Nerve cells in the human body can be up to three feet long, without breaking or disintegrating. What makes nerve cells so strong?
Researchers at the University of Illinois have discovered that a unique modification in the cytoskeletal composition makes the long axons on neurons particularly tough. The article was published in the Neuron magazine on April 10. This discovery will help people better treat neurodegenerative diseases.
Microtubules are hollow long cylinders formed by the polymerization of tubulin, which is an important skeleton in all cells of the body. Microtubules in neurons are responsible for intracellular transport and promote axon growth, which is the basis of neuromorphic formation.
"In addition to neurons, the microtubules of cells are in a continuous dynamic state, constantly undergoing disassembly and reconstruction," said Scott Brady, a professor at Illinois University who led the study. Only neurons grow so long in the body, and once these neurons are generated, they will accompany the individual for a lifetime, such as 80 or 100 years.
Compared with other cells, microtubules in neurons are particularly stable and can tolerate a variety of experimental conditions. For example, under conditions of low temperature, Ca2 +, or mitotic inhibitors, microtubules in general cells will collapse, but microtubules in neurons remain stable. Such stability is important for the normal growth and maintenance of axons. However, in aging or neurodegenerative degeneration, too stable neuronal microtubules can also damage the normal function of neurons.
In previous research Brady pointed out that the stability of neurons depends on a unique modification of tubulin. "But at the time we were still not sure what this modification was," he said.
So, Yuyu Song, the first author of the article, started to solve this problem. She was originally a graduate student in Brady's laboratory and now is a postdoctoral fellow at Howard Hughes Medical Research Institute.
The researchers used multiple methods to analyze the modification on the tubulin and the location of the modification. They found that the weak links in tubulin that are easily broken are connected to polyamines by chemical bonds, and it is transglutaminase that is responsible for adding these protective polyamines.
Studies have shown that glutamine transferase catalyzes post-translational modification, adding polyamines to the weak links of tubulin, increasing the positive charge carried by the protein. The researchers inhibited polyamine synthesis and glutamine transferase activity in neurons in vivo and in vitro, respectively, and significantly reduced the stability of neuronal microtubules.
Blocking the weak sites of tubulin tubulin gives the neuron microtubules extraordinary stability, Brady said. The researchers also pointed out that the increase in microtubule stability is related to a decrease in neuronal plasticity. In the course of aging and some neurodegenerative diseases, neuronal microtubules are too stable, which reduces the plasticity of neurons and impairs the normal function of neurons. They believe that further research will help develop new ways to prevent neurodegenerative changes and help people achieve nerve regeneration.
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