Dataset Information

High Field Asymmetric Waveform Ion Mobility Spectrometry in Non-targeted Bottom-up Proteomics of Dried Blood Spot

ABSTRACT: Dried Blood Spots samples are a rich source of proteins and have therefore great potential for proteomics biomarker discovery studies. Only a few articles have used DBS samples for non-targeted bottom-up protein analysis, probably due to the complexity of the DBS samples. Gas-phase separation by ion mobility spectrometry such as Field Asymmetric Waveform Ion Mobility (FAIMS) could be useful in analysis of DBS samples as FAIMS has previously shown to be advantageous for bottom-up protein analysis of complex samples. The aim of this project was therefore to evaluate FAIMS in non-targeted analysis of Dried Blood Spots.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood

SUBMITTER: Cecilie Rosting

LAB HEAD: Helen J Cooper

PROVIDER: PXD007926 | Pride | 2018-05-03

REPOSITORIES: Pride

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Publications

High Field Asymmetric Waveform Ion Mobility Spectrometry in Nontargeted Bottom-up Proteomics of Dried Blood Spots.

Rosting Cecilie C Yu Jinglei J Cooper Helen J HJ

Journal of proteome research 20180509 6

Despite the great potential of dried blood spots (DBS) as a source of endogenous proteins for biomarker discovery, the literature relating to nontargeted bottom-up proteomics of DBS is sparse, primarily due to the inherent complexity and very high dynamic range associated with these samples. Here, we present proof-of-concept results in which we have coupled high field asymmetric waveform ion mobility spectrometry (FAIMS) with liquid chromatography-tandem mass spectrometry (LC-MS/MS) for nontarge ...[more]

PMID: 29707944

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Project description:Gliomas represent 80% of all malignant cerebral tumors and are classified within different malignity grade. Glioblastoma, the most aggressive group, represent more than half of all gliomas but remain a heterogeneous group. Indeed, patient survival can reach from several months to a few years after surgery and chemotherapy. To study gliomas, MALDI mass spectrometry imaging is an interesting technique, allowing the analysis of tumor heterogeneity. In this study, MALDI-MSI is coupled with spatially-resolved microproteomic within the objective to identify subgroups of glioblastomas patients in order to help diagnosis and prognostic. Molecular images are generated from thin tissue section in order to determine the spatial localization of digested peptides. Thanks to unsupervised statistical analysis, we then generated hierarchical clustering of homogeneous molecular regions. According to these regions, spatially resolved proteomic gave access to large scale protein identification and relative quantification. Hierarchical clustering reveal three molecular region within all the tumors sample : region red which represent 33% of surface of all sample, region yellow (25.7%) and region blue (40.8%). Consequently, 3 groups of patient can be determined: group A composed mostly of region red (13/50 patients), group B composed mostly of region yellow (9/50 patients) and group C composed mostly of region blue (24/50 patients). Spatially resolved proteomic was performed and the 147 extractions were analyzed by nano-LC MS/MS. Two-way ANOVA test reveal panel of proteins specifically overexpressed in each region. Protein overexpressed in region red are associated with neurogenesis; protein overexpressed in region yellow are associated with an activation of the immune system and protein overexpressed in region blue are involved with viral processes. To conclude, the combination of MALDI-MSI and microproteomic provides new information on these tumors, allowing us to differentiate three group of patient. In the future, these data will permit to build a more precise classification, a better medical care for patients and the identification of potential new therapeutic targets.

Dataset Information

High Field Asymmetric Waveform Ion Mobility Spectrometry in Non-targeted Bottom-up Proteomics of Dried Blood Spot

Publications

High Field Asymmetric Waveform Ion Mobility Spectrometry in Nontargeted Bottom-up Proteomics of Dried Blood Spots.

Similar Datasets

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