Evidence map›Paper›PMID 30467633›Full record

ArticleJournal of cancer research and clinical oncology2019

Non-invasive profiling of protease-specific elastin turnover in lung cancer: biomarker potential.

Jeppe Thorlacius-Ussing, Stephanie Nina Kehlet, Sarah Rank Rønnow, Morten Asser Karsdal, Nicholas Willumsen

Open access · greenAbstract read
In one paragraph

Article in Journal of cancer research and clinical oncology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.6field-weighted citation impact, top 39% 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

17 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Trends in extracellular matrix biology.Molecular biology reports · 2023
    Review
  10. Article
  11. Review
  12. Effects ofExperimental and therapeutic medicine · 2021
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

Jeppe Thorlacius-UssingBiomarkers & Research, Nordic Bioscience, Herlev Hovedgade 205-207, 2730, Herlev, Denmark.ORCID http://orcid.org/0000-0002-3340-0786
Stephanie Nina KehletBiomarkers & Research, Nordic Bioscience, Herlev Hovedgade 205-207, 2730, Herlev, Denmark.
Sarah Rank RønnowBiomarkers & Research, Nordic Bioscience, Herlev Hovedgade 205-207, 2730, Herlev, Denmark.
Morten Asser KarsdalBiomarkers & Research, Nordic Bioscience, Herlev Hovedgade 205-207, 2730, Herlev, Denmark.
Nicholas WillumsenBiomarkers & Research, Nordic Bioscience, Herlev Hovedgade 205-207, 2730, Herlev, Denmark. nwi@nordicbio.com.ORCID http://orcid.org/0000-0002-5207-5173
Nordic Bioscience (Denmark) · DKUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeElastin is a signature protein of lungs. Increased elastin turnover driven by altered proteolytic activity is an important part of lung tumorigenesis. Elastin-derived fragments have been shown to be pro-tumorigenic, however, little is known regarding the biomarker potential of such elastin fragments. Here, we present an elastin turnover profile by non-invasively quantifying five specific elastin degradation fragments generated by different proteases.

methodsElastin fragments were assessed in serum from patients with stage I-IV non-small cell lung cancer (NSCLC) (n = 40) and healthy controls (n = 30) using competitive ELISAs targeting different protease-generated fragments of elastin: ELM12 (generated by matrix metalloproteinase MMP-9 and -12), ELM7 (MMP-7), EL-NE (neutrophil elastase), EL-CG (cathepsin G) and ELP-3 (proteinase 3).

resultsELM12, ELM7, EL-NE and EL-CG were all significantly elevated in NSCLC patients (n = 40) when compared to healthy controls (n = 30) (ELM12, p = 0.0191; ELM7, p < 0.0001; EL-NE, p < 0.0001; EL-CG, p < 0.0001). ELP-3 showed no significant difference between patients and controls (p = 0.8735). All fragments correlated positively (Spearman, r: 0.69-0.81) when compared pairwise, except ELM12 (Spearman, r: 0.042-0.097). In general, all fragments were detectable across all stages of the disease.

conclusionsElastin fragments generated by different proteases are elevated in lung cancer patients compared to healthy controls but differ in their presence. This demonstrates non-invasive biomarker potential of elastin fragments in serum from lung cancer patients and suggests that different pathological mechanisms may be responsible for the elastin turnover, warranting further validation in clinical trials.

Indexed as

Biomarkers, TumorCarcinoma, Non-Small-Cell LungCase-Control StudiesElastinFemaleFollow-Up StudiesHumansLungLung NeoplasmsMaleMiddle AgedPrognosisBiomarkers, TumorElastinBiomarkerCathepsin gECMElastinLung cancerMMPNeutrophil elastaseNSCLCProteinase 3Serum

Identifiers

PMID30467633
PMCPMC11810429
OpenAlexW2900882420

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.