Evidence map›Paper›PMID 11716072›Full record

ReviewJournal of neuro-oncology2001

The role of matrix metalloproteinase genes in glioma invasion: co-dependent and interactive proteolysis.

T E VanMeter, H K Rooprai, M M Kibble, H L Fillmore, W C Broaddus, G J Pilkington

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of neuro-oncology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 12% 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

52 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Tumor suppressive effect of low-frequency repetitive transcranial magnetic stimulation on glioblastoma progression.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Targeting RGS4 Ablates Glioblastoma Proliferation.International journal of molecular sciences · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Activation of NMDA receptor of glutamate influences MMP-2 activity and proliferation of glioma cells.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2014
    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

6 authors at 2 institutions in 2 countries.

T E VanMeterDepartment of Neuropathology, Institute of Psychiatry, King's College London, De Crespigny Park, London, UK.
H K Rooprai
M M Kibble
H L Fillmore
W C Broaddus
G J Pilkington
King's College London · GBVirginia Commonwealth University Medical Center · US

Funding

RADIOSENSITIZATION OF MALIGNANT GLIOMAS BY VIRAL TRANSDUCTION WITH WILD-TYPE P53P01CA072955 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI VALERIE, KRISTOFFER CARL · 1998 to 2007
$6.0M
NCI NIH HHS 1PO1 CA72955-01A1
6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) are cation-dependent endopeptidases which have been implicated in the malignancy of gliomas. It is thought that the MMPs play a critical role in both metastasis and angiogenesis, and that interference with proteases might therefore deter local tumor dissemination and neovascularization. However, the attempt to control tumor-associated proteolysis will rely on better definition of the normal tissue function of MMPs, an area of study still in its infancy in the central nervous system (CNS). Understanding the role of MMP-mediated proteolysis in the brain relies heavily on advances in other areas of molecular neuroscience, most notably an understanding of extracellular matrix (ECM) composition and the function of cell adhesion molecules such as integrins, which communicate knowledge of ECM composition intracellularly. Recently, protease expression and function has been shown to be strongly influenced by the functional state and signaling properties of integrins. Here we review MMP function and expression in gliomas and present examples of MMP profiling studies in glioma tissues and cell lines by RT-PCR and Western blotting. Co-expression of MMPs and certain integrins substantiates the gathering evidence of a functional intersection between the two, and inhibition studies using recombinant TIMP-1 and integrin antisera demonstrate significant inhibition of glioma invasion in vitro. Use of promising new therapeutic compounds with anti-MMP and anti-invasion effects are discussed. These data underline the importance of functional interaction of MMPs with accessory proteins such as integrins during invasion, and the need for further studies to elucidate the molecular underpinnings of this process.

Indexed as

AnimalsAntineoplastic AgentsBrain NeoplasmsCell MembraneCell Surface ExtensionsCytoskeletonDisease ProgressionDrug DesignEnzyme InductionExtracellular Matrix ProteinsGene Expression Regulation, NeoplasticGliomaHumansImmune SeraIntegrinsMembrane ProteinsAntineoplastic AgentsExtracellular Matrix ProteinsImmune SeraIntegrinsMembrane ProteinsMetalloendopeptidasesNeoplasm ProteinsReceptors, Growth FactorRNA, MessengerRNA, NeoplasmTissue Inhibitor of Metalloproteinase-1Tissue Inhibitor of Metalloproteinase-2Urokinase-Type Plasminogen Activator

Identifiers

PMID11716072
OpenAlexW1866664159

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.