Plasma Proteome Profiling to Assess Human Health and Disease.
By Philipp E. Geyer, N. Kulak, G. Pichler, L. Holdt, D. Teupser, Matthias Mann. Cell Systems, 2016
625 citations recorded by the source corpus.
Proteins in the circulatory system mirror an individual's physiology. In daily clinical practice, protein levels are generally determined using single-protein immunoassays. High-throughput, quantitative analysis using mass-spectrometry-based proteomics of blood, plasma, and serum would be advantageous but is challenging because of the high dynamic range of protein abundances. Here, we introduce a rapid and robust "plasma proteome profiling" pipeline. This single-run shotgun proteomic workflow does not require protein depletion and enables quantitative analysis of hundreds of plasma proteomes from 1 μl single finger pricks with 20 min gradients. The apolipoprotein family, inflammatory markers such as C-reactive protein, gender-related proteins, and >40 FDA-approved biomarkers are reproducibly quantified (CV <20% with label-free quantification). Furthermore, we functionally interpret a 1,000-protein, quantitative plasma proteome obtained by simple peptide pre-fractionation. Plasma proteome profiling delivers an informative portrait of a person's health state, and we envision its large-scale use in biomedicine.
Subfields: Molecular Biology, Spectroscopy
View Paper: https://www.semanticscholar.org/paper/bdb6c9220e0f57ad40792606ec0ae423aa483304
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In Molecular Biology
- Matthias Mann
- R. Aebersold
- D. Teupser
- L. Holdt
- Philipp E. Geyer
- Ludovic C. Gillet
- George A. Rosenberger
- Ben C. Collins
In Spectroscopy
- Matthias Mann
- R. Aebersold
- D. Teupser
- L. Holdt
- Philipp E. Geyer
- Ludovic C. Gillet
- George A. Rosenberger
- Ben C. Collins
Citations in the corpus
- Revisiting biomarker discovery by plasma proteomics (2017, methodology): “…the peptide in its original sequence context, for instance, in the SILAC-PrEST strategy, in which a 150- to 250-amino acid stretch of each protein of interest, fused to a quantification tag, is recombinant expressed in a heavy form (Zeiler et al, 2012; Edfors et al, 2014; Geyer et al, 2016a).”
- Data‐independent acquisition‐based SWATH‐MS for quantitative proteomics: a tutorial (2018, positive): “…classical label-free DDA proteomics workflow, where quantification is based on precursor ion (MS1) intensities or spectral counts, and which can possibly be combined with peptide fractionation techniques to improve proteome coverage (Lawrence et al , 2015; Geyer et al , 2016; Frejno et al , 2017).”