Researchers studying Parkinson’s disease have discovered toxic proteins, and identified them as the cause of the disruption of healthy brain cells. The integrity of the cell membranes is being harmed by these oligomers. The report was published in the Journal Science, and came from researchers in Italy, Spain and the United Kingdom. The scientists hope their results will help in the creation of improved drugs to prevent the toxic proteins of Parkinson’s disease from disrupting the healthy cells in the brain.
Parkinson’s slowly destroys the brain cells producing dopamine, and this is what helps control movement. The symptoms worsen as the disease progresses and include tremors, slow movements, rigidity, impaired balance, and difficulty swallowing or talking. Researchers additionally found Parkinson’s disrupts non-dopamine cells as well. This explains the symptoms of disrupted sleep, fatigue, depression and anxiety. The estimation is ten million people are affected by the disease, with roughly one million in the United States. Parkinson’s generally affects people over fifty, but ten percent of the individuals are much younger. For additional details, please visit https://www.medicalnewstoday.com/articles/320399.php.
The study demonstrated the effects when the alpha synuclein protein malfunctions. This causes the formation of oligomer clusters, and this is toxic to the cells in the brain. The oligomers structural features were examined to determine their cell interactions. The cells used came from human brain tumors and the brain cells of rats. The researchers discovered a way to keep the oligomers stable, so the level of detail could be observed. Although the stability was not permanent, it lent significance to the study. Once formed, oligomers rapidly dissolve, enter cells or become long fibers. Two features were identified by the researchers regarding toxicity. The first enabled the oligomers to stick to the walls of the cells, and the second enabled them to disrupt the function of the cells by penetrating the membrane.
Additional experiments discovered a way oligomer toxicity may be reduced. When the protein sequence of the oligomer was altered, it encountered more difficulty sticking to the membrane of the cell. The researchers believe the oligomers behavior is similar to that of virus cells. The difference is the oligomer disrupts, and the virus adapts. It has been suggested by Dr. De Simone that oligomers can attach to the membranes of cells due to an accident of nature. The oligomers contain the same features found in normal membrane proteins. This is what helps with brain signaling.