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Quantitative real-time quaking-induced conversion allows monitoring of disease-modifying therapy in the urine of prion-infected mice.

MPG-Autoren
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Ryazanov,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Leonov,  A.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Zitation

Shi, S., Wagner, J., Mitteregger-Kretzschmar, G., Ryazanov, S., Leonov, A., Griesinger, C., et al. (2015). Quantitative real-time quaking-induced conversion allows monitoring of disease-modifying therapy in the urine of prion-infected mice. Journal of Neuropathology and Experimental Neurology, 74(9), 924-933. doi:10.1097/NEN.0000000000000233.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0028-3F0E-6
Zusammenfassung
Prion diseases are fatal neurodegenerative diseases characterized by accumulation of the pathogenic prion protein PrP in the brain. We established quantitative real-time quaking-induced conversion for the measurement of minute amounts of PrP in body fluids such as urine. Using this approach, we monitored the efficacy of antiprion therapy by quantifying the seeding activity of PrP from the brain and urine of mice after prion infection. We found that the aggregation inhibitor anle138b decreased the levels of PrP in the brain and urine. Importantly, variations of PrP levels in the urine closely corresponded to those in the brain. Our findings indicate that quantification of urinary PrP enables measurement of prion disease progression in body fluids and can substitute for immunodetection in brain tissue. We expect PrP quantification biologic fluids (such as urine and cerebrospinal fluid) with quantitative real-time quaking-induced conversion to emerge as a valuable noninvasive diagnostic tool for monitoring disease progression and the efficacy of therapeutic approaches in animal studies and human clinical trials of prion diseases. Moreover, highly sensitive methods for quantifying pathologic aggregate seeds might provide novel molecular biomarkers for other neurodegenerative diseases that may involve prion-like mechanisms (protein aggregation and spreading), such as Alzheimer disease and Parkinson disease.