Wittung-Stafshede Pernilla
Department of Biology and Biological Engineering, Chalmers University of Technology, S-41296, Gothenburg, Sweden.
Curr Opin Struct Biol. 2022 Feb;72:33-38. doi: 10.1016/j.sbi.2021.07.009. Epub 2021 Aug 24.
Protein assembly into amyloid fibers underlies many neurodegenerative disorders. In Parkinson's disease, amyloid formation of α-synuclein is linked to brain cell death. The gut-brain axis plays a key role in Parkinson's disease, and initial α-synuclein amyloid formation may occur distant from the brain. Because different amyloidogenic proteins can cross-seed, and α-synuclein is expressed outside the brain, amyloids present in the gut (from food products and secreted by microbiota) may modulate α-synuclein amyloid formation via direct interactions. I here describe existing such data that only began to appear in the literature in the last few years. The striking, but limited, data set-spanning from acceleration to inhibition-calls for additional investigations that may unravel disease mechanisms as well as new treatments.
蛋白质组装成淀粉样纤维是许多神经退行性疾病的基础。在帕金森病中，α-突触核蛋白的淀粉样形成与脑细胞死亡有关。肠-脑轴在帕金森病中起关键作用，α-突触核蛋白淀粉样的初始形成可能发生在远离大脑的部位。由于不同的淀粉样蛋白生成蛋白可以交叉播种，并且α-突触核蛋白在大脑外表达，肠道中存在的淀粉样蛋白（来自食品和微生物群分泌）可能通过直接相互作用调节α-突触核蛋白淀粉样的形成。我在此描述仅在过去几年才开始出现在文献中的现有此类数据。这个涵盖从加速到抑制的显著但有限的数据集需要进一步的研究，这可能会揭示疾病机制以及新的治疗方法。
