Evidence map›Paper›PMID 21865586›Full record

ArticleAmerican journal of physiology. Cell physiology2011

Tissue length modulates "stimulated actin polymerization," force augmentation, and the rate of swine carotid arterial contraction.

Ankit D Tejani, Michael P Walsh, Christopher M Rembold

Abstract 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 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-weighted citation impact, top 34% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  2. Article
  3. Article
  4. Review
  5. Reply from Chun Y. Seow.The Journal of physiology · 2015
    Article
  6. Article
  7. Article
  8. The role of actin filament dynamics in the myogenic response of cerebral resistance arteries.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2013
    Review
  9. Review
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 2 countries.

Ankit D TejaniCardiovascular Division, University of Virginia Health System, Charlottesville, VA 22908-0146, USA.
Michael P Walsh
Christopher M Rembold
University of Virginia Health System · USUniversity of Calgary · CA

Funding

P20-Mediated Suppression of Vascular ForceR01HL071191 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI REMBOLD, CHRISTOPHER M · 2002 to 2004
$999k
Canadian Institutes of Health Research MOP13101NHLBI NIH HHS HL-71191
6 · The paper itself

Abstract

"Stimulated actin polymerization" has been proposed to be involved in force augmentation, in which prior submaximal activation of vascular smooth muscle increases the force of a subsequent maximal contraction by ∼15%. In this study, we altered stimulated actin polymerization by adjusting tissue length and then measured the effect on force augmentation. At optimal tissue length (1.0 L(o)), force augmentation was observed and was associated with increased prior stimulated actin polymerization, as evidenced by increased prior Y118 paxillin phosphorylation without changes in prior S3 cofilin or cross-bridge phosphorylation. Tissue length, per se, regulated Y118 paxillin, but not S3 cofilin, phosphorylation. At short tissue length (0.6 L(o)), force augmentation was observed and was associated with increased prior stimulated actin polymerization, as evidenced by reduced prior S3 cofilin phosphorylation without changes in Y118 paxillin or cross-bridge phosphorylation. At long tissue length (1.4 L(o)), force augmentation was not observed, and there were no prior changes in Y118 paxillin, S3 cofilin, or cross-bridge phosphorylation. There were no significant differences in the cross-bridge phosphorylation transients before and after the force augmentation protocol at all three lengths tested. Tissues contracted faster at longer tissue lengths; contractile rate correlated with prior Y118 paxillin phosphorylation. Total stress, per se, predicted Y118 paxillin phosphorylation. These data suggest that force augmentation is regulated by stimulated actin polymerization and that stimulated actin polymerization is regulated by total arterial stress. We suggest that K(+) depolarization first leads to cross-bridge phosphorylation and contraction, and the contraction-induced increase in mechanical strain increases Y118 paxillin phosphorylation, leading to stimulated actin polymerization, which further increases force, i.e., force augmentation and, possibly, latch.

Indexed as

ActinsAnimalsCarotid ArteriesElectrophoresis, Polyacrylamide GelMuscle ContractionMuscle, Smooth, VascularPaxillinPhosphorylationPolymerizationSwineVasoconstrictionActinsPaxillin

Identifiers

PMID21865586
PMCPMC3233796
OpenAlexW1978073592

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.