Evidence map›Paper›PMID 23705892›Full record

ArticleJournal of proteome research2013

Mapping proteolytic processing in the secretome of gastric cancer-associated myofibroblasts reveals activation of MMP-1, MMP-2, and MMP-3.

Christopher Holmberg, Bart Ghesquière, Francis Impens, Kris Gevaert, J Dinesh Kumar, Nicole Cash, Sandhir Kandola, Peter Hegyi, Timothy C Wang, Graham J Dockray and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Proteolytic Landscapes in Gastric Pathology and Cancerogenesis.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. A Network Pharmacology Analysis of the Active Components of the Traditional Chinese Medicine Zuojinwan in Patients with Gastric Cancer.Medical science monitor : international medical journal of experimental and clinical research · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. PeerJ · 2018
    Article
  18. Review
  19. Review
  20. 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

11 authors at 4 institutions in 4 countries.

Christopher HolmbergInstitute of Translational Medicine, University of Liverpool, Liverpool, UK.
Bart Ghesquière
Francis Impens
Kris Gevaert
J Dinesh Kumar
Nicole Cash
Sandhir Kandola
Peter Hegyi
Timothy C Wang
Graham J Dockray
Andrea Varro
University of Liverpool · GBGhent University · BEColumbia University Irving Medical Center · USUniversity of Szeged · HU

Funding

The Role of Inflammation and Stroma in Digestive CancerU54CA126513 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI TYCKO, BENJAMIN · 2006 to 2010
$5.1M
NCI NIH HHS 5U54CA126513NCI NIH HHS U54 CA126513Wellcome Trust
6 · The paper itself

Abstract

Cancer progression involves changes in extracellular proteolysis, but the contribution of stromal cell secretomes to the cancer degradome remains uncertain. We have now defined the secretome of a specific stromal cell type, the myofibroblast, in gastric cancer and its modification by proteolysis. SILAC labeling and COFRADIC isolation of methionine containing peptides allowed us to quantify differences in gastric cancer-derived myofibroblasts compared with myofibroblasts from adjacent tissue, revealing increased abundance of several proteases in cancer myofibroblasts including matrix metalloproteinases (MMP)-1 and -3. Moreover, N-terminal COFRADIC analysis identified cancer-restricted proteolytic cleavages, including liberation of the active forms of MMP-1, -2, and -3 from their inactive precursors. In vivo imaging confirmed increased MMP activity when gastric cancer cells were xenografted in mice together with gastric cancer myofibroblasts. Western blot and enzyme activity assays confirmed increased MMP-1, -2, and -3 activity in cancer myofibroblasts, and cancer cell migration assays indicated stimulation by MMP-1, -2, and -3 in cancer-associated myofibroblast media. Thus, cancer-derived myofibroblasts differ from their normal counterparts by increased production and activation of MMP-1, -2, and -3, and this may contribute to the remodelling of the cancer cell microenvironment.

Indexed as

AnimalsCell ProliferationGene Expression Regulation, NeoplasticHumansMatrix Metalloproteinase 1Matrix Metalloproteinase 2Matrix Metalloproteinase 3MiceMyofibroblastsProteolysisStomach NeoplasmsTumor MicroenvironmentXenograft Model Antitumor AssaysMatrix Metalloproteinase 1Matrix Metalloproteinase 2Matrix Metalloproteinase 3

Identifiers

PMID23705892
PMCPMC3709265
OpenAlexW2151552433

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.