Evidence map›Paper›PMID 24350264›Full record

ArticleBioMed research international2013

Regulation of PKC autophosphorylation by calponin in contractile vascular smooth muscle tissue.

Hak Rim Kim, Cynthia Gallant, Kathleen G Morgan

Open access · hybridAbstract read
In one paragraph

Article in BioMed research international, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. The machinery of healthy vasoconstriction: an overview.Pflugers Archiv : European journal of physiology · 2025
    Review
  3. Review
  4. Review
  5. Review
  6. Evolution and function of calponin and transgelin.Frontiers in cell and developmental biology · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. 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 1 institution in 2 countries.

Hak Rim KimDepartment of Health Sciences, Boston University, 635 Commonwealth Avenue, Boston, MA 02215, USA ; Department of Pharmacology, College of Medicine, Dankook University, 119 Dandaero, Chungnam, Cheonan-si 330-714, Republic of Korea.
Cynthia GallantDepartment of Health Sciences, Boston University, 635 Commonwealth Avenue, Boston, MA 02215, USA.
Kathleen G MorganDepartment of Health Sciences, Boston University, 635 Commonwealth Avenue, Boston, MA 02215, USA.
Boston University · US

Funding

Structure-Function of the CytoskeletonP01HL086655 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 2007 to 2011
$8.8M
Subcellular Organization of Signaling in Smooth MuscleR01HL080003 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 2006 to 2009
$1.7M
NHLBI NIH HHS P01 HL086655NHLBI NIH HHS R01 HL080003
6 · The paper itself

Abstract

Protein kinase C (PKC) is a key enzyme involved in agonist-induced smooth muscle contraction. In some cases, regulatory phosphorylation of PKC is required for full activation of the enzyme. However, this issue has largely been ignored with respect to PKC-dependent regulation of contractile vascular smooth muscle (VSM) contractility. The first event in PKC regulation is a transphosphorylation by PDK at a conserved threonine in the activation loop of PKC, followed by the subsequent autophosphorylation at the turn motif and hydrophobic motif sites. In the present study, we determined whether phosphorylation of PKC is a regulated process in VSM and also investigated a potential role of calponin in the regulation of PKC. We found that calponin increases the level of in vitro PKCα phosphorylation at the PDK and hydrophobic sites, but not the turn motif site. In vascular tissues, phosphorylation of the PKC hydrophobic site, but not turn motif site, as well as phosphorylation of PDK at S241 increased in response to phenylephrine. Calponin knockdown inhibits autophosphorylation of cellular PKC in response to phenylephrine, confirming results with recombinant PKC. Thus these results show that autophosphorylation of PKC is regulated in dVSM and calponin is necessary for autophosphorylation of PKC in VSM.

Indexed as

AdducinsAmino Acid MotifsCalcium-Binding ProteinsCalmodulin-Binding ProteinsCalponinsHumansMAP Kinase Signaling SystemMicrofilament ProteinsMuscle ContractionMuscle, Smooth, VascularPhosphorylationProtein Kinase CAdducinsCalcium-Binding ProteinsCalmodulin-Binding ProteinsCalponinsMicrofilament ProteinsProtein Kinase C

Identifiers

PMID24350264
PMCPMC3852320
OpenAlexW2096794031

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.