Evidence map›Paper›PMID 22573325›Full record

ArticleThe Journal of biological chemistry2012

Matrix metalloprotease-1a promotes tumorigenesis and metastasis.

Caitlin J Foley, Chi Luo, Katie O'Callaghan, Philip W Hinds, Lidija Covic, Athan Kuliopulos

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 2 pooled it
2.5field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 2 syntheses or guidelines pooled it, 60 citations in OpenAlex.

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  18. Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
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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 1 country.

Caitlin J FoleyMolecular Oncology Research Institute, Tufts Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
Chi Luo
Katie O'Callaghan
Philip W Hinds
Lidija Covic
Athan Kuliopulos
Molecular Oncology (United States) · USTufts Medical Center · US

Funding

THROMBIN RECEPTOR-G PROTEIN SIGNALING MECHANISMSR01HL064701 · NHLBI · TUFTS MEDICAL CENTER · PI KULIOPULOS, ATHAN · 2001 to 2011
$3.8M
Protease Activated Receptors in Cancer InvasionR01CA104406 · NCI · TUFTS MEDICAL CENTER · PI COVIC, LIDIJA · 2005 to 2009
$1.6M
Regulation and function of cdk5 and ezrin in senescenceR01CA104322 · NCI · TUFTS MEDICAL CENTER · PI HINDS, PHILIP W. · 2006 to 2010
$1.5M
Genetics of RAS, PTEN, BRAF and CDKN2A in MelanomaR01CA095798 · NCI · TUFTS MEDICAL CENTER · PI HINDS, PHILIP W. · 2005 to 2009
$1.4M
Inter-Cellular Signaling of Invastion Receptors in the Tumor MicroenvironmentR01CA122992 · NCI · TUFTS MEDICAL CENTER · PI KULIOPULOS, ATHAN · 2007 to 2010
$1.2M
MMP1-PAR1 Signaling in Vascular Integrity During SepsisF30HL104835 · NHLBI · TUFTS UNIVERSITY BOSTON · PI FOLEY, CAITLIN J · 2010 to 2013
$165k
NCI NIH HHS CA095798NCI NIH HHS CA104322NCI NIH HHS CA104406NCI NIH HHS CA122992NCI NIH HHS R01 CA095798NCI NIH HHS R01 CA104322NCI NIH HHS R01 CA104406NCI NIH HHS R01 CA122992NHLBI NIH HHS F30 HL104835NHLBI NIH HHS F30-HL104835NHLBI NIH HHS HL64701NHLBI NIH HHS R01 HL064701
6 · The paper itself

Abstract

Matrix metalloprotease-1 (MMP1), a collagenase and activator of the G protein-coupled protease activated receptor-1 (PAR1), is an emerging new target implicated in oncogenesis and metastasis in diverse cancers. However, the functional mouse homologue of MMP1 in cancer models has not yet been clearly defined. We report here that Mmp1a is a functional MMP1 homologue that promotes invasion and metastatic progression of mouse lung cancer and melanoma. LLC1 (Lewis lung carcinoma) and primary mouse melanoma cells harboring active BRAF express high levels of endogenous Mmp1a, which is required for invasion through collagen. Silencing of either Mmp1a or PAR1 suppressed invasive stellate growth of lung cancer cells in three-dimensional matrices. Conversely, ectopic expression of Mmp1a conferred an invasive phenotype in epithelial cells that do not express endogenous Mmp1a. Consistent with Mmp1a acting as a PAR1 agonist in an autocrine loop, inhibition or silencing of PAR1 resulted in a loss of the Mmp1a-driven invasive phenotype. Knockdown of Mmp1a on tumor cells resulted in significantly decreased tumorigenesis, invasion, and metastasis in xenograft models. Together, these data demonstrate that cancer cell-derived Mmp1a acts as a robust functional homologue of MMP1 by conferring protumorigenic and metastatic behavior to cells.

Indexed as

AnimalsCell LineCell Line, TumorFemaleHumansLung NeoplasmsMaleMatrix Metalloproteinase 1MelanomaMiceMice, Inbred C57BLMice, TransgenicReal-Time Polymerase Chain ReactionReceptor, PAR-1Xenograft Model Antitumor AssaysMatrix Metalloproteinase 1Receptor, PAR-1

Identifiers

PMID22573325
PMCPMC3397859
OpenAlexW2094585278

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.