帕金森病 z-bo 2020-10-26 390

　　In a new study, researchers from Linkoping University in Sweden, Karolinska Institutet, Uppsala University and Erlangen University Hospital in Germany have discovered a new mechanism that can make nerve cells The smaller channels spread in the brain. These results indicate that harmful protein aggregates or deposits can combine with channels to form proteins, called "free riding", and spread to healthy cells. Neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease and Huntington's disease affect different areas of the human brain. Despite these regional differences, existing studies have shown that the internal processes of cells affected by these diseases have a lot in common. The hallmark of these diseases is that certain proteins begin to form aggregates that destroy cells and ultimately kill them. In Parkinson's disease, an accidentally folded form of α-butenediolate is involved. These aggregates can mobilize the normal form of α-sinucrane, thereby producing more protein aggregates.

　　Martin Hallbeck, a co-author of the paper, a doctor at the Society of Surgical Pathology at Lincopin University Hospital, and an associate professor at the School of Clinical Experimental Medicine at Universite of Linkepin University, said: Spread as a seed to form new aggregates in the next cell. The disease spreads to the brain like an infection. Using the knowledge of how this protein aggregate spreads, in the long run, the spread of this disease in the brain can be controlled. As we all know, units close to each other can create small channels between them, called gap junction channels. These small channels are formed by members of a family of proteins called connexins. Studies by other scientists have shown that connexins also play an important role in other types of diseases (such as HIV/AIDS). This led researchers at Linkopine University to know whether connexin could play a similar role in the brain transmission of Parkinson's disease.

　　The co-author of the paper and senior postdoctoral researcher Juaneyes of Hallbeck's research team said: This shows that in Parkinson's disease and multispectral atrophy (related diseases), connexins play a role in the uptake of disease-related proteins and cell-to-cell migration. "

　　The brain contains more than 10 connexins, but this new study shows that Parkinson’s disease protein deposits only interact with one of them, Cx32. The details of the process by which harmful protein aggregates migrate from one cell to an adjacent cell through this channel-forming protein are still unknown. These researchers found that the channel formed by connexin is too narrow. They knew that these protein aggregates could not pass through, and they found that these protein aggregates bind to the channel forming protein Cx32 and sneak into the cells and culture them in vitro. Inhibition of channel formation in cells interferes with the uptake of α-synuclein. In an experiment using the brain tissues of four deceased patients diagnosed with Parkinson’s disease, 2 cases were directly α-synuclein And connexin. Observation of binding indicates that it is in Parkinson's disease. The brains of diseased patients also interact, but there is no interaction in the normal brain.

　　Hallbeck said: "Cx32 is the target of future drug therapy."

　　Parkinson's disease is the second most common neurodegenerative disease after Alzheimer's disease. The disease is characterized by tremor, muscle stiffness and slow physical activity. Cognitive symptoms are also common in the later stages of the disease. When symptoms become apparent, a relatively large number of nerve cells in the affected brain area die. Currently, there is no treatment available to slow the progression of the disease.