Evidence map›Paper›PMID 29975508›Full record

ArticleAnalytical chemistry2018

Digestion-Free Analysis of Peptides from 30-year-old Formalin-Fixed, Paraffin-Embedded Tissue by Mass Spectrometry Imaging.

Martin R L Paine, Shane R Ellis, Dan Maloney, Ron M A Heeren, Peter D E M Verhaert

Abstract read
In one paragraph

Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Mass Spectrometry Imaging.Analytical chemistry · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. ADAMDEC1 accelerates GBM progressionFrontiers in oncology · 2022
    Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

5 authors.

Martin R L PaineMaastricht MultiModal Molecular Imaging (M4I) Institute, Division of Imaging Mass Spectrometry , Maastricht University , Universiteitssingel 50 , 6229ER Maastricht , The Netherlands.ORCID 0000-0002-9360-1969
Shane R EllisMaastricht MultiModal Molecular Imaging (M4I) Institute, Division of Imaging Mass Spectrometry , Maastricht University , Universiteitssingel 50 , 6229ER Maastricht , The Netherlands.
Dan MaloneyBioinformatics Solutions Inc. , 470 Weber Street North , Waterloo , Ontario N2L 6J2 , Canada.
Ron M A HeerenMaastricht MultiModal Molecular Imaging (M4I) Institute, Division of Imaging Mass Spectrometry , Maastricht University , Universiteitssingel 50 , 6229ER Maastricht , The Netherlands.ORCID 0000-0002-6533-7179
Peter D E M VerhaertMaastricht MultiModal Molecular Imaging (M4I) Institute, Division of Imaging Mass Spectrometry , Maastricht University , Universiteitssingel 50 , 6229ER Maastricht , The Netherlands.ORCID 0000-0002-6921-087X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Formalin-fixed neuroendocrine tissues from American cockroaches ( Periplaneta americana) embedded in paraffin more than 30 years ago were recently analyzed by matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI), to reveal the histological localization of more than 20 peptide ions. These represented protonated, and other cationic species of, at least, 14 known neuropeptides. The characterization of peptides in such historical samples was made possible by a novel sample preparation protocol rendering the endogenous peptides readily amenable to MSI analysis. The protocol comprises brief deparaffinization steps involving xylene and ethanol, and is further devoid of conventional aqueous washing, buffer incubations, or antigen retrieval steps. Endogenous secretory peptides that are typically highly soluble are therefore retained in-tissue with this protocol. The method is fully "top-down", that is, without laborious in situ enzymatic digestion that typically disturbs the detection of low-abundance endogenous peptides by MSI. Peptide identifications were supported by accurate mass, on-tissue tandem MS analyses, and by earlier MALDI-MSI results reported for freshly prepared P. americana samples. In contrast to earlier literature accounts stating that MALDI-MSI detection of endogenous peptides is possible only in fresh or freshly frozen tissues, or exceptionally, in formalin-fixed, paraffin-embedded (FFPE) material of less than 1 year old, we demonstrate that MALDI-MSI works for endogenous peptides in FFPE tissue of up to 30 years old. Our findings put forward a useful method for digestion-free, high-throughput analysis of endogenous peptides from FFPE samples and offer the potential for reinvestigating archived and historically interesting FFPE material, such as those stored in hospital biobanks.

Indexed as

Paraffin EmbeddingAnimalsCockroachesFormaldehydeMass SpectrometryPeptidesTissue FixationFormaldehydePeptides

Identifiers

PMID29975508
PMCPMC6150647

What Socratic 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 Socratic graph.