Evidence map›Paper›PMID 39578074›Full record

ArticleLife science alliance2025

Membrane transporters modulating the toxicity of arsenic, cadmium, and mercury in human cells.

Andrè Ferdigg, Ann-Katrin Hopp, Gernot Wolf, Giulio Superti-Furga

Abstract read
In one paragraph

Article in Life science alliance, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. New insights on the role of some biometals in mancozeb induced hematological and hepatorenal toxicity in rats and the protective effect of naringin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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.

Andrè FerdiggCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.ORCID 0000-0002-9382-0985
Ann-Katrin HoppCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.ORCID 0000-0002-2594-4070
Gernot WolfCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria.ORCID 0000-0002-3943-8662
Giulio Superti-FurgaCeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria gsuperti@cemm.oeaw.ac.at.ORCID 0000-0002-0570-1768

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Non-essential metals are extremely toxic to living organisms, posing significant health risks, particularly in developing nations where they are a major contributor to illness and death. Although their toxicity is widely acknowledged, the mechanisms by which they are regulated within human cells remain incompletely understood. Specifically, the role of membrane transporters in mediating heavy metal toxicity is not well comprehended. Our study demonstrates how specific transporters can modulate the toxicity of cadmium, mercury, and the metalloid arsenic in human cells. Using CRISPR/Cas9 loss-of-function screens, we found that the multidrug resistance protein MRP1/ABCC1 provided protection against toxicity induced by arsenic and mercury. In addition, we found that SLC39A14 and SLC30A1 increased cellular sensitivity to cadmium. Using a reporter cell line to monitor cellular metal accumulation and performing a cDNA gain-of-function screen, we were able to clarify the function of SLC30A1 in controlling cadmium toxicity through the modulation of intracellular zinc levels. This transporter-wide approach provides new insights into the complex roles of membrane transporters in influencing the toxicity of arsenic, cadmium, and mercury in human cell lines.

Indexed as

ArsenicATP-Binding Cassette, Sub-Family C ProteinsCadmiumMercuryCation Transport ProteinsCell LineCRISPR-Cas SystemsHEK293 CellsHumansMembrane Transport ProteinsZincArsenicATP-Binding Cassette, Sub-Family C ProteinsCadmiumCation Transport ProteinsMembrane Transport ProteinsMercurymultidrug resistance-associated protein 1SLC30A1 protein, humanSLC39A14 protein, humanZinc

Identifiers

PMID39578074
PMCPMC11584324

What Socratic 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 Socratic graph.