Evidence map›Paper›PMID 19961487›Full record

ArticleCancer science2010

Imaging mass spectrometry of gastric carcinoma in formalin-fixed paraffin-embedded tissue microarray.

Yoshifumi Morita, Koji Ikegami, Naoko Goto-Inoue, Takahiro Hayasaka, Nobuhiro Zaima, Hiroki Tanaka, Takashi Uehara, Tomohiko Setoguchi, Takanori Sakaguchi, Hisashi Igarashi and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Cancer science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

28 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
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  11. Two-dimensional graphene as a matrix for MALDI imaging mass spectrometry.Journal of the American Society for Mass Spectrometry · 2015
    Article
  12. MALDI Imaging mass spectrometry: current frontiers and perspectives in pathology research and practice.Laboratory investigation; a journal of technical methods and pathology · 2015
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Imaging of intact tissue sections: moving beyond the microscope.The Journal of biological chemistry · 2011
    Review
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

13 authors at 1 institution in 1 country.

Yoshifumi MoritaSecond Department of Surgery, Hamamatsu University School of Medicine, Shizuoka, Japan.
Koji Ikegami
Naoko Goto-Inoue
Takahiro Hayasaka
Nobuhiro Zaima
Hiroki Tanaka
Takashi Uehara
Tomohiko Setoguchi
Takanori Sakaguchi
Hisashi Igarashi
Haruhiko Sugimura
Mitsutoshi Setou
Hiroyuki Konno
Hamamatsu University School of Medicine · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The popularity of imaging mass spectrometry (IMS) of tissue samples, which enables the direct scanning of tissue sections within a short time-period, has been considerably increasing in cancer proteomics. Most pathological specimens stored in medical institutes are formalin-fixed; thus, they had been regarded to be unsuitable for proteomic analyses, including IMS, until recently. Here, we report an easy-to-use screening method that enables the analysis of multiple samples in one experiment without extractions and purifications of proteins. We scanned, with an IMS technique, a tissue microarray (TMA) of formalin-fixed paraffin-embedded (FFPE) specimens. We detected a large amount of signals from trypsin-treated FFPE-TMA samples of gastric carcinoma tissues of different histological types. Of the signals detected, 54 were classified as signals specific to cancer with statistically significant differences between adenocarcinomas and normal tissues. We detected a total of 14 of the 54 signals as histological type-specific with the support of statistical analyses. Tandem MS revealed that a signal specific to poorly differentiated cancer tissue corresponded to histone H4. Finally, we verified the IMS-based finding by immunohistochemical analysis of more than 300 specimens spotted on TMAs; the immunoreactivity of histone H4 was remarkably strong in poorly differentiated cancer tissues. Thus, the application of IMS to FFPE-TMA can enable high-throughput analysis in cancer proteomics to aid in the understanding of molecular mechanisms underlying carcinogenesis, invasiveness, metastasis, and prognosis. Further, results obtained from the IMS of FFPE-TMA can be readily confirmed by commonly used immunohistochemical analyses.

Indexed as

FormaldehydeHistonesHumansImmunohistochemistryMass SpectrometryNeoplasm ProteinsParaffin EmbeddingProteomicsStomach NeoplasmsTissue Array AnalysisTissue FixationFormaldehydeHistonesNeoplasm Proteins

Identifiers

PMID19961487
PMCPMC11158157
OpenAlexW2007190470

What OpenQuestion holds

Textmetadata
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.