New insights into the role of mitochondrial dysfunction and protein aggregation in Parkinson's disease.
Parkinson's disease (PD) is a common neurodegenerative movement disorder that affects increasing number of elderly in the world population. The disease is caused by a selective degeneration of dopaminergic neurons in the substantia nigra pars compacta with the molecular mechanism underlying this neurodegeneration still not fully understood. However, various studies have shown that mitochondrial dysfunction and abnormal protein aggregation are two of the major contributors for PD. In fact this notion has been supported by recent studies on genes that are linked to familial PD (FPD). For instance, FPD linked gene products such as PINK1 and parkin have been shown to play critical roles in the quality control of mitochondria, whereas α-synuclein has been found to be the major protein aggregates accumulated in PD patients. These findings suggest that further understanding of how dysfunction of these pathways in PD will help develop new approaches for the treatment of this neurodegenerative disorder.
Xie
Weilin
W
Section of Biochemistry and Cell Biology, Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong.
Wan
Oi Wan
OW
Chung
Kenny K K
KK
D000818:Animals; D006801:Humans; D008928:Mitochondria / Q000378:metabolism / Q000502:physiology*; D008954:Models, Biological; D009154:Mutation; D010300:Parkinson Disease / Q000235:genetics / Q000503:physiopathology*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D051844:alpha-Synuclein / Q000737:chemistry / Q000235:genetics / Q000502:physiology
D011506:Proteins; D051844:alpha-Synuclein; D044767:Ubiquitin-Protein Ligases; C111567:parkin protein