Evidence map›Paper›PMID 28870220›Full record

ArticleJournal of biomedical science2017

The type VI adenylyl cyclase protects cardiomyocytes from β-adrenergic stress by a PKA/STAT3-dependent pathway.

Yu-Shuo Wu, Chien-Chang Chen, Chen-Li Chien, Hsing-Lin Lai, Si-Tse Jiang, Yong-Cyuan Chen, Lin-Ping Lai, Wei-Fan Hsiao, Wen-Pin Chen, Yijuang Chern

Open access · diamondAbstract read
In one paragraph

Article in Journal of biomedical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. An Update on the Multifaceted Roles of STAT3 in the Heart.Frontiers in cardiovascular medicine · 2019
    Review
  7. Function of Adenylyl Cyclase in Heart: the AKAP Connection.Journal of cardiovascular development and disease · 2018
    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

10 authors at 4 institutions in 1 country.

Yu-Shuo WuGraduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan.
Chien-Chang ChenGraduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan.
Chen-Li ChienGraduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan.
Hsing-Lin LaiInstitute of Biomedical Sciences, Academia Sinica, Nankang, Taipei, 115, Taiwan.
Si-Tse JiangNational Laboratory Animal Center, National Applied Research Laboratories, Tainan, Taiwan.
Yong-Cyuan ChenInstitute of Biomedical Sciences, Academia Sinica, Nankang, Taipei, 115, Taiwan.
Lin-Ping LaiInstitute of Internal Medicine, College of Medicine, National Taiwan University, Taipei, Taiwan.
Wei-Fan HsiaoInstitute of Pharmacology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Wen-Pin ChenInstitute of Pharmacology, College of Medicine, National Taiwan University, Taipei, Taiwan. chenwenpin@ntu.edu.tw.
Yijuang ChernGraduate Institute of Life Sciences, National Defense Medical Center, Taipei, Taiwan. bmychern@ibms.sinica.edu.tw.
Institute of Biomedical Sciences, Academia Sinica · TWNational Taiwan University · TWNational Applied Research Laboratories · TWNational Defense Medical Center · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe type VI adenylyl cyclase (AC6) is a main contributor of cAMP production in the heart. The amino acid (aa) sequence of AC6 is highly homologous to that of another major cardiac adenylyl cyclase, AC5, except for its N-terminus (AC6-N, aa 1-86). Activation of AC6, rather than AC5, produces cardioprotective effects against heart failure, while the underlying mechanism remains to be unveiled. Using an AC6-null (AC6

methodsWestern blot analysis and immunofluorescence staining were performed to determine the intracellular distribution of AC6, AC6-ΔN (a truncated AC6 lacking the first 86 amino acids), and STAT3 activation. Activities of AC6 and AC6-ΔN in the heart were assessed by cAMP assay. Apoptosis of cardiomyocytes were evaluated by the TUNEL assay and a propidium iodine-based survival assay. Fibrosis was examined by collagen staining.

resultsImmunofluorescence staining revealed that cardiac AC6 was mainly anchored on the sarcolemmal membranes, while AC6-ΔN was redistributed to the sarcoplasmic reticulum. AC6

conclusionsCollectively, AC6-N controls the anchorage of cardiac AC6 on the sarcolemmal membrane, which enables the coupling of AC6 with the pro-survival PKA-STAT3 pathway. Our findings may facilitate the development of novel therapies for heart failure.

Indexed as

Signal TransductionAdenylyl CyclasesAnimalsApoptosisHeart FailureMiceMice, Inbred C57BLMyocytes, CardiacProtective AgentsSTAT3 Transcription Factoradenylyl cyclase 6Adenylyl CyclasesProtective AgentsStat3 protein, mouseSTAT3 Transcription FactorAC6cAMPMicrodomainSTAT3Type V adenylyl cyclase

Identifiers

PMID28870220
PMCPMC5584049
OpenAlexW2751463172

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.