Enhanced oligomerization of the alpha-synuclein mutant by the Cu,Zn-superoxide dismutase and hydrogen peroxide system
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Oligomerisation of wild-type and mutant (A53T, A30P) alpha-synuclein exposed to Cu,Zn-SOD and hydrogen peroxide; effect of scavengers, chelators, carnosine and anserine.
What the authors reported
The A53T mutant oligomerised more than wild-type in the SOD/H2O2 system. Oligomerisation was blocked by a radical scavenger, a spin-trapping agent and a copper chelator, and carnosine and anserine inhibited it effectively. The authors propose hydroxyl radical generation and dityrosine formation as the mechanism.
Limits of this study
In vitro protein chemistry. Full text not read.
Source
PubMed 12661766 · doi:10.1016/s1016-8478(23)13712-5
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.