Torsin

TorsinA, a molecular chaperone-like protein, is localized to the endoplasmic reticulum (ER) where it functions to maintain proper folding and processing of proteins and helps prevent misfolding, ER stress, and protein accumulation associated with neurodegenerative disorders in the brain.  Abnormal torsinA protein resulting from a mutation in the DYT-1 gene was discovered within the past decade to represent an underlying cause of Early Onset Torsion Dystonia (EOTD). Furthermore, torsinA has been shown to be a potent suppressor of alpha-synuclein aggregation in neuronal cells and is co-localized with alpha-synuclein protein aggregates (Lewy Bodies) in postmortem brains of patients with Parkinson’s Disease (PD).

QRxPharma has licensed the torsin technology and established a broad-based Sponsored Research Agreement (SRA) with the University of Alabama, where scientists have established a phenotypic screen in C. elegans and identified known clinical compounds that enhance wild-type human torsinA activity, resulting in prevention of ER stress and neuroprotection of dopaminergic neurons from alpha-synuclein induced neurodegeneration in a preclinical model of PD. In addition, these lead compounds have demonstrated efficacy in mammalian and human models of EOTD.

Support for these discoveries is provided by the Michael J. Fox Foundation, the Bachmann Strauss Foundation, the Dystonia Medical Research Foundation, the NIH and QRxPharma.

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