Evidence map›Paper›PMID 20802137›Full record

ArticleAmerican journal of physiology. Heart and circulatory physiology2010

cGMP-dependent protein kinase and the regulation of vascular smooth muscle cell gene expression: possible involvement of Elk-1 sumoylation.

ChungSik Choi, Hassan Sellak, Felricia M Brown, Thomas M Lincoln

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Heart and circulatory physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. SUMO2 regulates vascular endothelial function and oxidative stress in mice.American journal of physiology. Heart and circulatory physiology · 2019
    Article
  4. cGMP Signaling and Vascular Smooth Muscle Cell Plasticity.Journal of cardiovascular development and disease · 2018
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Contractile protein expression is upregulated by reactive oxygen species in aorta of Goto-Kakizaki rat.American journal of physiology. Heart and circulatory physiology · 2014
    Article
  10. Hypoxic depression of PKG-mediated inhibition of serotonergic contraction in ovine carotid arteries.American journal of physiology. Regulatory, integrative and comparative physiology · 2013
    Article
  11. Review
  12. Review
  13. 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

4 authors at 1 institution in 1 country.

ChungSik ChoiDepartment of Physiology, College of Medicine, University of South Alabama, Mobile, Alabama 36609, USA.
Hassan Sellak
Felricia M Brown
Thomas M Lincoln
University of South Alabama · US

Funding

Expression of PKG in Vascular Smooth Muscle CellsR01HL066164 · NHLBI · UNIVERSITY OF SOUTH ALABAMA · PI LINCOLN, THOMAS M. · 2001 to 2013
$4.2M
CONTROL OF VASCULAR SMOOTH MUSCLE CELL PHENOTYPE BY CGMPR01HL053426 · NHLBI · UNIVERSITY OF SOUTH ALABAMA · PI LINCOLN, THOMAS M. · 1995 to 2009
$1.9M
NHLBI NIH HHS HL-053426NHLBI NIH HHS HL-066164
6 · The paper itself

Abstract

Although the regulation of smooth muscle cell (SMC) gene expression by cGMP-dependent protein kinase (PKG) is now recognized, the mechanisms underlying these effects are not fully understood. In this study, we report that PKG-I stimulates myocardin/serum response factor (SRF)-dependent gene expression in vascular SMCs. The expression of PKG in PKG-deficient cells enhanced myocardin-induced SM22 promoter activity in a concentration-dependent fashion. However, neither SRF nor myocardin expression was affected. To investigate alternative mechanisms, we examined whether PKG affects the phosphorylation of E26-like protein-1 (Elk-1), a SRF/myocardin transcription antagonist. The activation of PKG caused an increase in a higher molecular mass form of phospho-Elk-1 that was determined to be small ubiquitin-related modifier (sumo)ylated Elk-1. PKG increased Elk-1 sumoylation twofold compared with the PKG-deficient cells, and Elk-1 sumoylation was reduced using dominant-negative sumo-conjugating enzyme, DN-Ubc9, confirming PKG-dependent sumoylation of phospho-Elk-1 in vascular SMCs. In addition, PKG stimulated Elk-1 sumoylation in COS-7 cells overexpressing Elk-1, sumo-1, and PKG-I. The increased expression of PKG in vascular SMCs inhibited Elk-1 binding to SMC-specific promoters, SM22 and smooth muscle myosin heavy chain, as measured by EMSA and chromatin immunoprecipitation assay, and PKG suppressed the Elk-1 inhibition of SM22 reporter gene expression. Taken together, these data suggest that PKG-I decreases Elk-1 activity by sumo modification of Elk-1, thereby increasing myocardin-SRF activity on SMC-specific gene expression.

Indexed as

AnimalsCells, CulturedChlorocebus aethiopsCOS CellsCyclic GMP-Dependent Protein Kinasesets-Domain Protein Elk-1Gene Expression RegulationMicrofilament ProteinsModels, AnimalMuscle ProteinsMuscle, Smooth, VascularMyocardinNuclear ProteinsPhosphorylationRatsRats, Sprague-DawleyCyclic GMP-Dependent Protein Kinasesets-Domain Protein Elk-1Microfilament ProteinsMuscle ProteinsMyocardinNuclear ProteinsTrans-Activatorstransgelin

Identifiers

PMID20802137
PMCPMC2993191
OpenAlexW2101707570

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.