Evidence map›Paper›PMID 12966436›Full record

ArticleBritish journal of cancer2003

TNF-alpha increases human melanoma cell invasion and migration in vitro: the role of proteolytic enzymes.

E Katerinaki, G S Evans, P C Lorigan, S MacNeil

Open access · hybridAbstract read
In one paragraph

Article in British journal of cancer, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

35 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
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  4. Development of a TNF-α-mediated Trojan Horse for bacteria-based cancer therapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
  5. Article
  6. Signal pathways of melanoma and targeted therapy.Signal transduction and targeted therapy · 2021
    Review
  7. Review
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  9. Review
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  13. C5aR1 regulates migration of suppressive myeloid cells required for costimulatory blockade-induced murine allograft survival.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2019
    Article
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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

4 authors at 3 institutions in 2 countries.

E KaterinakiSection of Medicine, Division of Clinical Sciences, Northern General Hospital, Herries Road, Sheffield S5 7AU, UK.
G S Evans
P C Lorigan
S MacNeil
Northern General Hospital · GBSheffield Children's Hospital · GBWeston Park Cancer Centre · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inflammatory mediators have been reported to promote malignant cell growth, invasion and metastatic potential. More specifically, we have recently reported that tumour necrosis factor alpha (TNF-alpha) increases melanoma cell attachment to extracellular matrix (ECM) substrates and invasion through fibronectin. In this study, we extend these investigations asking specifically whether the TNF-alpha effect on cell invasion and migration involves activation of proteolytic enzymes. We examined the effect of TNF-alpha on melanoma expression/activation of type IV gelatinases matrix metalloproteinases 2 and 9 (MMPs -2 and -9) and general proteolytic enzymes. Stimulation with TNF-alpha significantly increased both melanoma cell migration at 24 h (+21%) and invasion through fibronectin (+35%) but did not upregulate/activate the expression of latent MMP-2 constitutively produced by these cells and did not upregulate their general protease activity. However, the increased cell migration and invasion through fibronectin observed following stimulation with TNF-alpha were inhibited by the general protease inhibitor alpha(2) macroglobulin. These findings suggest that the promigratory and proinvasive effect of TNF-alpha on this melanoma cell line may be mediated to some extent by induction of localised cell membrane-bound degradative enzyme activity, which is not readily detected in biochemical assays.

Indexed as

alpha-MacroglobulinsAntineoplastic AgentsCell AdhesionCell MovementEnzyme ActivationFibronectinsHumansIn Vitro TechniquesLymphatic MetastasisMatrix Metalloproteinase 2Matrix Metalloproteinase 9MelanomaNeoplasm InvasivenessPeptide HydrolasesRecombinant ProteinsSkin Neoplasmsalpha-MacroglobulinsAntineoplastic AgentsFibronectinsMatrix Metalloproteinase 2Matrix Metalloproteinase 9Peptide HydrolasesRecombinant ProteinsTumor Necrosis Factor-alpha

Identifiers

PMID12966436
PMCPMC2376936
OpenAlexW2120817406

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.