帕金森病 z-bo 2020-10-26 349

　　In a new study, researchers in the United Kingdom, Italy, and Spain discovered that toxic protein aggregates associated with Parkinson's disease can damage the cell membranes of healthy neurons, causing cell wall defects and eventually a series of lead.

　　This research studies so-called toxic oligomers. This is a collection of protein molecules that appear when a single protein accidentally folds and aggregates. In the case of Parkinson's disease, the protein involved is αsucucrane. When α-sinucrane functions normally, it plays an important role in signal transduction in the brain. The formation and diffusion of these protein aggregates are considered to be important elements of the molecular mechanism leading to this progressive disease. Understanding how they enter and destroy cells provides opportunities for the development of new and more effective drugs. However, so far, because they are generally unstable, it is difficult to study how they damage brain cells. They disappear or are assembled into larger structures immediately after they are formed, causing less damage to individual cells. In this new study, these researchers were able to study how α-synuclein oligomers remain stable long enough to damage brain cells in unprecedented detail. They determined the specific characteristics of this oligomer, enabling it to attach to the cell wall and "structural core", and subsequently achieved breakthrough results.

　　DeSimone explains: "This is a general feature of protein oligomers. When they bind to the surface of brain cells, they can destroy these brain cells. When this oligomer comes into contact with the cell membrane, it is destroyed. The integrity of the cell membrane Sex is destroyed. This is an important step in the mechanism that causes neuronal death."

　　Dr. Juliana Fusco, a postdoctoral fellow at St. John’s College, University of Cambridge, said: However, it is clear that understanding why these protein aggregates work in this way leads to faster scientific progress in the treatment of Parkinson’s disease. This means you can use a more reasonable approach. Do drug research and development. Toxic protein oligomers are formed in the early stages of a series of events leading to Parkinson's disease. It is believed that this formation process occurs when α-sinucrane is dysfunctional and begins to adhere to each other. at the begining. In this case, their appearance is critical to nerve function. When these oligomers are formed, they diffuse, allowing the first toxic oligomer to diffuse to other cells. In this new study, the researchers used solid-state nuclear magnetic resonance spectroscopy (SSNMR) in the laboratory to study toxic and non-toxic α-sinucrane samples. The latest advances in this technology will allow them to study these protein oligomers in an unprecedented way. They described the different properties of these oligomers, and then these different properties interact with brain cells extracted from rats and cells extracted from human brain tumors. I studied how it affects movement. interaction. In particular, the results of this study may help identify molecules that may attack these destructive α-synuclein oligomers and limit their effects. In October of this year, the University of Cambridge established a new Center for Dislocation Diseases, dedicated to developing treatment strategies for various diseases, including Parkinson's disease. Much of its work is based on such research, which deepens the scientific understanding of the basic processes of neurodegeneration. From this point, scientists can identify potential molecular candidates for future use and optimize them for specific diseases as needed.

　　Professor Dobson said: “One of the really exciting things in this study is the ability to determine the structure of key pathogenic molecules in neurodegenerative diseases. It provides important clues for suggesting its toxicity mechanism and seeking reasonable treatment strategies. ."