Evidence map›Paper›PMID 28378765›Full record

ArticleScientific reports2017

A lignan induces lysosomal dependent degradation of FoxM1 protein to suppress β-catenin nuclear translocation.

Guang-Zhi Dong, Ji Hye Jeong, Yu-Ih Lee, Yeong Eun Han, Jung Sook Shin, Yoon-Jung Kim, Raok Jeon, Young Hwa Kim, Tae Jun Park, Keun Il Kim and 1 more

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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Natural Extracts ofAntioxidants (Basel, Switzerland) · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Lignan fromMolecules (Basel, Switzerland) · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. 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

11 authors at 2 institutions in 1 country.

Guang-Zhi DongResearch Center for Cell Fate Control and College of Pharmacy, Sookmyung Women's University, Seoul 04310, Korea.
Ji Hye JeongResearch Center for Cell Fate Control and College of Pharmacy, Sookmyung Women's University, Seoul 04310, Korea.
Yu-Ih LeeResearch Center for Cell Fate Control and College of Pharmacy, Sookmyung Women's University, Seoul 04310, Korea.
Yeong Eun HanResearch Center for Cell Fate Control and College of Pharmacy, Sookmyung Women's University, Seoul 04310, Korea.
Jung Sook ShinResearch Center for Cell Fate Control and College of Pharmacy, Sookmyung Women's University, Seoul 04310, Korea.
Yoon-Jung KimResearch Center for Cell Fate Control and College of Pharmacy, Sookmyung Women's University, Seoul 04310, Korea.
Raok JeonResearch Center for Cell Fate Control and College of Pharmacy, Sookmyung Women's University, Seoul 04310, Korea.
Young Hwa KimDepartment of Biochemistry and Molecular Biology, School of Medicine, Ajou University, Suwon, 16499, Korea.
Tae Jun ParkDepartment of Biochemistry and Molecular Biology, School of Medicine, Ajou University, Suwon, 16499, Korea.
Keun Il KimDepartment of Biological Science, Sookmyung Women's University, Seoul 04310, Korea.
Jae-Ha RyuResearch Center for Cell Fate Control and College of Pharmacy, Sookmyung Women's University, Seoul 04310, Korea.
Sookmyung Women's University · KRAjou University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Colon cancer is one of the most common cancers. In this study, we isolated a lignan [(-)-(2R,3R)-1,4-O-diferuloylsecoisolariciresinol, DFS] from Alnus japonica (Betulaceae) and investigated its biological activity and mechanism of action on colon cancer. DFS reduced the viability of colon cancer cells and induced cell cycle arrest. DFS also suppressed β-catenin nuclear translocation and β-catenin target gene expression through a reduction in FoxM1 protein. To assess the mechanism of the action of DFS, we investigated the effect of DFS on endogenous and exogenous FoxM1 protein degradation in colon cancer cells. DFS-induced FoxM1 protein degradation was suppressed by lysosomal inhibitors, chloroquine and bafilomycin A1, but not by knock-down of proteasomal proteins. The mechanism of DFS for FoxM1 degradation is lysosomal dependent, which was not reported before. Furthermore, we found that FoxM1 degradation was partially lysosomal-dependent under normal conditions. These observations indicate that DFS from A. japonica suppresses colon cancer cell proliferation by reducing β-catenin nuclear translocation. DFS induces lysosomal-dependent FoxM1 protein degradation. This is the first report on the lysosomal degradation of FoxM1 by a small molecule. DFS may be useful in treating cancers that feature the elevated expression of FoxM1.

Indexed as

Active Transport, Cell NucleusAlnusAnimalsbeta CateninCell LineCell Line, TumorCell ProliferationCells, CulturedForkhead Box Protein M1Gene Expression Regulation, NeoplasticHCT116 CellsHEK293 CellsHumansLignansLysosomesMice, Inbred C57BLbeta CateninForkhead Box Protein M1FOXM1 protein, humanLignans

Identifiers

PMID28378765
PMCPMC5380986
OpenAlexW2605046123

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.