Prions are misfolded protein species known to cause neurodegeneration in vivo called transmissible spongiform encephalopathies (TSEs), a group of progressive encephalopathies that affect the brain and nervous system of animals and humans. Mental and physical abilities deteriorate and holes appear in the cortex giving the brain tissue a sponge-like-appearance. The disorders cause a steadily worsening impairment of brain function:
- Cognitive decline
- Behavioral changes
- Movement disorders
Examples include classic Creutzfeldt–Jakob disease, the new variant Creutzfeldt–Jakob disease (nvCJD, a human disorder thought to be induced by the consumption of bovine meat of animals with spongiform encephalopathy - BSE), Gerstmann–Sträussler–Scheinker syndrome, fatal familial insomnia and Kuru.
SynAging is using prion-protein-derived oligomer preparations on primary neuronal cultures to model prion disease and induce neurodegeneration and neuronal death.
This enables mechanistic studies of prion-induced neurodegeneration in vitro.
Clients can study their active substances for the ability to prevent or revert prion-derived neurotoxicity in SynAgings assays.
This model of PrP-derived low number oligomers is supported by key publications:
Sponne I, Fifre A, Koziel V, Kriem B, Oster T, Olivier JL, Pillot T. Oligodendrocytes are susceptible to apoptotic cell death induced by prion protein-derived peptides. Glia. 2004 Jul;47(1):1-8.
Sponne I, Fifre A, Koziel V, Kriem B, Oster T, Pillot T. Humanin rescues cortical neurons from prion-peptide-induced apoptosis. Mol. Cell. Neurosci. 2004 Jan;25(1):95-102.
Pillot T, Drouet B, Pinçon-Raymond M, Vandekerckhove J, Rosseneu M, Chambaz J. A nonfibrillar form of the fusogenic prion protein fragment [118-135] induces apoptotic cell death in rat cortical neurons. J. Neurochem. 2000 Dec;75(6):2298-308.
Pillot T, Lins L, Goethals M, Vanloo B, Baert J, Vandekerckhove J, Rosseneu M, Brasseur R. The 118-135 peptide of the human prion protein forms amyloid fibrils and induces liposome fusion. J. Mol. Biol. 1997 Dec 5;274(3):381-93.