Evidence map›Paper›PMID 21849669›Full record

ArticleAmerican journal of physiology. Cell physiology2011

Role of RhoA and its effectors ROCK and mDia1 in the modulation of deformation-induced FAK, ERK, p38, and MLC motogenic signals in human Caco-2 intestinal epithelial cells.

Lakshmi S Chaturvedi, Harold M Marsh, Marc D Basson

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

32 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
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  6. Review
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  11. Review
  12. Impact of Epithelial Cell Shedding on Intestinal Homeostasis.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Article
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  18. Article
  19. Recent Advances in Studies of Molecular Hydrogen against Sepsis.International journal of biological sciences · 2019
    Review
  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

3 authors at 2 institutions in 1 country.

Lakshmi S ChaturvediDepartment of Surgery, Michigan State University, Lansing, MI 48912, USA.
Harold M Marsh
Marc D Basson
John D. Dingell VA Medical Center · USWayne State University · US

Funding

Regulation of FAK protein in mucosal healingR01DK067257 · NIDDK · WAYNE STATE UNIVERSITY · PI BASSON, MARC D. · 2005 to 2009
$1.2M
NIDDK NIH HHS R01 DK-067257
6 · The paper itself

Abstract

Repetitive deformation enhances intestinal epithelial migration across tissue fibronectin. We evaluated the contribution of RhoA and its effectors Rho-associated kinase (ROK/ROCK) and mammalian diaphanous formins (mDia1) to deformation-induced intestinal epithelial motility across fibronectin and the responsible focal adhesion kinase (FAK), extracellular signal-regulated kinase (ERK), p38, and myosin light chain (MLC) signaling. We reduced RhoA, ROCK1, ROCK2, and mDia1 by smart-pool double-stranded short-interfering RNAs (siRNA) and pharmacologically inhibited RhoA, ROCK, and FAK in human Caco-2 intestinal epithelial monolayers on fibronectin-coated membranes subjected to 10% repetitive deformation at 10 cycles/min. Migration was measured by wound closure. Stimulation of migration by deformation was prevented by exoenzyme C3, Y27632, or selective RhoA, ROCK1, and ROCK2 or mDia1 siRNAs. RhoA, ROCK inhibition, or RhoA, ROCK1, ROCK2, mDia1, and FAK reduction by siRNA blocked deformation-induced nuclear ERK phosphorylation without preventing ERK phosphorylation in the cytoplasmic protein fraction. Furthermore, RhoA, ROCK inhibition or RhoA, ROCK1, ROCK2, and mDia1 reduction by siRNA also blocked strain-induced FAK-Tyr(925), p38, and MLC phosphorylation. These results suggest that RhoA, ROCK, mDia1, FAK, ERK, p38, and MLC all mediate the stimulation of intestinal epithelial migration by repetitive deformation. This pathway may be an important target for interventions to promote mechanotransduced mucosal healing during inflammation.

Indexed as

MAP Kinase Signaling SystemAdaptor Proteins, Signal TransducingADP Ribose TransferasesAmidesBotulinum ToxinsCaco-2 CellsCell MovementEnzyme InhibitorsExtracellular Signal-Regulated MAP KinasesFibronectinsFocal Adhesion Protein-Tyrosine KinasesForminsHumansMechanotransduction, CellularMyosin Light ChainsPyridinesAdaptor Proteins, Signal TransducingADP Ribose TransferasesAmidesBotulinum ToxinsDIAPH1 protein, humanEnzyme Inhibitorsexoenzyme C3, Clostridium botulinumExtracellular Signal-Regulated MAP KinasesFibronectinsFocal Adhesion Protein-Tyrosine KinasesForminsMyosin Light ChainsPyridinesrhoA GTP-Binding ProteinRHOA protein, humanrho-Associated KinasesRNA, Small InterferingROCK1 protein, humanROCK2 protein, humanY 27632

Identifiers

PMID21849669
PMCPMC3213924
OpenAlexW2168186943

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.