Evidence map›Paper›PMID 22174795›Full record

ArticlePloS one2011

Functional and transcriptional induction of aquaporin-1 gene by hypoxia; analysis of promoter and role of Hif-1α.

Irene Abreu-Rodríguez, Rocío Sánchez Silva, Ana Paula Martins, Graça Soveral, Juan José Toledo-Aral, José López-Barneo, Miriam Echevarría

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

48 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Aquaporin-mediated dysregulation of cell migration in disease states.Cellular and molecular life sciences : CMLS · 2023
    Review
  11. The Role of Propranolol as a Repurposed Drug in Rare Vascular Diseases.International journal of molecular sciences · 2022
    Review
  12. Review
  13. Review
  14. Aquaporins in Cancer Biology.Frontiers in oncology · 2022
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Anti-Angiogenic Properties of Ginsenoside Rg3.Molecules (Basel, Switzerland) · 2020
    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

7 authors at 6 institutions in 2 countries.

Irene Abreu-RodríguezDepartamento de Fisiología Médica y Biofísica, Instituto de Biomedicina de Sevilla, Hospital Universitario Virgen del Rocío, CSIC, Universidad de Sevilla, Seville, Spain.
Rocío Sánchez Silva
Ana Paula Martins
Graça Soveral
Juan José Toledo-Aral
José López-Barneo
Miriam Echevarría
Hospital Universitario Virgen del Rocío · ESBiomedical Research Networking Center on Neurodegenerative Diseases · ESInstituto de Biomedicina de Sevilla · ESRede de Química e Tecnologia · PTUniversidad de Sevilla · ESUniversity of Lisbon · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aquaporin-1 (AQP1) is a water channel that is highly expressed in tissues with rapid O(2) transport. It has been reported that this protein contributes to gas permeation (CO(2), NO and O(2)) through the plasma membrane. We show that hypoxia increases Aqp1 mRNA and protein levels in tissues, namely mouse brain and lung, and in cultured cells, the 9L glioma cell line. Stopped-flow light-scattering experiments confirmed an increase in the water permeability of 9L cells exposed to hypoxia, supporting the view that hypoxic Aqp1 up-regulation has a functional role. To investigate the molecular mechanisms underlying this regulatory process, transcriptional regulation was studied by transient transfections of mouse endothelial cells with a 1297 bp 5' proximal Aqp1 promoter-luciferase construct. Incubation in hypoxia produced a dose- and time-dependent induction of luciferase activity that was also obtained after treatments with hypoxia mimetics (DMOG and CoCl(2)) and by overexpressing stabilized mutated forms of HIF-1α. Single mutations or full deletions of the three putative HIF binding domains present in the Aqp1 promoter partially reduced its responsiveness to hypoxia, and transfection with Hif-1α siRNA decreased the in vitro hypoxia induction of Aqp1 mRNA and protein levels. Our results indicate that HIF-1α participates in the hypoxic induction of AQP1. However, we also demonstrate that the activation of Aqp1 promoter by hypoxia is complex and multifactorial and suggest that besides HIF-1α other transcription factors might contribute to this regulatory process. These data provide a conceptual framework to support future research on the involvement of AQP1 in a range of pathophysiological conditions, including edema, tumor growth, and respiratory diseases.

Indexed as

Promoter Regions, GeneticTranscriptional ActivationTranscription, GeneticAnimalsAquaporin 1Binding SitesCell HypoxiaCell Line, TumorCell Membrane PermeabilityDown-RegulationHypoxia-Inducible Factor 1, alpha SubunitMiceProtein StabilityRatsRNA, MessengerSequence DeletionAquaporin 1Hypoxia-Inducible Factor 1, alpha SubunitRNA, MessengerWater

Identifiers

PMID22174795
PMCPMC3233559
OpenAlexW2168736084

What OpenQuestion 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 OpenQuestion graph.