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Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model
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Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model
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Journal Article
Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model
2024
Overview
The cellular prion protein, PrP.sup.C, has been postulated to function as a receptor for [alpha]-synuclein, potentially facilitating cell-to-cell spreading and/or toxicity of [alpha]-synuclein aggregates in neurodegenerative disorders such as Parkinson's disease. Previously, we generated the \"Salt (S)\" and \"No Salt (NS)\" strains of [alpha]-synuclein aggregates that cause distinct pathological phenotypes in M83 transgenic mice overexpressing A53T-mutant human [alpha]-synuclein. To test the hypothesis that PrP.sup.C facilitates the propagation of [alpha]-synuclein aggregates, we produced M83 mice that either express or do not express PrP.sup.C . Following intracerebral inoculation with the S or NS strain, the absence of PrP.sup.C in M83 mice did not prevent disease development and had minimal influence on [alpha]-synuclein strain-specified attributes such as the extent of cerebral [alpha]-synuclein deposition, selective targeting of specific brain regions and cell types, the morphology of induced [alpha]-synuclein deposits, and the structural fingerprints of protease-resistant [alpha]-synuclein aggregates. Likewise, there were no appreciable differences in disease manifestation between PrP.sup.C -expressing and PrP.sup.C -lacking M83 mice following intraperitoneal inoculation of the S strain. Interestingly, intraperitoneal inoculation with the NS strain resulted in two distinct disease phenotypes, indicative of [alpha]-synuclein strain evolution, but this was also independent of PrP.sup.C expression. Overall, these results suggest that PrP.sup.C plays at most a minor role in the propagation, neuroinvasion, and evolution of [alpha]-synuclein strains in mice that express A53T-mutant human [alpha]-synuclein. Thus, other putative receptors or cell-to-cell propagation mechanisms may have a larger effect on the spread of [alpha]-synuclein aggregates during disease.
Publisher
Public Library of Science
Subject
