Dataset Information

Characterization of cerebrospinal fluid via data-independent acquisition mass spectrometry

ABSTRACT: Cerebrospinal fluid (CSF) is in direct contact with the brain and serves as a valuable specimen to examine neurodegenerative diseases in order to identify suitable diagnostic biomarkers. In the field of neuroproteomics the most popular mass spectrometry-based strategy for biomarker discovery studies is data-dependent acquisition (DDA). Drawbacks of this method are stochastic and irreproducible precursor ion selection. Recently, data-independent acquisition (DIA) emerged as an alternative method. In this study we evaluate the use of DIA for native CSF analytics with particular focus on spectral library generation for data analysis, DIA data reproducibility and identification of brain specific proteins.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain, Cerebrospinal Fluid, Blood

SUBMITTER: Katalin Barkovits

LAB HEAD: Katrin Marcus

PROVIDER: PXD009624 | Pride | 2018-09-17

REPOSITORIES: Pride

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Characterization of Cerebrospinal Fluid via Data-Independent Acquisition Mass Spectrometry.

Barkovits Katalin K Linden Andreas A Galozzi Sara S Schilde Lukas L Pacharra Sandra S Mollenhauer Brit B Stoepel Nadine N Steinbach Simone S May Caroline C Uszkoreit Julian J Eisenacher Martin M Marcus Katrin K

Journal of proteome research 20180912 10

Cerebrospinal fluid (CSF) is in direct contact with the brain and serves as a valuable specimen to examine diseases of the central nervous system through analyzing its components. These include the analysis of metabolites, cells as well as proteins. For identifying new suitable diagnostic protein biomarkers bottom-up data-dependent acquisition (DDA) mass spectrometry-based approaches are most popular. Drawbacks of this method are stochastic and irreproducible precursor ion selection. Recently, d ...[more]

PMID: 30207155

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Project description:The current state of proteomics requires a choice between targeted and discovery methods. The former provides exceptional quantitation and data completeness, but only with few analytes. Discovery proteomics can identify hundreds and thousands of proteins in a sample, but with poor quantitation and data completeness. We have established and optimized a method that combines targeted and data-independent acquisition for absolute quantitation of all plasma proteins in a single sequential window acquisition of all theoretical fragment ions (SWATH) acquisition run using a panel of spike-in standards (SIS). We compared the absolute quantitation (AQ) of SWATH and high-resolution multiple-reaction monitoring (MRM-HR) acquisition methods using the 100 protein PlasmaDive SIS panel spiked into human plasma. SWATH provided equivalent quantitation and differentially abundant protein profiles as MRM-HR. Absolute quantities of the SIS peptides from the SWATH data were used to estimate the absolute quantities (eAQ) for all the proteins in the run. The eAQ values provided similar quantitation and differentially abundant protein profiles as AQ and protein group (PG) values, and the eAQ method was the only scheme where all selected proteins were verified by MRM-HR. We applied the eAQ method to a cohort of 16 non-small cell lung cancer (NSCLC) patients receiving immunotherapeutics and found that fibronectin (FN1) and proteoglycan 4 (PRG4) were useful markers for predicting patients who would stay on these agents for at least 6 months (area under the curve of 0.8438 and 0.6735, respectively). Thirteen additional plasma samples confirmed that FN1 and PRG4 are putative biomarkers (positive predictive value is 100% and 85.7%, respectively) for a prolonged (>6 months) response to immunotherapeutic agents. In conclusion, we describe an optimized method for absolute quantification of all proteins in a SWATH run, and this approach is amenable for the identification of plasma biomarkers.

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