Lobster
Distinguished member
- Joined
- Jul 18, 2011
- Messages
- 137
- Reason
- PALS
- Diagnosis
- 01/2007
- Country
- US
- State
- Virginia
- City
- Near DC
Researchers confirm prion-like properties in ALS
2011-09-20
Vancouver, BC - A team of researchers from the University of British Columbia and the Vancouver Coastal Health Research Institute have found a key link between prions and the neurodegenerative disease amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig's disease. The discovery is significant as it opens the door to novel approaches to the treatment of ALS.
A paper, entitled "Intermolecular transmission of SOD-1 misfolding in living cells", was published by the team this week in Proceedings of the National Academy of Sciences (PNAS). The paper demonstrates that the SOD1 protein (superoxide dismutase 1), which has been shown to be implicated in the ALS disease process, exhibits prion-like properties. The researchers found that SOD1 participates in a process called template-directed misfolding. This term refers to the coercion of one protein by another protein to change shape and accumulate in large complexes in a fashion similar to the process underlying prion diseases.
These findings provide a molecular explanation for the progressive spread of ALS through the nervous system, and highlight the central role of the propagation of misfolded proteins in the pathogenesis of neurodegenerative diseases, including ALS, Alzheimer's and Parkinson's.
"Our work has identified a specific molecular target, which when manipulated halts the conversion of the SOD1 protein to a misfolded, disease-causing form," says Dr Neil Cashman, scientific director of PrioNet Canada, Canada Research Chair in Neurodegeneration and Protein Misfolding at UBC, and academic director of the Vancouver Coastal Health ALS Centre. "This discovery is a first-step toward the development of targeted treatments that may stop progression of ALS."
"For many years, ALS has remained a complex puzzle and we have found a key piece to help guide the research community to solutions," says Dr Leslie Grad, a co-first author of the project and current manager of scientific programs at PrioNet Canada. "PrioNet is further exploring this discovery through newly-funded research projects."
The work was completed by Dr Cashman's lab at the Brain Research Centre based at the University of British Columbia and the Vancouver Coastal Health Research Institute, in collaboration with researchers at the University of Alberta. The research was supported by PrioNet Canada and in part by Amorfix Life Sciences and the Canadian Institutes of Health Research.
2011-09-20
Vancouver, BC - A team of researchers from the University of British Columbia and the Vancouver Coastal Health Research Institute have found a key link between prions and the neurodegenerative disease amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig's disease. The discovery is significant as it opens the door to novel approaches to the treatment of ALS.
A paper, entitled "Intermolecular transmission of SOD-1 misfolding in living cells", was published by the team this week in Proceedings of the National Academy of Sciences (PNAS). The paper demonstrates that the SOD1 protein (superoxide dismutase 1), which has been shown to be implicated in the ALS disease process, exhibits prion-like properties. The researchers found that SOD1 participates in a process called template-directed misfolding. This term refers to the coercion of one protein by another protein to change shape and accumulate in large complexes in a fashion similar to the process underlying prion diseases.
These findings provide a molecular explanation for the progressive spread of ALS through the nervous system, and highlight the central role of the propagation of misfolded proteins in the pathogenesis of neurodegenerative diseases, including ALS, Alzheimer's and Parkinson's.
"Our work has identified a specific molecular target, which when manipulated halts the conversion of the SOD1 protein to a misfolded, disease-causing form," says Dr Neil Cashman, scientific director of PrioNet Canada, Canada Research Chair in Neurodegeneration and Protein Misfolding at UBC, and academic director of the Vancouver Coastal Health ALS Centre. "This discovery is a first-step toward the development of targeted treatments that may stop progression of ALS."
"For many years, ALS has remained a complex puzzle and we have found a key piece to help guide the research community to solutions," says Dr Leslie Grad, a co-first author of the project and current manager of scientific programs at PrioNet Canada. "PrioNet is further exploring this discovery through newly-funded research projects."
The work was completed by Dr Cashman's lab at the Brain Research Centre based at the University of British Columbia and the Vancouver Coastal Health Research Institute, in collaboration with researchers at the University of Alberta. The research was supported by PrioNet Canada and in part by Amorfix Life Sciences and the Canadian Institutes of Health Research.
