PINK1 Defect Causes Mitochondrial Dysfunction, Proteasomal Deficit and α-Synuclein Aggregation in Cell Culture Models of Parkinson's Disease
2009

PINK1 Defect Causes Mitochondrial Dysfunction in Parkinson's Disease Models

Sample size: 15 publication 10 minutes Evidence: moderate

Author Information

Author(s): Wencheng Liu, Christofol Vives-Bauza, Rebeca Acín-Pérez, Ai Yamamoto, Yingcai Tan, Yanping Li, Jordi Magrané, Mihaela A. Stavarache, Sebastian Shaffer, Simon Chang, Michael G. Kaplitt, Xin-Yun Huang, M. Flint Beal, Giovanni Manfredi, Chenjian Li

Primary Institution: Weill Medical College of Cornell University

Hypothesis

Mutations in PINK1 lead to mitochondrial dysfunction and proteasomal deficits in cell culture models of Parkinson's disease.

Conclusion

Mutant PINK1 or loss of PINK1 impairs mitochondrial respiration, ATP synthesis, and increases α-synuclein aggregation.

Supporting Evidence

  • Mutant PINK1 or PINK1 knock-down caused deficits in mitochondrial respiration and ATP synthesis.
  • Proteasome function is impaired with a loss of PINK1.
  • Increased α-synuclein aggregation was observed in cells with mutant PINK1.
  • Del 245-PINK1 did not cause a respiratory defect, acting as a null control.
  • Statistically significant reductions in oxygen consumption and ATP synthesis were detected in cells expressing L347P and E417G PINK1.

Takeaway

When a part of the cell called PINK1 doesn't work right, it can cause problems with energy production and lead to the buildup of harmful proteins in the brain, which is linked to Parkinson's disease.

Methodology

Cell culture systems were used to study the effects of PINK1 mutations on mitochondrial function, respiration, ATP synthesis, and proteasome activity.

Limitations

The study primarily uses cell culture models, which may not fully replicate the complexity of Parkinson's disease in humans.

Statistical Information

P-Value

p<0.01

Statistical Significance

p<0.05

Digital Object Identifier (DOI)

10.1371/journal.pone.0004597

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication