Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM.
Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease.
Science. 2002 Feb 1;295(5556):865-8.
PubMed.
This report is relevant both from the perspectives of pathogenesis (i.e., does chaperone activity alter susceptibility to PD ?) and potential avenue for therapeutic intervention (i.e., could increasing chaperone Hsp70 activity confer neuroprotection of affected brainstem neurons in PD and, by inference, cortical neurons in dementia with Lewy bodies?)
In related news, data presented by Oyler GA et al. at last month's Society for Neuroscience meeting suggested that parkin also directly binds to Hsp70. This could hint at a complex interplay in normal brain between misfolded proteins, refolding chaperone proteins, and ubiquitin ligases in the ER that mechanistically all are part of the UPR.
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Ottawa Hospital Research Institute
This report is relevant both from the perspectives of pathogenesis (i.e., does chaperone activity alter susceptibility to PD ?) and potential avenue for therapeutic intervention (i.e., could increasing chaperone Hsp70 activity confer neuroprotection of affected brainstem neurons in PD and, by inference, cortical neurons in dementia with Lewy bodies?)
In related news, data presented by Oyler GA et al. at last month's Society for Neuroscience meeting suggested that parkin also directly binds to Hsp70. This could hint at a complex interplay in normal brain between misfolded proteins, refolding chaperone proteins, and ubiquitin ligases in the ER that mechanistically all are part of the UPR.
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