Kuznetsov Andrey V
Department of Mechanical and Aerospace Engineering, North Carolina State University, Raleigh, North Carolina, USA.
Int J Numer Method Biomed Eng. 2025 Apr;41(4):e70027. doi: 10.1002/cnm.70027.
The paper introduces a parameter called "accumulated neurotoxicity" of α-syn oligomers, which measures the cumulative damage these toxic species inflict on neurons over time, given the years it typically takes for such damage to manifest. A threshold value for accumulated neurotoxicity is estimated, beyond which neuron death is likely. Numerical results suggest that rapid deposition of α-syn oligomers into fibrils minimizes neurotoxicity, indicating that the formation of Lewy bodies might play a neuroprotective role. Strategies such as reducing α-syn monomer production or enhancing degradation can decrease accumulated neurotoxicity. In contrast, slower degradation (reflected by longer half-lives of monomers and free aggregates) increases neurotoxicity, supporting the idea that impaired protein degradation may contribute to Parkinson's disease progression. Accumulated neurotoxicity is highly sensitive to the half-deposition time of free α-syn aggregates into fibrils, exhibiting a sharp increase as it transitions from negligible to elevated levels, indicative of neural damage.
该论文介绍了一种名为α-突触核蛋白寡聚体“累积神经毒性”的参数,它衡量了这些有毒物质随着时间推移对神经元造成的累积损伤,考虑到这种损伤通常需要数年时间才会显现。估计了累积神经毒性的阈值,超过该阈值神经元死亡很可能发生。数值结果表明,α-突触核蛋白寡聚体快速沉积形成原纤维可使神经毒性最小化,这表明路易小体的形成可能起到神经保护作用。诸如减少α-突触核蛋白单体产生或增强降解等策略可以降低累积神经毒性。相比之下,较慢的降解(表现为单体和游离聚集体的半衰期更长)会增加神经毒性,这支持了蛋白质降解受损可能导致帕金森病进展的观点。累积神经毒性对游离α-突触核蛋白聚集体形成原纤维的半沉积时间高度敏感,当它从可忽略不计的水平转变为升高水平时会急剧增加,这表明存在神经损伤。