Understanding Molecular Bodyguards Against Parkinson’s Disease

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Understanding Molecular Bodyguards Against Parkinson’s Disease

Neurons are considered the building blocks of the human central nervous system, which consists primarily of the spinal cord and brain. These specialized cells serve many functions, including transmitting signals to other neurons as well as sending commands and receiving sensory input to and from the rest of the body. While they are one of the most important parts of the nervous system, neurons don’t have the ability to repair or replace themselves when they’ve been damaged or degraded.

For this reason, researchers are trying to continue uncovering knowledge about the molecular interactions between the partner molecules that contribute to neuron degradation so that they are able to provide insights about how neurodegenerative diseases like Parkinson’s form.

The Rise of Parkinson’s Disease

Neurodegenerative diseases can cause ongoing damage, deterioration, and even death of the nerve cells of the brain and spinal cord. Since the cells cannot be repaired or replaced, this degeneration results in problems with the functions they once performed. As a result, neurodegenerative diseases often lead to issues with the movement known as ataxias, as well as issues with cognitive functioning, known as dementias.

Parkinson’s disease, known for the tremors, balance issues, and slowed movement, is one of the most common neurodegenerative diseases, affecting more than 10 million people worldwide. Parkinson’s generally affects aging adults. As the world’s life expectancy continues to rise, cases of Parkinson’s are expected to increase as well. Unfortunately, the cause of the disease is still not well understood, making it difficult for researchers to develop therapies to combat it.

α-Synuclein and Cell Damage

While researchers haven’t yet identified the exact cause of Parkinson’s, it has been shown that a protein is known as α-Synuclein likely plays a role in its development. When left to its own devices, α-Synuclein can gather and accumulate on the surface of cell mitochondria. As cell mitochondria die, the neurons themselves are unable to continue to function and slowly degenerate and die. These events correspond with one of the significant features of Parkinson’s—Lewy bodies, which are deposits of destroyed mitochondria and α-Synuclein proteins that accumulate in the brain.

Researchers at the University of Basel Biozentrum in Switzerland have discovered that to prevent cell damage by α-Synuclein, the body has developed a host of chaperone molecules. These molecules interact with and bind to α-Synuclein, helping it fold into the proper shape and preventing its accumulation on cell mitochondria. As more chaperone molecules are discovered—researchers have currently identified 30 to 40 of these helpers—interest in their specific interactions with α-Synuclein has increased.

New Discoveries and Implications for the Future

Biozentrum researchers have continued to make great strides in the discovery of additional chaperone molecules, as well as the areas they seem to interact with on the α-Synuclein protein. Using systematic research on a molecular level, researchers discovered a regular pattern that has revealed the binding location on α-Synuclein. This additional insight suggests that chaperone molecules do much more than help with healthy protein folding, but also prevent cell damage in other ways to maintain the proper amount of healthy α-Synuclein in the cell.

As research continues, scientists hope to develop a deeper understanding of how these molecular interactions prevent cell damage. A better understanding of the development of Parkinson’s disease and other neurodegenerative disorders could lead to more effective therapies to combat—or even cure—this widespread disease.

Stacey Chillemi


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