Evidence map›Paper›PMID 29021584›Full record

ArticleScientific reports2017

Mortalin deficiency suppresses fibrosis and induces apoptosis in keloid spheroids.

Won Jai Lee, Hyo Min Ahn, Youjin Na, Renu Wadhwa, JinWoo Hong, Chae-Ok Yun

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Targeting the Akt/PI3K/mTOR signaling pathway for complete eradication of keloid disease by sunitinib.Apoptosis : an international journal on programmed cell death · 2022
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Advances in wound care · 2019
    Review
  14. 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

6 authors at 4 institutions in 2 countries.

Won Jai LeeInstitute for Human Tissue Restoration, Department of Plastic & Reconstructive Surgery, Yonsei University College of Medicine, Seoul, Korea.
Hyo Min AhnDepartment of Bioengineering, College of Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul, 04763, Korea.
Youjin NaDepartment of Bioengineering, College of Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul, 04763, Korea.
Renu WadhwaDAILAB, National Institute of Advanced Industrial Science and Technology (AIST), Central 5-41, 1-1-1 Higashi, Tsukuba, Ibaraki, 305-8565, Japan.
JinWoo HongDepartment of Bioengineering, College of Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul, 04763, Korea.
Chae-Ok YunDepartment of Bioengineering, College of Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul, 04763, Korea. chaeok@hanyang.ac.kr.
Anyang University · KRHanyang University · KRNational Institute of Advanced Industrial Science and Technology · JPYonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mortalin (Mot) is a mitochondrial chaperone of the heat shock protein 70 family and it's pro-proliferative and anti-apoptosis functions could be associated with keloid pathogenesis, and blocking of mortalin and its interaction with p53 might be a potential novel target for the treatment of keloid. Therefore, we generated mortalin-specific small hairpin (sh) RNAs (dE1-RGD/GFP/shMot) and introduced into keloid spheroids for examination of its apoptotic and anti-fibrotic effect. On keloid tissues, mortalin expression was higher than adjacent normal tissues and it's protein expressions were activated keloid fibroblasts (KFs). After primary keloid spheroid were transduced with dE1-RGD/GFP/shMot for knockdown of mortalin, expression of type I, III collagen, fibronectin, and elastin was significantly reduced and transforming growth factor-β1, epidermal growth factor receptor (EGFR), Extracellular Signal-Regulated Kinases 1 and 2 (Erk 1/2), and Smad 2/3 complex protein expression were decreased. In addition, increased TUNEL activities and cytochrome C were observed. Further, for examine of mortalin and p53 interaction, we performed immunofluorescence analysis. Knockdown of mortalin relocated p53 to the cell nucleus in primary keloid spheroids by dE1-RGD/GFP/shMot transduction. These results support the utility of knockdown of mortalin to induce apoptosis and reduce ECMs expression in keloid spheroid, which may be highly beneficial in treating keloids.

Indexed as

AdenoviridaeApoptosisCell NucleusCollagen Type ICollagen Type IIIElastinErbB ReceptorsExtracellular Signal-Regulated MAP KinasesFibroblastsFibronectinsFibrosisHSP70 Heat-Shock ProteinsHumansKeloidProliferating Cell Nuclear AntigenProtein BindingCollagen Type ICollagen Type IIIElastinErbB ReceptorsExtracellular Signal-Regulated MAP KinasesFibronectinsHSP70 Heat-Shock ProteinsmortalinProliferating Cell Nuclear AntigenRNA, Small InterferingTransforming Growth Factor betaTumor Suppressor Protein p53

Identifiers

PMID29021584
PMCPMC5636810
OpenAlexW2763734056

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.