Evidence map›Paper›PMID 31882975›Full record

ArticleScientific reports2019

Matrisome-Associated Gene Expression Patterns Correlating with TIMP2 in Cancer.

David Peeney, Yu Fan, Trinh Nguyen, Daoud Meerzaman, William G Stetler-Stevenson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. The TIMP protein family: diverse roles in pathophysiology.American journal of physiology. Cell physiology · 2024
    Review
  6. bioRxiv : the preprint server for biology · 2023
    Article
  7. Tissue inhibitors of metalloproteinases are proteolytic targets of matrix metalloproteinase 9.Matrix biology : journal of the International Society for Matrix Biology · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. A functional outside-in signaling network of proteoglycans and matrix molecules regulating autophagy.Matrix biology : journal of the International Society for Matrix Biology · 2021
    Article
  19. Article
  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

5 authors at 1 institution in 1 country.

David PeeneyExtracellular Matrix Pathology Section, Laboratory of Pathology, National Cancer Institute, National Institute of Health, Bethesda, Maryland, USA. david.peeney@nih.gov.
Yu FanComputational Genomics and Bioinformatics Group, Center for Biomedical Informatics & Information Technology, National Cancer Institute, National Institute of Health, Rockville, Maryland, USA.
Trinh NguyenComputational Genomics and Bioinformatics Group, Center for Biomedical Informatics & Information Technology, National Cancer Institute, National Institute of Health, Rockville, Maryland, USA.ORCID http://orcid.org/0000-0002-6606-6948
Daoud MeerzamanComputational Genomics and Bioinformatics Group, Center for Biomedical Informatics & Information Technology, National Cancer Institute, National Institute of Health, Rockville, Maryland, USA.
William G Stetler-StevensonExtracellular Matrix Pathology Section, Laboratory of Pathology, National Cancer Institute, National Institute of Health, Bethesda, Maryland, USA.ORCID http://orcid.org/0000-0002-5500-5808
National Cancer Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Remodeling of the extracellular matrix (ECM) to facilitate invasion and metastasis is a universal hallmark of cancer progression. However, a definitive therapeutic target remains to be identified in this tissue compartment. As major modulators of ECM structure and function, matrix metalloproteinases (MMPs) are highly expressed in cancer and have been shown to support tumor progression. MMP enzymatic activity is inhibited by the tissue inhibitor of metalloproteinase (TIMP1-4) family of proteins, suggesting that TIMPs may possess anti-tumor activity. TIMP2 is a promiscuous MMP inhibitor that is ubiquitously expressed in normal tissues. In this study, we address inconsistencies in the literature regarding the role of TIMP2 in tumor progression by analyzing co-expressed genes in tumor vs. normal tissue. Utilizing data from The Cancer Genome Atlas and Genotype-Tissue expression studies, focusing on breast and lung carcinomas, we analyzed the correlation between TIMP2 expression and the transcriptome to identify a list of genes whose expression is highly correlated with TIMP2 in tumor tissues. Bioinformatic analysis of the identified gene list highlights a core of matrix and matrix-associated genes that are of interest as potential modulators of TIMP2 function, thus ECM structure, identifying potential tumor microenvironment biomarkers and/or therapeutic targets for further study.

Indexed as

Gene Expression Regulation, NeoplasticComputational BiologyGene Expression ProfilingHumansMatrix MetalloproteinasesNeoplasmsPhylogenyTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of MetalloproteinasesTranscriptomeMatrix MetalloproteinasesTIMP2 protein, humanTissue Inhibitor of Metalloproteinase-2Tissue Inhibitor of Metalloproteinases

Identifiers

PMID31882975
PMCPMC6934702
OpenAlexW2997795468

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.