Evidence map›Paper›PMID 20154261›Full record

ArticleAmerican journal of physiology. Heart and circulatory physiology2010

Novel bradykinin signaling in adult rat cardiac myocytes through activation of p21-activated kinase.

Yunbo Ke, Katherine A Sheehan, E Eroume A Egom, Ming Lei, R John Solaro

Abstract 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 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Targeting p21-activated kinase 1 for development of a novel anti-arrhythmic drug class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  2. Review
  3. Review
  4. Role of p21-activated kinases in cardiovascular development and function.Cellular and molecular life sciences : CMLS · 2013
    Review
  5. Article
  6. Novel roles of PAK1 in the heart.Cellular logistics · 2012
    Article
  7. Article
  8. Review
  9. Article
  10. 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

5 authors at 3 institutions in 2 countries.

Yunbo KeDepartment of Physiology and Biophysics and Center for Cardiovascular Research, University of Illinois at Chicago, USA.
Katherine A Sheehan
E Eroume A Egom
Ming Lei
R John Solaro
University of Illinois Chicago · USUniversity of Manchester · GBVictoria Hospital · GB

Funding

Sarcomeric Modifications and Progressive Cardiac MaladaptationP01HL062426 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI AI, XUN · 2000 to 2020
$42.4M
TRAINING IN CELLULAR SIGNALLING IN THE CARDIOVASCULAR SYT32HL007692 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLARO, R JOHN · 1990 to 2014
$8.5M
Troponin Mudulation in Heart FailureR01HL064035 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLARO, R JOHN, WOLSKA, BEATA M. · 2000 to 2013
$4.7M
Pak1 Regulation of Cardiac Protein PhosphorylationF32HL076984 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SHEEHAN, KATHERINE ANN · 2004 to 2005
$81k
British Heart FoundationNHLBI NIH HHS F32-HL-076984NHLBI NIH HHS P01-HL-62426NHLBI NIH HHS R01 HL064035NHLBI NIH HHS R01-HL-64035NHLBI NIH HHS T32-HL-07692Wellcome Trust
6 · The paper itself

Abstract

Although bradykinin (BK) is known to exert effects on the myocardium, its intracellular signaling pathways remain poorly understood. Experiments in other cell types indicated that p21-activated kinase-1 (Pak1), a Ser/Thr kinase downstream of small monomeric G proteins, is activated by BK. We previously reported that the expression of active Pak1 in adult cardiac myocytes induced activation of protein phosphatase 2A and dephosphorylation of myofilament proteins (Ke et al. Circ Res 94: 194-200, 2004). In experiments reported here, we tested the hypothesis that BK signals altered protein phosphorylation in adult rat cardiac myocytes through the activation and translocation of Pak1. Treatment of myocytes with BK resulted in the activation of Pak1 as demonstrated by increased autophosphorylation at Thr423 and a diminished striated localization, which is present in the basal state. BK induced dephosphorylation of both cardiac troponin I and phospholamban. Treatment of isolated myocytes with BK also blunted the effect of isoproterenol to enhance peak Ca(2+) and relaxation of Ca(2+) transients. Protein phosphatase 2A was demonstrated to associate with both Pak 1 and phospholamban. Our studies indicate a novel signaling mechanism for BK in adult rat cardiac myocytes and support our hypothesis that Pak 1 is a significant regulator of phosphatase activity in the heart.

Indexed as

Adrenergic beta-AgonistsAnimalsBradykininCalcium-Binding ProteinsCells, CulturedIsoproterenolMaleModels, AnimalMyocytes, Cardiacp21-Activated KinasesPhospholambanPhosphorylationProtein Phosphatase 2RatsSignal TransductionTroponin IAdrenergic beta-AgonistsBradykininCalcium-Binding ProteinsIsoproterenolp21-Activated KinasesPak1 protein, ratPhospholambanProtein Phosphatase 2Troponin I

Identifiers

PMID20154261
PMCPMC2853422
OpenAlexW2157357993

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.