Arias-Carrión Oscar, Guerra-Crespo Magdalena, Padilla-Godínez Francisco J, Soto-Rojas Luis O, Manjarrez Elías
Experimental Neurology, Instituto Nacional de Rehabilitación Luis Guillermo Ibarra Ibarra, Mexico City 14389, Mexico.
Tecnologico de Monterrey, Escuela de Medicina y Ciencias de la Salud, Mexico City 14380, Mexico.
Int J Mol Sci. 2025 Jun 4;26(11):5405. doi: 10.3390/ijms26115405.
Parkinson's disease and related synucleinopathies, including dementia with Lewy bodies and multiple system atrophy, are characterised by the pathological aggregation of the α-synuclein (aSyn) protein in neuronal and glial cells, leading to cellular dysfunction and neurodegeneration. This review synthesizes knowledge of aSyn biology, including its structure, aggregation mechanisms, cellular interactions, and systemic influences. We highlight the structural diversity of aSyn aggregates, ranging from oligomers to fibrils, their strain-like properties, and their prion-like propagation. While the role of prion-like mechanisms in disease progression remains a topic of ongoing debate, these processes may contribute to the clinical heterogeneity of synucleinopathies. Dysregulation of protein clearance pathways, including chaperone-mediated autophagy and the ubiquitin-proteasome system, exacerbates aSyn accumulation, while post-translational modifications influence its toxicity and aggregation propensity. Emerging evidence suggests that immune responses and alterations in the gut microbiome are key modulators of aSyn pathology, linking peripheral processes-particularly those of intestinal origin-to central neurodegeneration. Advances in biomarker development, such as cerebrospinal fluid assays, post-translationally modified aSyn, and real-time quaking-induced conversion technology, hold promise for early diagnosis and disease monitoring. Furthermore, positron emission tomography imaging and conformation-specific antibodies offer innovative tools for visualising and targeting aSyn pathology in vivo. Despite significant progress, challenges remain in accurately modelling human synucleinopathies, as existing animal and cellular models capture only specific aspects of the disease. This review underscores the need for more reliable aSyn biomarkers to facilitate the development of effective treatments. Achieving this goal requires an interdisciplinary approach integrating genetic, epigenetic, and environmental insights.
帕金森病及相关的突触核蛋白病,包括路易体痴呆和多系统萎缩,其特征是α-突触核蛋白(aSyn)在神经元和神经胶质细胞中发生病理性聚集,导致细胞功能障碍和神经退行性变。本综述综合了关于aSyn生物学的知识,包括其结构、聚集机制、细胞相互作用和全身影响。我们强调了aSyn聚集体的结构多样性,从寡聚体到原纤维,它们类似毒株的特性以及它们的朊病毒样传播。虽然朊病毒样机制在疾病进展中的作用仍是一个持续争论的话题,但这些过程可能导致突触核蛋白病的临床异质性。蛋白质清除途径的失调,包括伴侣介导的自噬和泛素-蛋白酶体系统,会加剧aSyn的积累,而翻译后修饰会影响其毒性和聚集倾向。新出现的证据表明,免疫反应和肠道微生物群的改变是aSyn病理学的关键调节因子,将外周过程——尤其是肠道起源的过程——与中枢神经退行性变联系起来。生物标志物开发方面的进展,如脑脊液检测、翻译后修饰的aSyn和实时震颤诱导转化技术,有望实现早期诊断和疾病监测。此外,正电子发射断层扫描成像和构象特异性抗体为在体内可视化和靶向aSyn病理学提供了创新工具。尽管取得了重大进展,但在准确模拟人类突触核蛋白病方面仍存在挑战,因为现有的动物和细胞模型仅捕捉到该疾病的特定方面。本综述强调需要更可靠的aSyn生物标志物来促进有效治疗的开发。实现这一目标需要一种整合遗传、表观遗传和环境见解的跨学科方法。