Evidence map›Paper›PMID 24963846›Full record

ArticleNature communications2014

Diverse matrix metalloproteinase functions regulate cancer amoeboid migration.

Jose L Orgaz, Pahini Pandya, Rimple Dalmeida, Panagiotis Karagiannis, Berta Sanchez-Laorden, Amaya Viros, Jean Albrengues, Frank O Nestle, Anne J Ridley, Cedric Gaggioli and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

110 citing papers in PubMed, 191 citations in OpenAlex.

  1. Contrasting the dynamic changes of carotenoid accumulation in Rhodotorula mucilaginosa under Pb and Cd stress.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Amoeboid cancer cells at a glance.Journal of cell science · 2026
    Review
  7. Amoeboid-mesenchymal transition and the proteolytic control of cancer invasion plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Plasticity in leukocyte migration during haematopoiesis and inflammation.Journal of muscle research and cell motility · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024
    Review
  19. Article
  20. Article

50 more citing papers are in PubMed but not listed here.

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

13 authors at 3 institutions in 1 country.

Jose L OrgazTumour Plasticity Team, Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Pahini PandyaTumour Plasticity Team, Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Rimple Dalmeida *Tumour Plasticity Team, Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Panagiotis Karagiannis *NIHR Biomedical Research Centre at Guy's and St Thomas' Hospitals, Cutaneous Medicine and Immunotherapy Unit, St John's Institute of Dermatology, Division of Genetics and Molecular Medicine at Guy's Hospital, King's College London, London SE1 9RT, UK.
Berta Sanchez-Laorden *Molecular Oncology Group, Cancer Research UK Manchester Institute, The University of Manchester, Manchester M20 4BX, UK.
Amaya VirosMolecular Oncology Group, Cancer Research UK Manchester Institute, The University of Manchester, Manchester M20 4BX, UK.
Jean AlbrenguesINSERM, U1081, CNRS, UMR7284, Institute for Research on Cancer and Aging in Nice (IRCAN), Faculté de Médecine, University of Nice Sophia-Antipolis, 28 Avenue de Valombrose, F-06107 Nice, France.
Frank O NestleNIHR Biomedical Research Centre at Guy's and St Thomas' Hospitals, Cutaneous Medicine and Immunotherapy Unit, St John's Institute of Dermatology, Division of Genetics and Molecular Medicine at Guy's Hospital, King's College London, London SE1 9RT, UK.
Anne J RidleyCell Signalling in Invasion and Motility Team, Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
Cedric GaggioliINSERM, U1081, CNRS, UMR7284, Institute for Research on Cancer and Aging in Nice (IRCAN), Faculté de Médecine, University of Nice Sophia-Antipolis, 28 Avenue de Valombrose, F-06107 Nice, France.
Richard MaraisMolecular Oncology Group, Cancer Research UK Manchester Institute, The University of Manchester, Manchester M20 4BX, UK.
Sophia N KaragiannisNIHR Biomedical Research Centre at Guy's and St Thomas' Hospitals, Cutaneous Medicine and Immunotherapy Unit, St John's Institute of Dermatology, Division of Genetics and Molecular Medicine at Guy's Hospital, King's College London, London SE1 9RT, UK.
Victoria Sanz-MorenoTumour Plasticity Team, Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, UK.
King's College London · GBUniversity of Manchester · GBCancer Research UK Manchester Institute · GB

Funding

Cancer Research UK 12065Cancer Research UK 15961Cancer Research UK 17098Cancer Research UK 17240Cancer Research UK 19279Cancer Research UK A12065Cancer Research UK C1519/A10331Cancer Research UK C30122/A11527Cancer Research UK C6620/A15961Cancer Research UK CRUK C33043/A12065Medical Research Council MR/J006742/1
6 · The paper itself

Abstract

Rounded-amoeboid cancer cells use actomyosin contractility driven by Rho-ROCK and JAK-STAT3 to migrate efficiently. It has been suggested that rounded-amoeboid cancer cells do not require matrix metalloproteinases (MMPs) to invade. Here we compare MMP levels in rounded-amoeboid and elongated-mesenchymal melanoma cells. Surprisingly, we find that rounded-amoeboid melanoma cells secrete higher levels of several MMPs, including collagenase MMP-13 and gelatinase MMP-9. As a result, rounded-amoeboid melanoma cells degrade collagen I more efficiently than elongated-mesenchymal cells. Furthermore, using a non-catalytic mechanism, MMP-9 promotes rounded-amoeboid 3D migration through regulation of actomyosin contractility via CD44 receptor. MMP-9 is upregulated in a panel of rounded-amoeboid compared with elongated-mesenchymal melanoma cell lines and its levels are controlled by ROCK-JAK-STAT3 signalling. MMP-9 expression increases during melanoma progression and it is particularly prominent in the invasive fronts of lesions, correlating with cell roundness. Therefore, rounded-amoeboid cells use both catalytic and non-catalytic activities of MMPs for invasion.

Indexed as

Cell MovementActomyosinCell Line, TumorHumansJanus KinasesMatrix Metalloproteinase 13Matrix Metalloproteinase 9MelanomaNeoplasm Invasivenessrho-Associated KinasesSignal TransductionSTAT3 Transcription FactorActomyosinJanus KinasesMatrix Metalloproteinase 13Matrix Metalloproteinase 9rho-Associated KinasesSTAT3 Transcription Factor

Identifiers

PMID24963846
PMCPMC4118761
OpenAlexW2031004837

What OpenQuestion holds

Textmetadata
LicenceTDM
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.