Evidence map›Paper›PMID 16877348›Full record

ArticleThe American journal of pathology2006

Mechanotransduction of extracellular signal-regulated kinases 1 and 2 mitogen-activated protein kinase activity in smooth muscle is dependent on the extracellular matrix and regulated by matrix metalloproteinases.

Karen J Aitken, Gregory Block, Armando Lorenzo, Daniel Herz, Nesrin Sabha, Omar Dessouki, France Fung, Marta Szybowska, Laura Craig, Darius J Bägli

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 52 citations in OpenAlex.

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  14. Advances in biomimetic regeneration of elastic matrix structures.Drug delivery and translational research · 2012
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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

10 authors at 3 institutions in 1 country.

Karen J AitkenResearch Institute and Division of Urology, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada.
Gregory Block
Armando Lorenzo
Daniel Herz
Nesrin Sabha
Omar Dessouki
France Fung
Marta Szybowska
Laura Craig
Darius J Bägli
University of Toronto · CAHospital for Sick Children · CASickKids Foundation · CA

Funding

Urethral Tissue BioengineeringP50DK065298 · NIDDK · CHILDREN'S HOSPITAL BOSTON · PI ADAM, ROSALYN M · 2003 to 2012
$9.8M
NIDDK NIH HHS P50 DK065298NIDDK NIH HHS P50DK065298-01
6 · The paper itself

Abstract

Excessive wall stretch of distensible hollow organs in cardiovascular and urinary systems can activate matrix metalloproteinases (MMPs), thereby releasing matrix neoepitopes and growth factor ligands, leading to ERK1/2 activation. However, the role of MMPs in mechanotransduction of ERK1/2 signaling in the bladder is unknown. We examined bladders undergoing sustained distension over time, which provides a novel platform for smooth muscle mechanotransduction studies. Bladder distension ex vivo caused increased proliferation and MMP activity. Conditioned medium from distended compared with undistended bladders induced proliferation in bladder smooth muscle cells (BSMCs). When conditioned medium from distended bladders was used to proteolyze collagen type I matrices, matrices augmented BSMC proliferation, which was inhibited if bladders were distended in presence of broad-spectrum MMP inhibitors. Distension of ex vivo bladders also induced ERK1/2 phosphorylation in situ, which was dependent on MMP activity in the intact bladder. Similarly, stretching BSMCs in vitro induced increases in ERK1/2 activation and ERK1/2-dependent proliferation under discrete mechanical conditions, and distension conditioned medium itself induced MMP-dependent ERK1/2 activation in BSMCs. Overall, stretch-induced proliferation and ERK1/2 signaling in bladder tissue and BSMCs likely depend on secreted MMP activity. Identification of intermediaries between MMPs and ERK1/2 may elaborate novel mechanisms underlying mechanotransduction in bladder smooth muscle.

Indexed as

Mechanotransduction, CellularAnimalsCell ProliferationCells, CulturedCulture Media, ConditionedExtracellular MatrixFemaleGelatinasesGrowth SubstancesIn Vitro TechniquesMatrix MetalloproteinasesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Models, BiologicalMyocytes, Smooth MuscleRatsCulture Media, ConditionedGelatinasesGrowth SubstancesMatrix MetalloproteinasesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3

Identifiers

PMID16877348
PMCPMC1698787
OpenAlexW1988102087

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.