Evidence map›Paper›PMID 30230261›Full record

ArticleJournal of cellular and molecular medicine2018

PKCα replaces AMPK to regulate mitophagy: Another PEDF role on ischaemic cardioprotection.

Haoran Miao, Fan Qiu, Bing Huang, Xiucheng Liu, Hao Zhang, Zhiwei Liu, Yanliang Yuan, Qixiang Zhao, Hu Zhang, Hongyan Dong and 1 more

Open access · goldAbstract read
In one paragraph

Article in Journal of cellular and molecular medicine, 2018. 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
1.0field-weighted citation impact, top 23% 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, 16 citations in OpenAlex.

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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

11 authors at 1 institution in 1 country.

Haoran MiaoDepartment of Thoracic Cardiovascular Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Fan QiuMorphological Research Experiment Center, Xuzhou Medical University, Xuzhou, China.
Bing HuangDepartment of Thoracic Cardiovascular Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Xiucheng LiuDepartment of Thoracic Cardiovascular Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Hao ZhangDepartment of Thoracic Cardiovascular Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Zhiwei LiuMorphological Research Experiment Center, Xuzhou Medical University, Xuzhou, China.
Yanliang YuanDepartment of Thoracic Cardiovascular Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Qixiang ZhaoDepartment of Thoracic Cardiovascular Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Hu ZhangDepartment of Thoracic Cardiovascular Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.
Hongyan DongMorphological Research Experiment Center, Xuzhou Medical University, Xuzhou, China.
Zhongming ZhangDepartment of Thoracic Cardiovascular Surgery, Affiliated Hospital of Xuzhou Medical University, Xuzhou, China.ORCID 0000-0001-9435-8000
Xuzhou Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Both decreased autophagy positive regulator AMP activated protein kinase (AMPK) level and promoted mitophagy are observed in oxygen-glucose deprivation (OGD) cardiomyocytes treated with pigment epithelium-derived factor (PEDF). This contradictory phenomenon and its underlying mechanisms have not been thoroughly elucidated. Our previous study reveals that PEDF increases the protein kinase Cα (PKCα) and phospho-PKCα (p-PKCα) contents to promote mitophagy. Thus, we investigated the association between PKCα and mitophagy. Here we identify an interaction between PKCα and Unc-51-like kinase 1 (ULK1), essential component of mitophagy. Further analyses show this is a direct interaction within a domain of ULK1 that termed the serine/threonine-rich domain (S/T domain). Notably, a deletion mutant ULK1 that lacks the binding domain is defective in mediating PEDF-induced mitophagy. Furthermore, we demonstrate that ULK1 is phosphorylated at Ser317/555/777 and Raptor is also phosphorylated by phospho-PKCα. Phospho-ULK1 (p-ULK1) at these sites are all essential for PEDF-induced mitophagy and reduce the release of mitochondrial ROS and DNA. This study therefore identifies a previously uncharacterized interaction between the ULK1 and PKCα that can replace the AMPK-dependent mitophagy processes.

Indexed as

AMP-Activated Protein KinasesAnimalsAutophagyAutophagy-Related Protein-1 HomologEye ProteinsHeart VentriclesHumansMitochondriaMitophagyMyocardial IschemiaMyocytes, CardiacNerve Growth FactorsPhosphorylationPigment Epithelium-Derived FactorPrimary Cell CultureProtein Kinase C-alphaAMP-Activated Protein KinasesAutophagy-Related Protein-1 HomologEye ProteinsNerve Growth FactorsPigment Epithelium-Derived FactorProtein Kinase C-alphaRegulatory-Associated Protein of mTORSerpinscardioprotectionmitophagyPhosphorylationpigment epithelium-derived factorprotein kinase CαUnc-51-like kinase 1

Identifiers

PMID30230261
PMCPMC6201373
OpenAlexW2891607166

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.