{"id":8681,"date":"2016-06-28T11:00:49","date_gmt":"2016-06-28T11:00:49","guid":{"rendered":"http:\/\/admin.acceleratingscience.com\/proteomics\/?p=8681"},"modified":"2016-07-12T14:04:53","modified_gmt":"2016-07-12T14:04:53","slug":"assessing-health-using-mass-spectrometry-based-proteomics","status":"publish","type":"post","link":"https:\/\/www.thermofisher.com\/blog\/proteomics\/assessing-health-using-mass-spectrometry-based-proteomics\/","title":{"rendered":"Assessing Health Using Mass Spectrometry\u2013Based Proteomics"},"content":{"rendered":"

\"ResearcherProtein levels from vials of whole blood\u00a0are generally clinically determined using single-protein immunoassays. However, according to research by Geyer et al.,1<\/sup>\u00a0a single drop of blood and a mass spectrometer may be all that\u2019s needed to assess human health and disease.<\/p>\n

Currently, single-protein immunoassays are used in clinical practice. However, immunoassays have fundamental limitations when it comes to multiplexing, their specificity for protein isoforms and their incompatibility with hypothesis-free investigations.<\/p>\n

Mass spectrometry (MS)-based proteomics is a technology that could tackle these limitations. Another benefit is that the technology could be capable of discovering biomarkers in just a single drop of blood.<\/p>\n

High-throughput, quantitative MS-based proteomics approaches are thought to be advantageous. But they are\u00a0challenging for various reasons: there is a high dynamic range of protein abundances as well as a lack of reproducible, robust and high-throughput proteomic workflows to identify potential biomarkers in large cohorts. In fact, less than 1.5 novel biomarkers per year were established between 1995 and 2010.1<\/sup><\/p>\n

Geyer et al. show how this is now possible via a rapid and robust \u201cplasma proteome profiling\u201d pipeline, developed thanks to vast improvements in MS-based proteomics technologies in recent years. The workflow uses a single-run shotgun approach, does not require protein depletion, and enables quantitative analysis of hundreds of plasma proteomes from only 1 \u03bcl of blood, using 20-minute gradients.<\/p>\n

This new approach is capable of quantitatively measuring hundreds of plasma proteomes, including members of the inflammatory marker family such as C-reactive protein, as well as the apolipoprotein family, gender-related proteins and more than 40 FDA-approved biomarkers.<\/p>\n

The researchers collected small quantities of blood from 10 individuals, via simple finger pricks, and prepared the samples using protein digestion and the in-StageTip\u00a0method<\/a>.2<\/sup>\u00a0All preparation steps were performed in a single vial.<\/p>\n

Samples were measured using liquid chromatography (LC)-MS consisting\u00a0of an EASY-nLC 1000 ultra-high-pressure system<\/a> coupled via a nano-electrospray ion source to a Q Exactive HF Orbitrap<\/a>\u00a0mass spectrometer\u00a0(all Thermo Scientific). MaxQuant was then used for quantitative label-free analysis of the LC-MS\/MS data.<\/p>\n

Following MS analysis, the team performed data analysis by searching against two different databases: the human UniProt FASTA database and a common contaminants database by the Andromeda search engine. Of the 347 protein groups identified in the 20-minute gradients, 285 were detected in all 10 individuals.<\/p>\n

The entire workflow was shown to be robust and highly reproducible and, including sample preparation and data analysis, took less than three\u00a0hours,\u00a0highlighting the value of quantifying hundreds of proteins in a very short analysis time. Despite using extremely\u00a0short measurements, accuracy and precision of the label-free workflow were excellent, with intra-assay correlation of about R2<\/sup>\u00a0= 0.98 and coefficients of variation smaller than 20% for the majority of quantified proteins. Further, the\u00a0ability to use small sample amounts makes blood testing much less invasive, improves cost-efficiency and is clinically attractive.<\/p>\n

As part of the same study, to investigate a “deeper plasma proteome,” the team also used a combination of peptide prefractionation, a matching library consisting of depleted plasma, and 100-minute high-performance LC (HPLC) gradients\u00a0to obtain a ~1,000 protein quantitative proteome. Unexpectedly, the deep plasma proteome contained only 14\u00a0additional FDA-approved biomarkers compared with the 49\u00a0already found in the 20-minute gradients.<\/p>\n

This\u00a0research shows that plasma proteome profiling from a\u00a0minuscule\u00a0amount of blood can deliver an informative portrait of a patient\u2019s health state. Geyer et al. envision its large-scale use in biomedicine.<\/p>\n

 <\/p>\n

References<\/strong><\/p>\n

1. Geyer, P.E., et al. (2016) \u201cPlasma proteome profiling to assess human health and disease<\/a>,\u201d Cell Systems, 2(3) (pp.185\u2013195). doi:\u00a0http:\/\/dx.doi.org\/10.1016\/j.cels.2016.02.015.<\/p>\n

2. Kulak, N.A., et al. (2014) \u201cMinimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells<\/a>,\u201d Nature Methods, 11 (pp. 319\u2013324). doi: 10.1038\/nmeth.2834.<\/p>\n

Post Author: Kathryn Loydall. Kathryn is a science and medical writer with a background in protein chemistry, biochemistry and applied biology. She enjoys making science accessible to a lay audience through writing, illustrations and media. Originally from the UK, she moved to Vancouver Island in 2008 to complete her PhD focussed on sepsis research and x-ray crystallography of monoclonal antibodies. In 2012, Kathryn left the lab behind to start freelancing as a science and medical writer and editor, and hasn’t looked back since. <\/i><\/p>\n","protected":false},"excerpt":{"rendered":"

Protein levels from vials of whole blood\u00a0are generally clinically determined using single-protein immunoassays. However, according to research by Geyer et al.,1\u00a0a single drop of blood and a mass spectrometer may be all that\u2019s needed to assess human health and disease. Currently, single-protein immunoassays are used in clinical practice. However, immunoassays have fundamental limitations when it<\/p>\n","protected":false},"author":244,"featured_media":8680,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"_monsterinsights_skip_tracking":false,"_genesis_hide_title":false,"_genesis_hide_breadcrumbs":false,"_genesis_hide_singular_image":false,"_genesis_hide_footer_widgets":false,"_genesis_custom_body_class":"","_genesis_custom_post_class":"","_genesis_layout":"","_jetpack_newsletter_access":"","_jetpack_dont_email_post_to_subs":false,"_jetpack_newsletter_tier_id":0,"_jetpack_memberships_contains_paywalled_content":false,"_jetpack_memberships_contains_paid_content":false,"footnotes":""},"categories":[12],"tags":[510,259],"division":[],"class_list":{"0":"post-8681","1":"post","2":"type-post","3":"status-publish","4":"format-standard","5":"has-post-thumbnail","7":"category-methods","8":"tag-whole-blood","9":"tag-workflow","10":"entry"},"_selected_authors":"","_selected_reviewers":"","acf":[],"yoast_head":"\nAssessing 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