Asset Details
Do you wish to reserve the book?
Aggregated α-synuclein and complex I deficiency: exploration of their relationship in differentiated neurons
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Aggregated α-synuclein and complex I deficiency: exploration of their relationship in differentiated neurons
Do you wish to request the book?
Aggregated α-synuclein and complex I deficiency: exploration of their relationship in differentiated neurons
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Aggregated α-synuclein and complex I deficiency: exploration of their relationship in differentiated neurons
2015
Overview
α
-Synuclein becomes misfolded and aggregated upon damage by various factors, for example, by reactive oxygen species. These aggregated forms have been proposed to have differential toxicities and their interaction with mitochondria may cause dysfunction within this organelle that contributes to the pathogenesis of Parkinson’s disease (PD). In particular, the association of
α
-synuclein with mitochondria occurs through interaction with mitochondrial complex I and importantly defects of this protein have been linked to the pathogenesis of PD. Therefore, we investigated the relationship between aggregated
α
-synuclein and mitochondrial dysfunction, and the consequences of this interaction on cell survival. To do this, we studied the effects of
α
-synuclein on cybrid cell lines harbouring mutations in either mitochondrial complex I or IV. We found that aggregated
α
-synuclein inhibited mitochondrial complex I in control and complex IV-deficient cells. However, when aggregated
α
-synuclein was applied to complex I-deficient cells, there was no additional inhibition of mitochondrial function or increase in cell death. This would suggest that as complex I-deficient cells have already adapted to their mitochondrial defect, the subsequent toxic effects of
α
-synuclein are reduced.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 14/19
/ 14/34
/ 14/63
/ alpha-Synuclein - metabolism
/ Animals
/ Biomedical and Life Sciences
/ Electron Transport Complex I - deficiency
/ Electron Transport Complex I - genetics
/ Electron Transport Complex I - metabolism
/ Humans
/ Membrane Potential, Mitochondrial
/ Mice
/ Mitochondrial Diseases - genetics
/ Mitochondrial Diseases - pathology
/ Mutation
/ Original
/ Parkinson Disease - genetics
/ Parkinson Disease - metabolism
/ Parkinson Disease - pathology
