Evidence map›Paper›PMID 39456676›Full record

ArticleInternational journal of molecular sciences2024

Overexpression of Glyoxalase 2 in Human Breast Cancer Cells: Implications for Cell Proliferation and Doxorubicin Resistance.

Brenda Romaldi, Andrea Scirè, Cristina Minnelli, Andrea Frontini, Giulia Casari, Laura Cianfruglia, Giovanna Mobbili, Lidia de Bari, Cinzia Antognelli, Federico V Pallardó and 1 more

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
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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.

Brenda RomaldiDepartment of Odontostomatologic and Specialized Clinical Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.
Andrea ScirèDepartment of Life and Environmental Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.ORCID 0000-0002-8288-6989
Cristina MinnelliDepartment of Life and Environmental Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.ORCID 0000-0001-8034-8557
Andrea FrontiniDepartment of Life and Environmental Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.ORCID 0000-0002-7381-4107
Giulia CasariDepartment of Odontostomatologic and Specialized Clinical Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.
Laura CianfrugliaDepartment of Odontostomatologic and Specialized Clinical Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.ORCID 0000-0002-0322-0282
Giovanna MobbiliDepartment of Life and Environmental Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.ORCID 0000-0003-0243-5844
Lidia de BariInstitute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IBIOM), National Research Council (CNR), 70126 Bari, Italy.ORCID 0000-0003-2164-5660
Cinzia AntognelliDepartment of Medicine and Surgery, Università degli Studi di Perugia, 06129 Perugia, Italy.ORCID 0000-0002-8259-680X
Federico V PallardóDepartment of Physiology, Medicine and Dentistry School, University of Valencia-INCLIVA, Center for Biomedical Network Research on Rare Diseases (CIBERER), 46010 Valencia, Spain.ORCID 0000-0003-3715-1980
Tatiana ArmeniDepartment of Odontostomatologic and Specialized Clinical Sciences, Università Politecnica delle Marche, 60131 Ancona, Italy.ORCID 0000-0003-0931-1342

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glyoxalase 2 (Glo2) is an enzyme of the glyoxalase system whose pathway parallels glycolysis and which aims to remove methylglyoxal (MGO). This study analyzed the possible additional roles of the Glo2 enzyme in breast cancer (MCF7) and non-cancer (HDF) cell lines, investigating its presence at the nuclear level and its potential involvement in cell proliferation and chemotherapy resistance. The results revealed that Glo2 is overexpressed in cancer cells, and its expression is higher during the proliferative (S and G2/M) phases of the cell cycle. The study also examined a post-translational modification (PTM) in which Glo2 could be involved, with S-glutathionylation revealing that Glo2 enhances this PTM in cancer cells both in the cytoplasm and nucleus. Inhibition of Glo2 by p-NCBG resulted in increased sensitivity to doxorubicin, a common chemotherapeutic agent. This suggests that Glo2 increases cancer cell resistance to chemotherapy, potentially through its role in regulating oxidative stress. These results highlight Glo2 as a potential therapeutic target to improve the efficacy of existing treatments.

Indexed as

Breast NeoplasmsCell ProliferationDoxorubicinDrug Resistance, NeoplasmLactoylglutathione LyaseThiolester HydrolasesCell CycleCell Line, TumorFemaleGene Expression Regulation, NeoplasticHumansHydroxyacylglutathione HydrolaseMCF-7 CellsOxidative StressProtein Processing, Post-TranslationalDoxorubicinHydroxyacylglutathione HydrolaseLactoylglutathione LyaseThiolester Hydrolasesbreast cancer cellsglyoxalase 2 (Glo2)nucleusproliferationredox metabolismS-glutathionylation

Identifiers

PMID39456676
PMCPMC11507095

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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.