Evidence map›Paper›PMID 29141455›Full record

ReviewExperimental biology and medicine (Maywood, N.J.)2018

Methionine adenosyltransferases in cancers: Mechanisms of dysregulation and implications for therapy.

Lauren Y Maldonado, Diana Arsene, José M Mato, Shelly C Lu

Open access · bronzeAbstract readReview
In one paragraph

Review in Experimental biology and medicine (Maywood, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Methionine restriction and mimetics to ameliorate human aging and disease.Trends in endocrinology and metabolism: TEM · 2026
    Review
  3. Review
  4. A novel role of secreted methionine adenosyltransferase α2 in colorectal liver metastases.Journal of experimental & clinical cancer research : CR · 2025
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Cellular Signaling of Amino Acid Metabolism in Prostate Cancer.International journal of molecular sciences · 2025
    Review
  10. Article
  11. Review
  12. Formaldehyde regulatesScience (New York, N.Y.) · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 4 institutions in 2 countries.

Lauren Y Maldonado1 Keck School of Medicine, University of Southern California, Los Angeles, CA 90033, USA.
Diana Arsene2 Division of Gastroenterology and Hepatology, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
José M Mato3 CIC bioGUNE, Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (Ciberehd), Technology, Derio, Bizkaia 48160, Spain.
Shelly C Lu4 Division of Digestive and Liver Diseases, 22494 Cedars-Sinai Medical Center , Cedars-Sinai Medical Center, LA, CA 90048, USA.
Cedars-Sinai Medical Center · USCIC bioGUNE · ESUniversity of North Carolina at Chapel Hill · USUniversity of Southern California · US

Funding

Role of SAMe in Pathogenesis and Treatment of Non-Alcholic Fatty Liver DiseaseR01AT001576 · NCCIH · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LU, SHELLY CHI-LOO · 2002 to 2018
$5.0M
S-Adenosylmethionine in Protein Posttranslational Modifications and HCC TreatmentR01DK107288 · NIDDK · CEDARS-SINAI MEDICAL CENTER · PI LU, SHELLY CHI-LOO · 2015 to 2018
$1.6M
DYSREGULATION OF GSH SYNTHESIS DURING LIVER INJURY AND FIBROSISR01DK092407 · NIDDK · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LU, SHELLY CHI-LOO · 2012 to 2016
$1.6M
PROHIBITIN 1 IN LIVER INJURY AND CANCERR01CA172086 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LU, SHELLY CHI-LOO · 2014 to 2018
$1.6M
NCCIH NIH HHS R01 AT001576NCI NIH HHS R01 CA172086NIDDK NIH HHS R01 DK092407NIDDK NIH HHS R01 DK107288
6 · The paper itself

Abstract

Methionine adenosyltransferase genes encode enzymes responsible for the biosynthesis of S-adenosylmethionine, the principal biological methyl donor and precursor of polyamines and glutathione. Mammalian cells express three genes - MAT1A, MAT2A, and MAT2B - with distinct expression and functions. MAT1A is mainly expressed in the liver and maintains the differentiated states of both hepatocytes and bile duct epithelial cells. Conversely, MAT2A and MAT2B are widely distributed in non-parenchymal cells of the liver and extrahepatic tissues. Increasing evidence suggests that methionine adenosyltransferases play significant roles in the development of cancers. Liver cancers, namely hepatocellular carcinoma and cholangiocarcinoma, involve dysregulation of all three methionine adenosyltransferase genes. MAT1A reduction is associated with increased oxidative stress, progenitor cell expansion, genomic instability, and other mechanisms implicated in tumorigenesis. MAT2A/MAT2B induction confers growth and survival advantage to cancerous cells, enhancing tumor migration. Highlighted examples from colon, gastric, breast, pancreas and prostate cancer studies further underscore methionine adenosyltransferase genes' role beyond the liver in cancer development. In this subset of extra-hepatic cancers, MAT2A and MAT2B are induced via different regulatory mechanisms. Understanding the role of methionine adenosyltransferase genes in tumorigenesis helps identify attributes of these genes that may serve as valuable targets for therapy. While S-adenosylmethionine, and its metabolite, methylthioadenosine, have been largely explored as therapeutic interventions, targets aimed at regulation of MAT gene expression and methionine adenosyltransferase protein-protein interactions are now surfacing as potential effective strategies for treatment and chemoprevention of cancers. Impact statement This review examines the role of methionine adenosyltransferases (MATs) in human cancer development, with a particular focus on liver cancers in which all three MAT genes are implicated in tumorigenesis. An overview of MAT genes, isoenzymes and their regulation provide context for understanding consequences of dysregulation. Highlighting examples from liver, colon, gastric, breast, pancreas and prostate cancers underscore the importance of understanding MAT's tumorigenic role in identifying future targets for cancer therapy.

Indexed as

AnimalsDisease Models, AnimalHumansMethionine AdenosyltransferaseNeoplasmsS-AdenosylmethionineMethionine AdenosyltransferaseS-AdenosylmethionineChemopreventioncholangiocarcinomacolon cancerhepatocellular carcinomamethionine adenosyltransferaseS-adenoylmethionine

Identifiers

PMID29141455
PMCPMC5788143
OpenAlexW2768361988

What OpenQuestion holds

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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.