Evidence map›Paper›PMID 40855238›Full record

ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2025

ABCC1 promotes GSH-dependent iron transport and resistance to Fe(II) and Cu(II) chelators.

Anikó Gaál, Lúcia Torma, Éva Bakos, Katalin Német, Peter Kregsamer, Christina Streli, Miklós Péter Mohai, Elina Üveges, Julia H Bormio Nunes, Petra Heffeter and 2 more

Abstract read
In one paragraph

Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 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. 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

12 authors.

Anikó Gaál *Biological Nanochemistry Research Group, Institute of Materials and Environmental Chemistry, HUN-REN Research Centre for Natural Sciences, Budapest, Hungary.
Lúcia Torma *Doctoral School of Pharmaceutical Sciences, Semmelweis University, Budapest, Hungary.
Éva BakosInstitute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences, Budapest, Hungary. bakos.eva@ttk.hu.
Katalin NémetInstitute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences, Budapest, Hungary.
Peter KregsamerInstitute of Atomic and Subatomic Physics, Vienna University of Technology, Vienna, Austria.
Christina StreliInstitute of Atomic and Subatomic Physics, Vienna University of Technology, Vienna, Austria.
Miklós Péter MohaiInstitute of Materials and Environmental Chemistry, HUN-REN Research Centre for Natural Sciences, Budapest, Hungary.
Elina ÜvegesDoctoral School of Pharmaceutical Sciences, Semmelweis University, Budapest, Hungary.
Julia H Bormio NunesCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.
Petra HeffeterCenter for Cancer Research, Medical University of Vienna, Vienna, Austria.
Gergely Szakács *Institute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences, Budapest, Hungary. gergely.szakacs@meduniwien.ac.at.
Norbert Szoboszlai *Integrative Health and Environmental Analysis Research Laboratory, Institute of Chemistry, ELTE Eötvös Loránd University, Budapest, Hungary. norbert.szoboszlai@ttk.elte.hu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Therapy resistance is a major challenge in cancer treatment, with multidrug resistance (MDR) being a well-characterized phenomenon wherein cancer cells develop resistance not only to the administered drug but also to structurally diverse compounds. Metal chelators, including quinolines and thiosemicarbazones, have shown broad antitumor activity and potential in overcoming MDR by modulating metal metabolism. However, predicting whether chelators increase or decrease toxicity in MDR cells remains complex, especially as chelator-metal complexes may become substrates for ATP-binding cassette (ABC) transporters, leading to resistance or hypersensitivity. In this study, we developed cell lines with comparable expression levels of the three major MDR ABC transporters (ABCB1, ABCC1, and ABCG2). Our findings demonstrated distinct transporter-specific influences on chelator toxicity. Cells expressing ABCC1 displayed significant resistance to thiosemicarbazones (Dp44mT, COTI-2, DpC) in both their metal-free and metal-bound forms. Vesicular transport assays further demonstrated that ABCC1 actively transports the Fe-GSH complex, formed under physiological glutathione levels, indicating its role in regulating the labile iron pool and reducing intracellular iron toxicity. These findings underscore the importance of transporter-chelator interactions in shaping drug resistance and sensitivity and highlight the intricate roles of ABC transporters in modulating chelator activity.

Indexed as

ATP-Binding Cassette, Sub-Family C ProteinsChelating AgentsCopperFerrous CompoundsGlutathioneIronIron Chelating AgentsCell Line, TumorDrug Resistance, NeoplasmHumansThiosemicarbazonesATP-Binding Cassette, Sub-Family C ProteinsChelating AgentsCopperFerrous CompoundsGlutathioneIronIron Chelating Agentsmultidrug resistance-associated protein 1ThiosemicarbazonesABC transportersAnticancer chelatorsCollateral sensitivityIron transportMultidrug resistance

Identifiers

PMID40855238
PMCPMC12686069

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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.