Evidence map›Paper›PMID 25880590›Full record

ArticleBMC cancer2015

A multiplexed, targeted mass spectrometry assay of the S100 protein family uncovers the isoform-specific expression in thyroid tumours.

Juan Martínez-Aguilar, Roderick Clifton-Bligh, Mark P Molloy

Open access · goldAbstract read
In one paragraph

Article in BMC cancer, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  9. Impact of proteomics investigations on gastric cancer treatment and diagnosis.Gastroenterology and hepatology from bed to bench · 2019
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  13. What gastric cancer proteomic studies show about gastric carcinogenesis?Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Review
  14. Article
  15. Article
  16. S100A4 participates in epithelial-mesenchymal transition in breast cancer via targeting MMP2.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

Juan Martínez-AguilarDepartment of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, 2109, Australia. juan.martinez-aguilar@students.mq.edu.au.
Roderick Clifton-BlighKolling Institute of Medical Research, Royal North Shore Hospital, St Leonards, Sydney, NSW, 2065, Australia. jclifton@med.usyd.edu.au.
Mark P MolloyDepartment of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, 2109, Australia. mark.molloy@mq.edu.au.
Australian Genome Research Facility · AUMacquarie University · AURoyal North Shore Hospital · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMounting evidence demonstrates a causal role for S100 proteins in tumourigenesis and several S100 isoforms have shown utility as biomarkers of several types of cancer. The S100 family is comprised of 21 small isoforms, many of them implicated in important cellular functions such as proliferation, motility and survival. Furthermore, in vivo experiments have proven the role of S100 proteins in tumour growth and disease progression, while other studies have shown their prognostic value and involvement in resistance to chemotherapy drugs. Taken together, all these aspects highlight S100 proteins as potential therapeutic targets and as a promising panel of cancer biomarkers. In this work, we have developed a mass spectrometry (MS)-based method for the multiplexed and specific analysis of the entire S100 protein family in tumour tissues and have applied it to investigate the expression of S100 isoforms in the context of thyroid cancer, the main endocrine malignancy.

methodsSelected Reaction Monitoring (SRM)-MS and stable isotope labelling/label-free analysis were employed to investigate the expression of the 21 S100 protein isoforms in thyroid tissue samples. Specimens included 9 normal thyroid tissues and 27 tumour tissues consisting of 9 follicular adenomas (FA), 8 follicular carcinomas (FTC) and 10 papillary carcinomas (PTC).

resultsThe multiplexed and targeted mass spectrometry method led to the detection of eleven S100 protein isoforms across all tissues. Label- and label-free analyses showed the same significant differences and results were confirmed by western blot. S100A6, S100A11 and its putative interaction partner annexin A1 showed the highest overexpression in PTC compared to normal thyroid. S100A13 was also elevated in PTC. Reduced S100A4 expression was observed in FA compared to all other tissues. FA and FTC showed reduction of S100A10 and annexin A2 expression.

conclusionsTargeted mass spectrometry allows the multiplexed and specific analysis of S100 protein isoforms in tumour tissue specimens. It revealed S100A13 as a novel candidate PTC biomarker. Results show that S100A6, S100A11 and Annexin A1 could help discriminate follicular and papillary tumours. The diagnostic and functional significance of S100A4 and S100A10 reduction in follicular tumours requires further investigation.

Indexed as

AdultAgedAged, 80 and overBiomarkers, TumorFemaleGene ExpressionHumansMaleMass SpectrometryMiddle AgedNeoplasm InvasivenessProtein IsoformsProteomicsReproducibility of ResultsS100 ProteinsThyroid NeoplasmsBiomarkers, TumorProtein IsoformsS100 Proteins

Identifiers

PMID25880590
PMCPMC4391164
OpenAlexW2003109543

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Registered trials

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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.