Graduate School of Pharmaceutical Sciences, Duquesne University, 418C Mellon Hall, 913 Bluff Street, Pittsburgh, PA, 15219, USA.
Department of Neurology, University of Pittsburgh, Pittsburgh, PA, USA.
Acta Neuropathol. 2024 Aug 14;148(1):18. doi: 10.1007/s00401-024-02781-3.
Lewy body disorders are heterogeneous neurological conditions defined by intracellular inclusions composed of misshapen α-synuclein protein aggregates. Although α-synuclein aggregates are only one component of inclusions and not strictly coupled to neurodegeneration, evidence suggests they seed the propagation of Lewy pathology within and across cells. Genetic mutations, genomic multiplications, and sequence polymorphisms of the gene encoding α-synuclein are also causally linked to Lewy body disease. In nonfamilial cases of Lewy body disease, the disease trigger remains unidentified but may range from industrial/agricultural toxicants and natural sources of poisons to microbial pathogens. Perhaps due to these peripheral exposures, Lewy inclusions appear at early disease stages in brain regions connected with cranial nerves I and X, which interface with inhaled and ingested environmental elements in the nasal or gastrointestinal cavities. Irrespective of its identity, a stealthy disease trigger most likely shifts soluble α-synuclein (directly or indirectly) into insoluble, cross-β-sheet aggregates. Indeed, β-sheet-rich self-replicating α-synuclein multimers reside in patient plasma, cerebrospinal fluid, and other tissues, and can be subjected to α-synuclein seed amplification assays. Thus, clinicians should be able to capitalize on α-synuclein seed amplification assays to stratify patients into potential responders versus non-responders in future clinical trials of α-synuclein targeted therapies. Here, we briefly review the current understanding of α-synuclein in Lewy body disease and speculate on pathophysiological processes underlying the potential transmission of α-synucleinopathy across the neuraxis.
路易体障碍是一组异质性神经疾病,其特征是由错误折叠的α-突触核蛋白聚集物组成的细胞内包涵体。尽管α-突触核蛋白聚集物只是包涵体的一个组成部分,并且与神经退行性变没有严格的关联,但有证据表明它们在细胞内和细胞间引发路易体病理的传播。α-突触核蛋白基因的基因突变、基因组倍增和序列多态性也与路易体病有因果关系。在非家族性路易体病中,疾病的触发因素仍未确定,但可能包括工业/农业毒素和天然毒物来源,以及微生物病原体。也许由于这些外围暴露,路易体包涵体在与颅神经 I 和 X 相连的大脑区域的早期疾病阶段出现,这些区域与鼻腔或胃肠道腔中的吸入和摄入的环境元素相互作用。无论其身份如何,一个隐秘的疾病触发因素很可能将可溶性α-突触核蛋白(直接或间接)转化为不溶性的、交叉β-片层聚集物。事实上,富含β-片层的自我复制的α-突触核蛋白多聚体存在于患者的血浆、脑脊液和其他组织中,可以进行α-突触核蛋白种子扩增测定。因此,临床医生应该能够利用α-突触核蛋白种子扩增测定来将患者分层为未来针对α-突触核蛋白的靶向治疗的潜在应答者和非应答者。在这里,我们简要回顾了目前对路易体病中α-突触核蛋白的理解,并推测了α-突触核蛋白病在神经轴内潜在传播的病理生理过程。