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DOI 10.1074/mcp.ra119.001702

Медицинская библиотека · Molecular & cellular proteomics : MCP · 2019

Domain-specific Quantification of Prion Protein in Cerebrospinal Fluid by Targeted Mass Spectrometry.

Minikel Eric Vallabh, Kuhn Eric, Cocco Alexandra R, Vallabh Sonia M, Hartigan Christina R, Reidenbach Andrew G, Safar Jiri G, Raymond Gregory J, McCarthy Michael D, O'Keefe Rhonda, Llorens Franc, Zerr Inga, Capellari Sabina, Parchi Piero, Schreiber Stuart L, Carr Steven A

СтатьяПоддержка NIH: внешняя программаПоддержка исследования: вне правительства СШАПоддержка правительства СШАВалидационное исследованиеПеревод в очереди

Аннотация

Therapies currently in preclinical development for prion disease seek to lower prion protein (PrP) expression in the brain. Trials of such therapies are likely to rely on quantification of PrP in cerebrospinal fluid (CSF) as a pharmacodynamic biomarker and possibly as a trial endpoint. Studies using PrP ELISA kits have shown that CSF PrP is lowered in the symptomatic phase of disease, a potential confounder for reading out the effect of PrP-lowering drugs in symptomatic patients. Because misfolding or proteolytic cleavage could potentially render PrP invisible to ELISA even if its concentration were constant or increasing in disease, we sought to establish an orthogonal method for CSF PrP quantification. We developed a multi-species targeted mass spectrometry method based on multiple reaction monitoring (MRM) of nine PrP tryptic peptides quantified relative to an isotopically labeled recombinant protein standard for human samples, or isotopically labeled synthetic peptides for nonhuman species. Analytical validation experiments showed process replicate coefficients of variation below 15%, good dilution linearity and recovery, and suitable performance for both CSF and brain homogenate and across humans as well as preclinical species of interest. In n = 55 CSF samples from individuals referred to prion surveillance centers with rapidly progressive dementia, all six human PrP peptides, spanning the N- and C-terminal domains of PrP, were uniformly reduced in prion disease cases compared with individuals with nonprion diagnoses. Thus, lowered CSF PrP concentration in prion disease is a genuine result of the disease process and not an artifact of ELISA-based measurement. As a result, dose-finding studies for PrP lowering drugs may need to be conducted in presymptomatic at-risk individuals rather than in symptomatic patients. We provide a targeted mass spectrometry-based method suitable for preclinical quantification of CSF PrP as a tool for drug development.

Для цитирования: Minikel Eric Vallabh, Kuhn Eric, Cocco Alexandra R, Vallabh Sonia M, Hartigan Christina R, Reidenbach Andrew G, Safar Jiri G, Raymond Gregory J, McCarthy Michael D, O'Keefe Rhonda, Llorens Franc, Zerr Inga, Capellari Sabina, Parchi Piero, Schreiber Stuart L, Carr Steven A. Domain-specific Quantification of Prion Protein in Cerebrospinal Fluid by Targeted Mass Spectrometry.. Molecular & cellular proteomics : MCP. 2019. DOI: 10.1074/mcp.ra119.001702.

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