Evidence map›Paper›PMID 21840960›Full record

ArticleAmerican journal of physiology. Lung cellular and molecular physiology2011

Pulmonary fibroblasts mobilize the membrane-tethered matrix metalloprotease, MT1-MMP, to destructively remodel and invade interstitial type I collagen barriers.

R Grant Rowe, Daniel Keena, Farideh Sabeh, Amanda L Willis, Stephen J Weiss

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Lung cellular and molecular physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Mechanobiology and Resolution of Lung Fibrosis.Annual review of physiology · 2026
    Review
  2. Article
  3. Invadosome Formation by Lung Fibroblasts in Idiopathic Pulmonary Fibrosis.International journal of molecular sciences · 2022
    Article
  4. Review
  5. Article
  6. Matrix biomechanics and dynamics in pulmonary fibrosis.Matrix biology : journal of the International Society for Matrix Biology · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Matrix metalloproteinases as therapeutic targets for idiopathic pulmonary fibrosis.American journal of respiratory cell and molecular biology · 2015
    Review
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

R Grant RoweDivisions of Molecular Medicine & Genetics, Department of Internal Medicine, University of Michigan, Ann Arbor, Michigan 48109-2216, USA.
Daniel Keena
Farideh Sabeh
Amanda L Willis
Stephen J Weiss
University of Michigan–Ann Arbor · US

Funding

PUBLIC HEALTH DEMONSTRATIONP60DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1985 to 2012
$26.5M
FUNCTION OF THE MEMBRANE TYPE MATRIX METALLOPROTEINASER01CA071699 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEISS, STEPHEN J · 1997 to 2024
$7.3M
NCI NIH HHS CA71699NIDDK NIH HHS P60 DK020572
6 · The paper itself

Abstract

In acute and chronic lung disease, widespread disruption of tissue architecture underlies compromised pulmonary function. Pulmonary fibroblasts have been implicated as critical effectors of tissue-destructive extracellular matrix (ECM) remodeling by mobilizing a spectrum of proteolytic enzymes. Although efforts to date have focused on the catabolism of type I collagen, the predominant component of the lung interstitial matrix, the key collagenolytic enzymes employed by pulmonary fibroblasts remain unidentified. Herein, membrane type-1 matrix metalloprotease (MT1-MMP) is identified as the dominant and direct-acting protease responsible for the type I collagenolytic activity mediated by both mouse and human pulmonary fibroblasts. Furthermore, MT1-MMP is shown to be essential for pulmonary fibroblast migration within three-dimensional (3-D) hydrogels of cross-linked type I collagen that recapitulate ECM barriers encountered in the in vivo environment. Together, these findings demonstrate that MT1-MMP serves as a key effector of type I collagenolytic activity in pulmonary fibroblasts and earmark this pericellular collagenase as a potential target for therapeutic intervention.

Indexed as

FibroblastsAirway RemodelingAnimalsAsthmaCell MovementChronic DiseaseCollagen Type IExtracellular MatrixGene SilencingHumansHydrogelsLungMatrix Metalloproteinase 1Matrix Metalloproteinase 14MiceMice, KnockoutCollagen Type IHydrogelsMatrix Metalloproteinase 1Matrix Metalloproteinase 14MMP14 protein, humanMmp14 protein, mouseMmp1a protein, mouseRNA, Small Interfering

Identifiers

PMID21840960
PMCPMC3213981
OpenAlexW1985013552

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.