中国神经再生研究(英文版) ›› 2020, Vol. 15 ›› Issue (12): 2260-2261.doi: 10.4103/1673-5374.284993

• 观点:神经损伤修复保护与再生 • 上一篇    下一篇

小分子防止神经变性引起α-突触核蛋白聚集

  

  • 出版日期:2020-12-15 发布日期:2020-08-05

Small molecules to prevent the neurodegeneration caused by α-synuclein aggregation

Samuel Peña-Díaz1, Jordi Pujols1, Salvador Ventura1,2   

  1. 1 Institut de Biotecnologia i Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, Spain  2 Institució Catalana de Recerca i Estudis Avançats (ICREA),  Barcelona, Spain
  • Online:2020-12-15 Published:2020-08-05
  • Contact: Salvador Ventura, PhD, salvador.ventura@uab.cat.

摘要: orcid: 0000-0002-9652-6351 (Salvador Ventura)

Abstract: Parkinson’s disease (PD) is a neurodegenerative disorder belonging to a group of human pathologies known as synucleinopathies, which includes multiple system atrophy or dementia with Lewy bodies (Spill- antini et al., 1998). Tese diseases share a common neuropathological feature, the presence of α-synuclein (α-Syn) deposits, although they difer in the cellular and anatomical compartment in which α-Syn in- clusions accumulate. PD afects more than 1% of people over 60 years of age, thus being the second most prevalent neurodegenerative disease in the world and the most common synucleinopathy. Te loss of do- paminergic neurons in the substantia nigra pars compacta during PD progression induces a pronounced dopamine concentration decrease in the synaptic area, which translates into motor symptoms such as bradykinesia, rigidity or resting tremor (Martí et al., 2003). Damaged neurons were reported to have large proteinaceous inclusions, named Lewy’s bodies and neurites, which constitute the major histopathologi- cal hallmark in PD. Amyloid fbrils of α-Syn were identifed as the main component of these inclusions (Spillantini et al., 1997). Te detection of genetic mutations (Polymeropoulos et al., 1997) and multiplications in the SNCA gene (Singleton et al., 2003), which encodes for α-Syn, linked to the early onset and higher penetrance of PD, provide evidence for the connection between the aggregation of this particular protein and PD.