Evidence map›Paper›PMID 9223295›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion.

H Nakahara, L Howard, E W Thompson, H Sato, M Seiki, Y Yeh, W T Chen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed, 1 pooled it
–field-weighted citation impact, top 99% 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

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

  1. Pooled it
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  18. Invadopodia: clearing the way for cancer cell invasion.Annals of translational medicine · 2020
    Review
  19. Article
  20. Article

58 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

7 authors at 4 institutions in 2 countries.

H NakaharaLombardi Cancer Center and Department of Cell Biology, Georgetown University Medical Center, Washington, DC 20007, USA.
L Howard
E W Thompson
H Sato
M Seiki
Y Yeh
W T Chen
Cancer Research Institute · USGeorgetown University · USKanazawa University · JPGeorgetown University Medical Center · US

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI STEPHEN W BYERS · 1990 to 2026
$71.5M
MOLECULAR ULTRASTRUCTURE UNDERLYING CELL ADHESIONR01CA039077 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI CHEN, WEN-TIEN · 1985 to 2007
$1.6M
REGULATION OF TISSUE REPAIRR01HL033711 · NHLBI · STATE UNIVERSITY NEW YORK STONY BROOK · PI CHEN, WEN-TIEN · 1985 to 2002
$1.0M
NCI NIH HHS 2P30-CA-51008NCI NIH HHS P30 CA051008NCI NIH HHS R01 CA039077NCI NIH HHS R01 CA-39077NHLBI NIH HHS HL-33711NHLBI NIH HHS R01 HL033711
6 · The paper itself

Abstract

The invasion of human malignant melanoma cells into the extracellular matrix (ECM) involves the accumulation of proteases at sites of ECM degradation where activation of matrix metalloproteases (MMP) occurs. Here, we show that when membrane type 1 MMP (MT-MMP) was overexpressed in RPMI7951 human melanoma cells, the cells made contact with the ECM, activated soluble and ECM-bound MMP-2, and degraded and invaded the ECM. Further experiments demonstrated the importance of localization of the MT-MMP to invadopodia. Overexpression of MT-MMP without invadopodial localization caused activation of soluble MMP-2, but did not facilitate ECM degradation or cell invasiveness. Up-regulation of endogenous MT-MMP with concanavalin A caused activation of MMP-2. However, concanavalin A treatment prevented invadopodial localization of MT-MMP and ECM degradation. Neither a truncated MT-MMP mutant lacking transmembrane (TM) and cytoplasmic domains (DeltaTMMT-MMP), nor a chimeric MT-MMP containing the interleukin 2 receptor alpha chain (IL-2R) TM and cytoplasmic domains (DeltaTMMT-MMP/TMIL-2R) were localized to invadopodia or exhibited ECM degradation. Furthermore, a chimera of the TM/cytoplasmic domain of MT-MMP (TMMT-MMP) with tissue inhibitor of MMP 1 (TIMP-1/TMMT-MMP) directed the TIMP-1 molecule to invadopodia. Thus, the MT-MMP TM/cytoplasmic domain mediates the spatial organization of MT-MMP into invadopodia and subsequent degradation of the ECM.

Indexed as

Neoplasm InvasivenessAmino Acid SequenceCell MembraneCollagenasesExtracellular MatrixFibronectinsHumansMatrix Metalloproteinase 1MelanomaMolecular Sequence DataReceptors, Interleukin-2Substrate SpecificityTumor Cells, CulturedCollagenasesFibronectinsMatrix Metalloproteinase 1Receptors, Interleukin-2

Identifiers

PMID9223295
PMCPMC21537
OpenAlexW89180169

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.