Evidence map›Paper›PMID 15967115›Full record

ArticleNeoplasia (New York, N.Y.)2005

Membrane type 1 matrix metalloprotease cleaves laminin-10 and promotes prostate cancer cell migration.

Elisabeth L Bair, Man Ling Chen, Kathy McDaniel, Kiyotoshi Sekiguchi, Anne E Cress, Raymond B Nagle, George Timothy Bowden

Open access · goldAbstract read
In one paragraph

Article in Neoplasia (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
2.4field-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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.

  1. Pooled it
  2. Review
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  4. Article
  5. Review
  6. Article
  7. Review
  8. Matrix-metalloproteinases as targets for controlled delivery in cancer: An analysis of upregulation and expression.Journal of controlled release : official journal of the Controlled Release Society · 2017
    Review
  9. Article
  10. Article
  11. Review
  12. Article
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  19. Article
  20. Basement membranes: cell scaffoldings and signaling platforms.Cold Spring Harbor perspectives in biology · 2011
    Review
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 2 institutions in 2 countries.

Elisabeth L BairCancer Biology Graduate Interdisciplinary Program, Arizona Cancer Center, University of Arizona, Tucson, AZ 85724, USA.
Man Ling Chen
Kathy McDaniel
Kiyotoshi Sekiguchi
Anne E Cress
Raymond B Nagle
George Timothy Bowden
University of Arizona · USProtein Research Foundation · JP

Funding

VITAMIN AP30CA023074 · NCI · UNIVERSITY OF ARIZONA · PI Dan Theodorescu · 1985 to 2026
$110.2M
SOUTHWEST ENVIRONMENTAL HEALTH SCIENCES CENTERP30ES006694 · NIEHS · UNIVERSITY OF ARIZONA · PI DEAN BILLHEIMER · 1994 to 2026
$36.7M
Integrative Cancer Scholars Training GrantT32CA009213 · NCI · UNIVERSITY OF ARIZONA · PI CAREW, JENNIFER S, CURIEL-LEWANDROWSKI, CLARA · 1985 to 2024
$8.6M
ROLE OF METALLOPROTEINASES AND TIMP IN HUMAN PROSTATE CELL INVASIONP01CA056666 · NCI · UNIVERSITY OF ARIZONA · PI HEIMARK, RONALD L. · 1993 to 2008
$6.3M
NCI NIH HHS CA23074NCI NIH HHS CA56666NCI NIH HHS P01 CA056666NCI NIH HHS P30 CA023074NCI NIH HHS T32 CA009213NCI NIH HHS T32-CA09213NIEHS NIH HHS ES06694NIEHS NIH HHS P30 ES006694
6 · The paper itself

Abstract

Disruption of the extracellular matrix by proteases is crucial for tumor invasion. Laminin-10 (Ln-10) has previously been identified as a substrate for cell migration and cell adhesion, and is present in the basal lamina (BL) of both normal prostate and prostate cancer. Here, we investigate a role for membrane type 1 matrix metalloprotease (MT1-MMP) in modifying this Ln-10-rich BL. MT1-MMP is a transmembrane member of the MMP family that has been demonstrated to be upregulated as prostate cancer progresses from normal to prostate intraepithelial neoplasia to invasive cancer, suggesting a role for MT1-MMP in the invasion of prostate cancer. We show that MT1-MMP cleaves the alpha5 chain of purified human Ln-10 from its 350-kDa form into 310-, 190-, 160-, and 45-kDa fragments. This cleavage causes a decrease in DU-145 prostate cancer cell adhesion to purified Ln-10, and an increase in transmigration of DU-145 cells through cleaved Ln-10. We also show that prostate cancer cells expressing membrane-bound MT1-MMP cleave the alpha5 chain of Ln-10. Ln alpha5-chain cleavage is also observed in human prostate cancer tissues. These findings suggest that prostate cancer cells expressing high levels of MT1-MMP have increased invasive potential through their ability to degrade and invade Ln-10 barriers.

Indexed as

Cell AdhesionCell Line, TumorCell MembraneCell MovementCulture Media, ConditionedCulture Media, Serum-FreeHumansImmunohistochemistryLamininMaleMass SpectrometryMatrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidasesModels, BiologicalModels, GeneticNeoplasm InvasivenessCulture Media, ConditionedCulture Media, Serum-FreeLamininlaminin 10Matrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidases

Identifiers

PMID15967115
PMCPMC1501144
OpenAlexW2094923489

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.