber, which has receptors for acetylcholine.

When an action potential reaches the nerve terminal, it causes the release of acetylcholine, which diffuses across the synapse and binds to receptors on the muscle fiber. This activates an ion channel, allowing ions to flow into the muscle fiber and causing it to depolarize. This depolarization triggers the release of calcium ions from intracellular stores, which initiates the contraction of the muscle.

Sources

  1. "Medical Physiology" Elsevier (2016)
  2. "Physiology" Elsevier (2017)
  3. "Human Anatomy & Physiology" Pearson (2018)
  4. "Principles of Anatomy and Physiology" Wiley (2014)
  5. "End-Plate Acetylcholine Receptor: Structure, Mechanism, Pharmacology, and Disease" Physiological Reviews (2012)
  6. "Postsynaptic potentiation and desensitization at the vertebrate end-plate receptors" Progress in Neurobiology (1992)
  7. "Motor neuron, nerve, and neuromuscular junction disease" Current Opinion in Neurology (2011)
Elsevier

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