Evidence map›Paper›PMID 24670416›Full record

ArticlePloS one2014

Quantification of pancreatic cancer proteome and phosphorylome: indicates molecular events likely contributing to cancer and activity of drug targets.

David Britton, Yoh Zen, Alberto Quaglia, Stefan Selzer, Vikram Mitra, Christopher Löβner, Stephan Jung, Gitte Böhm, Peter Schmid, Petra Prefot and 11 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 60 citations in OpenAlex.

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  11. Regulatory effects of post-translational modifications on zDHHCThe Journal of biological chemistry · 2020
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  15. Decreased plasma C-reactive protein levels inAnnals of clinical and translational neurology · 2018
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

21 authors at 5 institutions in 1 country.

David BrittonProteome Sciences plc, Cobham, United Kingdom.
Yoh ZenInstitute of Liver Studies, King's College Hospital, London, United Kingdom.
Alberto QuagliaInstitute of Liver Studies, King's College Hospital, London, United Kingdom.
Stefan SelzerProteome Sciences plc, Cobham, United Kingdom.
Vikram MitraProteome Sciences plc, Cobham, United Kingdom.
Christopher LöβnerProteome Sciences plc, Cobham, United Kingdom.
Stephan JungProteome Sciences plc, Cobham, United Kingdom.
Gitte BöhmProteome Sciences plc, Cobham, United Kingdom.
Peter SchmidProteome Sciences plc, Cobham, United Kingdom.
Petra PrefotProteome Sciences plc, Cobham, United Kingdom.
Claudia HoehleProteome Sciences plc, Cobham, United Kingdom.
Sasa KoncarevicProteome Sciences plc, Cobham, United Kingdom.
Julia GeeCardiff School of Pharmacy & Pharmaceutical Sciences, Cardiff University, Cardiff, United Kingdom.
Robert NicholsonCardiff School of Pharmacy & Pharmaceutical Sciences, Cardiff University, Cardiff, United Kingdom.
Malcolm WardProteome Sciences plc, Cobham, United Kingdom.
Leandro CastellanoFaculty of Medicine, Department of Surgery & Cancer, Imperial College, London, United Kingdom.
Justin StebbingFaculty of Medicine, Department of Surgery & Cancer, Imperial College, London, United Kingdom.
Hans Dieter ZuchtProteome Sciences plc, Cobham, United Kingdom.
Debashis SarkerInstitute of Liver Studies, King's College Hospital, London, United Kingdom.
Nigel HeatonInstitute of Liver Studies, King's College Hospital, London, United Kingdom.
Ian PikeProteome Sciences plc, Cobham, United Kingdom.
Proteome Sciences (United Kingdom) · GBCobham (United Kingdom) · GBKing's College Hospital · GBCardiff University · GBImperial College London · GB

Funding

Cancer Research UK 14549Cancer Research UK 16057Department of Health NIHR-RP-011-053Medical Research Council MR/J006742/1
6 · The paper itself

Abstract

objectiveLC-MS/MS phospho-proteomics is an essential technology to help unravel the complex molecular events that lead to and propagate cancer. We have developed a global phospho-proteomic workflow to determine activity of signaling pathways and drug targets in pancreatic cancer tissue for clinical application.

methodsPeptides resulting from tryptic digestion of proteins extracted from frozen tissue of pancreatic ductal adenocarcinoma and background pancreas (n = 12), were labelled with tandem mass tags (TMT 8-plex), separated by strong cation exchange chromatography, then were analysed by LC-MS/MS directly or first enriched for phosphopeptides using IMAC and TiO2, prior to analysis. In-house, commercial and freeware bioinformatic platforms were used to identify relevant biological events from the complex dataset.

resultsOf 2,101 proteins identified, 152 demonstrated significant difference in abundance between tumor and non-tumor tissue. They included proteins that are known to be up-regulated in pancreatic cancer (e.g. Mucin-1), but the majority were new candidate markers such as HIPK1 & MLCK. Of the 6,543 unique phosphopeptides identified (6,284 unique phosphorylation sites), 635 showed significant regulation, particularly those from proteins involved in cell migration (Rho guanine nucleotide exchange factors & MRCKα) and formation of focal adhesions. Activator phosphorylation sites on FYN, AKT1, ERK2, HDAC1 and other drug targets were found to be highly modulated (≥2 fold) in different cases highlighting their predictive power.

conclusionHere we provided critical information enabling us to identify the common and unique molecular events likely contributing to cancer in each case. Such information may be used to help predict more bespoke therapy suitable for an individual case.

Indexed as

Amino Acid SequenceAntineoplastic AgentsBiomarkersDiscriminant AnalysisDNA DamageDNA RepairExtracellular MatrixFocal AdhesionsGene OntologyHumansLeast-Squares AnalysisNeoplasm ProteinsPancreatic NeoplasmsPhosphopeptidesPhosphorylationProtein KinasesAntineoplastic AgentsBiomarkersNeoplasm ProteinsPhosphopeptidesProtein KinasesProteome

Identifiers

PMID24670416
PMCPMC3966770
OpenAlexW2082514169

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.