Evidence map›Paper›PMID 30871110›Full record

ArticleInternational journal of molecular sciences2019

Extracellular Spermine Activates DNA Methyltransferase 3A and 3B.

Taro Fukui, Kuniyasu Soda, Koichi Takao, Toshiki Rikiyama

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 28% 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, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Polyamine metabolism and anti-tumor immunity.Frontiers in immunology · 2025
    Review
  6. Review
  7. Association of spermidine plasma levels with brain aging in a population-based study.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2023
    Article
  8. Nrf2Frontiers in genetics · 2023
    Article
  9. Nucleosome destabilization by polyamines.Archives of biochemistry and biophysics · 2022
    Article
  10. Review
  11. Article
  12. Observational
  13. Article
  14. 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

4 authors at 2 institutions in 1 country.

Taro FukuiDepartment of Surgery, Saitama Medical Center, Jichi Medical University, Saitama-city, Saitama 330-8503, Japan. d1423@jichi.ac.jp.
Kuniyasu SodaCardiovascular Research Institute, Saitama Medical Center, Jichi Medical University, Saitama-city, Saitama 330-8503, Japan. soda@jichi.ac.jp.ORCID 0000-0003-3371-8986
Koichi TakaoLaboratory of Cellular Physiology, Department of Clinical Dietetics & Human Nutrition, Faculty of Pharmaceutical Sciences, Josai University, Sakado, Saitama 350-0295, Japan. ktakao@josai.ac.jp.
Toshiki RikiyamaDepartment of Surgery, Saitama Medical Center, Jichi Medical University, Saitama-city, Saitama 330-8503, Japan. trikiyama@jichi.ac.jp.
Jichi Medical University · JPJosai University · JP

Funding

Food and Health Program of the Honjo International Scholarship Foundation no numberJapan Society for the Promotion of Science JSPS KAKENHI 26500015
6 · The paper itself

Abstract

We first demonstrated that long-term increased polyamine (spermine, spermidine, putrescine) intake elevated blood spermine levels in mice and humans, and lifelong consumption of polyamine-rich chow inhibited aging-associated increase in aberrant DNA methylation, inhibited aging-associated pathological changes, and extend lifespan of mouse. Because gene methylation status is closely associated with aging-associated conditions and polyamine metabolism is closely associated with regulation of gene methylation, we investigated the effects of extracellular spermine supplementation on substrate concentrations and enzyme activities involved in gene methylation. Jurkat cells and human mammary epithelial cells were cultured with spermine and/or D,L-alpha-difluoromethylornithine (DFMO), an inhibitor of ornithine decarboxylase. Spermine supplementation inhibited enzymatic activities of adenosylmethionine decarboxylase in both cells. The ratio of decarboxylated S-adenosylmethionine to S-adenosyl-L-methionine increased by DFMO and decreased by spermine. In Jurkat cells cultured with DFMO, the protein levels of DNA methyltransferases (DNMTs) 1, 3A and 3B were not changed, however the activity of the three enzymes markedly decreased. The protein levels of these enzymes were not changed by addition of spermine, DNMT 3A and especially 3B were activated. We show that changes in polyamine metabolism dramatically affect substrate concentrations and activities of enzymes involved in gene methylation.

Indexed as

Adenosylmethionine DecarboxylaseCell Line, TumorCells, CulturedDNA (Cytosine-5-)-MethyltransferasesDNA MethylationDNA Methyltransferase 3ADNA Methyltransferase 3BDNA Modification MethylasesEflornithineEpithelial CellsHumansJurkat CellsMammary Glands, HumanOrnithine DecarboxylasePolyaminesPutrescineAdenosylmethionine DecarboxylaseDNA (Cytosine-5-)-MethyltransferasesDNA Methyltransferase 3ADNA Methyltransferase 3BDNA Modification MethylasesDNMT3A protein, humanDnmt3a protein, mouseEflornithineOrnithine DecarboxylasePolyaminesPutrescineS-adenosyl-3-methylthiopropylamineS-AdenosylmethionineSpermidineSpermineadenosylmethionineD,L-alpha-difluoromethylornithine (DFMO)DNA methyltransferase (DNMT)gene methylationmethyltransferaseornithine decarboxylase (ODC)polyaminespermine

Identifiers

PMID30871110
PMCPMC6429523
OpenAlexW2922515515

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.