Evidence mapPaperPMID 41355505Full record

ArticleIUBMB life2025

Effects of Methylglyoxal on Intestinal Cells: Insights on Epigenetic Regulatory Enzymes.

Camilla Morresi, Giulia Feliziani, Luisa Bellachioma, Christian Giommi, Rosita Gabbianelli, Laura Bordoni, Gianna Ferretti, Tiziana Bacchetti, Elisabetta Damiani

Abstract read
In one paragraph

Article in IUBMB life, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

9 authors.

Camilla MorresiDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Ancona, Italy.
Giulia FelizianiSchool of Advanced Studies, University of Camerino, Camerino, MC, Italy.
Luisa BellachiomaDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Ancona, Italy.
Christian GiommiDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Ancona, Italy.
Rosita GabbianelliUnit of Molecular Biology and Nutrigenomics, University of Camerino, Camerino, MC, Italy.ORCID 0000-0003-0037-7740
Laura BordoniUnit of Molecular Biology and Nutrigenomics, University of Camerino, Camerino, MC, Italy.ORCID 0000-0001-6968-1164
Gianna FerrettiDepartment of Clinical Experimental Science and Odontostomatology, Polytechnic University of Marche, Ancona, Italy.
Tiziana BacchettiDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Ancona, Italy.ORCID 0000-0003-3346-9588
Elisabetta DamianiDepartment of Life and Environmental Sciences, Polytechnic University of Marche, Ancona, Italy.

Funding

NGEU PNRR, D.M. n. 118/2023 M4C1 I.4.1. FPA300015Polytechnic University of Marche - Scientific Research FundsRosita Gabbianelli FPD112001University of Camerino - Scientific Research Funds
6 · The paper itself

Abstract

Methylglyoxal (MGO) is endogenously produced under physiological conditions as a by-product of glycolysis and by autooxidation of glucose and lipid peroxidation. The digestive system can also take up MGO from exogenous sources, especially from ultra-processed foods. MGO is a highly reactive molecule, able to react with macromolecules forming covalent adducts resulting in advanced glycation end-products formation. MGO can also enter the nucleus and react with nucleic acids with the formation of MGO-nucleic acid adducts. The intestinal epithelium is continuously exposed to dietary and endogenous stimuli, including MGO, but the potential harmful role of MGO at the intestinal level has been poorly investigated. Therefore, the aim of the study was to further investigate the effects of MGO in intestinal cells and the molecular mechanisms involved, with particular attention to epigenetic regulatory enzymes such as histone deacetylases (HDAC), ten-eleven translocation (TET) family enzymes, and DNA methyltransferases (DNMT). Our results demonstrate that MGO exposure induces alterations in intestinal barrier function in differentiated Caco-2 cells monolayers. Moreover, MGO treatment induces cell apoptosis associated with an increase in cytosolic and mitochondrial reactive oxygen species. MGO-induced oxidative stress was associated with activation of the NFκB pathway and increased levels of proinflammatory molecules such as TNF-α and antioxidant enzymes (superoxide dismutase 1 [SOD1] and catalase). The increased expression of γH2AX suggests damage to DNA in MGO-treated cells. A decrease in HDAC1/2 expression, consistent with the increase in acetylated histone H4 levels, and an inhibition of the expression of TET (TET1, TET2) proteins was observed in MGO-treated cells. These results suggest that MGO may also disrupt epigenetic homeostasis mechanisms, offering further insight into the pathways through which MGO causes cellular damage in intestinal cells.

Indexed as

Epigenesis, GeneticIntestinal MucosaPyruvaldehydeApoptosisCaco-2 CellsDioxygenasesDNA-Binding ProteinsHistone DeacetylasesHistonesHumansMixed Function OxygenasesNF-kappa BOxidative StressProto-Oncogene ProteinsReactive Oxygen SpeciesDioxygenasesDNA-Binding ProteinsHistone DeacetylasesHistonesMixed Function OxygenasesNF-kappa BProto-Oncogene ProteinsPyruvaldehydeReactive Oxygen SpeciesTET1 protein, humanTET2 protein, humanepigeneticsinflammatory bowel diseasesmethylglyoxaloxidative stressultra‐processed foods

Identifiers

PMID41355505
PMCPMC12683318

What Socratic 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 Socratic graph.