Evidence map›Paper›PMID 22449415›Full record

ArticleExperimental cell research2012

MMP-2 expression by fibroblasts is suppressed by the myofibroblast phenotype.

Eric W Howard, Beverly J Crider, Dawn L Updike, Elizabeth C Bullen, Eileen E Parks, Carol J Haaksma, David M Sherry, James J Tomasek

Abstract read
In one paragraph

Article in Experimental cell research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.0field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 44 citations in OpenAlex.

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  15. The Actin-Binding Protein Drebrin Inhibits Neointimal Hyperplasia.Arteriosclerosis, thrombosis, and vascular biology · 2016
    Article
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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

8 authors at 1 institution in 1 country.

Eric W HowardDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. eric-howard@ouhsc.edu
Beverly J Crider
Dawn L Updike
Elizabeth C Bullen
Eileen E Parks
Carol J Haaksma
David M Sherry
James J Tomasek
University of Oklahoma Health Sciences Center · US

Funding

FIBROBLAST DIFFERENTIATION IN WOUND HEALINGR01GM060651 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI TOMASEK, JAMES J · 2000 to 2017
$3.4M
REGULATION OF CELL MIGRATION IN VASCULAR REMODELINGR01HL062268 · NHLBI · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI HOWARD, ERIC W · 1999 to 2002
$699k
NHLBI NIH HHS R01 HL062268NIGMS NIH HHS R01 GM060651
6 · The paper itself

Abstract

During wound healing, fibroblasts transition from quiescence to a migratory state, then to a contractile myofibroblast state associated with wound closure. We found that the myofibroblast phenotype, characterized by the expression of high levels of contractile proteins, suppresses the expression of the pro-migratory gene, MMP-2. Fibroblasts cultured in a 3-D collagen lattice and allowed to develop tension showed increased contractile protein expression and decreased MMP-2 levels in comparison to a stress-released lattice. In 2-D cultures, factors that promote fibroblast contractility, including serum or TGF-β, down-regulated MMP-2. Pharmacologically inducing F-actin disassembly or reduced contractility increased MMP-2 expression, while conditions that promote F-actin assembly suppressed MMP-2 expression. In all cases, changes in MMP-2 levels were inversely related to changes in the contractile marker, smooth muscle α-actin. To determine if the mechanisms involved in contractile protein gene expression play a direct role in MMP-2 regulation, we used RNAi-mediated knock-down of the myocardin-like factors, MRTF-A and MRTF-B, which induced the down-regulation of contractile protein genes by fibroblasts under both serum-containing and serum-free conditions. In the presence of serum or TGF-β, MRTF-A/B knock-down resulted in the up-regulation of MMP-2; serum-free conditions prevented this increased expression. Together, these results indicate that, while MMP-2 expression is suppressed by F-actin formation, its up-regulation is not simply a consequence of contractile protein down-regulation.

Indexed as

ActinsAnimalsCell Culture TechniquesCell LineCell MovementFibroblastsGene Expression Regulation, EnzymologicGene Knockdown TechniquesInsulin-Like Growth Factor IMatrix Metalloproteinase 2Models, BiologicalMyofibroblastsPhenotypeProtein MultimerizationRatsRNA InterferenceActa2 protein, ratActinsInsulin-Like Growth Factor IMatrix Metalloproteinase 2Mmp2 protein, ratmyocardin-related transcription factor-A, ratmyocardin-related transcription factor-B, ratTranscription Factors

Identifiers

PMID22449415
PMCPMC4164435
OpenAlexW1963798142

What OpenQuestion holds

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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.