Evidence map›Paper›PMID 20479130›Full record

ReviewCardiovascular research2010

Myosin light chain kinase in microvascular endothelial barrier function.

Qiang Shen, Robert R Rigor, Christopher D Pivetti, Mack H Wu, Sarah Y Yuan

Open access · bronzeAbstract readReview
In one paragraph

Review in Cardiovascular research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

132 citing papers in PubMed, 250 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Octreotide Counteracts IFN-γ-Induced Endothelial Inflammation.Journal of biochemical and molecular toxicology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Decoding ultrasensitive self-assembly of the calcium-regulatedbioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

72 more citing papers are in PubMed but not listed here.

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.

Qiang ShenDivision of Research, Department of Surgery, University of California at Davis School of Medicine, 4625 2nd Avenue, Sacramento, CA 95817, USA.
Robert R Rigor
Christopher D Pivetti
Mack H Wu
Sarah Y Yuan
University of California, Davis · US

Funding

NEUTROPHIL DEPENDENT REGULATION OF VENULAR PERMEABILITYR01HL061507 · NHLBI · UNIVERSITY OF SOUTH FLORIDA · PI YUAN, SARAH Y · 1999 to 2011
$3.4M
Microvascular Permeability and Matrix Fibrinogen Degradation in TraumaR01HL096640 · NHLBI · UNIVERSITY OF SOUTH FLORIDA · PI WU, MACK H · 2009 to 2013
$1.9M
PKC Isoenzymes Diabetic Microvascular HyperpermeabilityR01HL084542 · NHLBI · UNIVERSITY OF SOUTH FLORIDA · PI YUAN, SARAH Y · 2006 to 2010
$1.9M
VEGF Regulation of Microvascular PermeabilityR01HL073324 · NHLBI · UNIVERSITY OF CALIFORNIA DAVIS · PI WU, MACK H · 2004 to 2008
$1.6M
NHLBI NIH HHS HL61507NHLBI NIH HHS HL70752NHLBI NIH HHS HL73324NHLBI NIH HHS HL84542NHLBI NIH HHS HL96640
6 · The paper itself

Abstract

Microvascular barrier dysfunction is implicated in the initiation and progression of inflammation, posttraumatic complications, sepsis, ischaemia-reperfusion injury, atherosclerosis, and diabetes. Under physiological conditions, a precise equilibrium between endothelial cell-cell adhesion and actin-myosin-based centripetal tension tightly controls the semi-permeability of microvascular barriers. Myosin light chain kinase (MLCK) plays an important role in maintaining the equilibrium by phosphorylating myosin light chain (MLC), thereby inducing actomyosin contractility and weakening endothelial cell-cell adhesion. MLCK is activated by numerous physiological factors and inflammatory or angiogenic mediators, causing vascular hyperpermeability. In this review, we discuss experimental evidence supporting the crucial role of MLCK in the hyperpermeability response to key cell signalling events during inflammation. At the cellular level, in vitro studies of cultured endothelial monolayers treated with MLCK inhibitors or transfected with specific inhibiting peptides have demonstrated that induction of endothelial MLCK activity is necessary for hyperpermeability. Ex vivo studies of live microvessels, enabled by development of the isolated, perfused venule method, support the importance of MLCK in endothelial permeability regulation in an environment that more closely resembles in vivo tissues. Finally, the role of MLCK in vascular hyperpermeability has been confirmed with in vivo studies of animal disease models and the use of transgenic MLCK210 knockout mice. These approaches provide a more complete view of the role of MLCK in vascular barrier dysfunction.

Indexed as

Capillary PermeabilityActomyosinAnimalsBody FluidsCells, CulturedEndothelium, VascularHumansInflammationInflammation MediatorsMiceMice, TransgenicMicrovesselsModels, AnimalMyosin-Light-Chain KinaseMyosin Light ChainsPhosphorylationActomyosinInflammation MediatorsMyosin-Light-Chain KinaseMyosin Light ChainsProtein Kinase Inhibitors

Identifiers

PMID20479130
PMCPMC2895546
OpenAlexW1993409946

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.