Evidence map›Paper›PMID 26972385›Full record

ArticleAntioxidants & redox signaling2016

Stress Regulates Aquaporin-8 Permeability to Impact Cell Growth and Survival.

Iria Medraño-Fernandez, Stefano Bestetti, Milena Bertolotti, Gerd P Bienert, Cinzia Bottino, Umberto Laforenza, Anna Rubartelli, Roberto Sitia

Open access · hybridAbstract read
In one paragraph

Article in Antioxidants & redox signaling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

64 citing papers in PubMed, 91 citations in OpenAlex.

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  17. Aquaporins in Reproductive System.Advances in experimental medicine and biology · 2023
    Review
  18. Article
  19. Article
  20. Review

4 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 3 countries.

Iria Medraño-Fernandez1 Protein Transport and Secretion Unit, Division of Genetics and Cell Biology, IRCCS Ospedale San Raffaele/Università Vita-Salute San Raffaele , Milan, Italy .
Stefano Bestetti1 Protein Transport and Secretion Unit, Division of Genetics and Cell Biology, IRCCS Ospedale San Raffaele/Università Vita-Salute San Raffaele , Milan, Italy .
Milena Bertolotti1 Protein Transport and Secretion Unit, Division of Genetics and Cell Biology, IRCCS Ospedale San Raffaele/Università Vita-Salute San Raffaele , Milan, Italy .
Gerd P Bienert2 Metalloid Transport Group, Leibniz Institute of Plant Genetics and Crop Plant Research , Gatersleben, Germany .
Cinzia Bottino3 Department of Molecular Medicine, University of Pavia , Pavia, Italy .
Umberto Laforenza3 Department of Molecular Medicine, University of Pavia , Pavia, Italy .
Anna Rubartelli4 Cell Biology Unit, IRCCS AOU San Martino-IST , Genoa, Italy .
Roberto Sitia1 Protein Transport and Secretion Unit, Division of Genetics and Cell Biology, IRCCS Ospedale San Raffaele/Università Vita-Salute San Raffaele , Milan, Italy .
Vita-Salute San Raffaele University · ITUniversity of Pavia · ITLeibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK) · DEMartin University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

unlabelledAquaporin-8 (AQP8) allows the bidirectional transport of water and hydrogen peroxide across biological membranes. Depending on its concentration, H2O2 exerts opposite roles, amplifying growth factor signaling in physiological conditions, but causing severe cell damage when in excess. Thus, H2O2 permeability is likely to be tightly controlled in living cells.

aimsIn this study, we investigated whether and how the transport of H2O2 through plasma membrane AQP8 is regulated, particularly during cell stress.

resultsWe show that diverse cellular stress conditions, including heat, hypoxia, and ER stress, reversibly inhibit the permeability of AQP8 to H2O2 and water. Preventing the accumulation of intracellular reactive oxygen species (ROS) during stress counteracts AQP8 blockade. Once inhibition is established, AQP8-dependent transport can be rescued by reducing agents. Neither H2O2 nor water transport is impaired in stressed cells expressing a mutant AQP8, in which cysteine 53 had been replaced by serine. Cells expressing this mutant are more resistant to stress-, drug-, and radiation-induced growth arrest and death. INNOVATION AND

conclusionThe control of AQP8-mediated H2O2 transport provides a novel mechanism to regulate cell signaling and survival during stress. Antioxid. Redox Signal. 24, 1031-1044.

Indexed as

Oxidative StressAquaporinsBiological TransportCell Membrane PermeabilityCell ProliferationCell SurvivalGene ExpressionHeLa CellsHumansHydrogen PeroxideOxidation-ReductionSaccharomyces cerevisiaeWateraquaporin 8AquaporinsHydrogen PeroxideWater

Identifiers

PMID26972385
PMCPMC4931348
OpenAlexW2336978614

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.