Evidence map›Paper›PMID 28042826›Full record

ArticleInternational journal of molecular sciences2016

Aquaporin-Mediated Water and Hydrogen Peroxide Transport Is Involved in Normal Human Spermatozoa Functioning.

Umberto Laforenza, Giorgia Pellavio, Anna Lisa Marchetti, Claudia Omes, Federica Todaro, Giulia Gastaldi

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

44 citing papers in PubMed, 67 citations in OpenAlex.

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  15. Article
  16. Aquaporins in Reproductive System.Advances in experimental medicine and biology · 2023
    Review
  17. Article
  18. Article
  19. Relevance of Aquaporins for Gamete Function and Cryopreservation.Animals : an open access journal from MDPI · 2022
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  20. 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

6 authors at 3 institutions in 1 country.

Umberto LaforenzaDepartment of Molecular Medicine, University of Pavia, I-27100 Pavia, Italy. lumberto@unipv.it.
Giorgia PellavioDepartment of Molecular Medicine, University of Pavia, I-27100 Pavia, Italy. giorgia.pellavio@gmail.com.
Anna Lisa MarchettiScientific Direction, Fondazione IRCCS Policlinico San Matteo, I-27100 Pavia, Italy. a.marchetti@smatteo.pv.it.
Claudia OmesCenter for Reproductive Medicine, Obstetrics and Ginecology Unit, Fondazione IRCCS Policlinico San Matteo, I-27100 Pavia, Italy. claudia.omes@unipv.it.
Federica TodaroCenter for Reproductive Medicine, Obstetrics and Ginecology Unit, Fondazione IRCCS Policlinico San Matteo, I-27100 Pavia, Italy. todarofederica@gmail.com.
Giulia GastaldiDepartment of Molecular Medicine, University of Pavia, I-27100 Pavia, Italy. gastaldi@unipv.it.
University of Pavia · ITIstituti di Ricovero e Cura a Carattere Scientifico · ITPoliclinico San Matteo Fondazione · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Different aquaporins (AQPs) are expressed in human sperm cells and with a different localization. Their function has been related to cell volume control in response to the osmotic changes encountered passing from the epididymal fluid to the cervical mucus or involved in the end stage of cytoplasm removal during sperm maturation. Recently, AQPs have also shown hydrogen peroxide (H₂O₂) permeability properties. Here, we investigate the expression, localization and functioning of AQPs in human sperm cells with particular attention to their role as peroxiporins in reactive oxygen species (ROS) scavenging in both normospermic and sub-fertile human subjects. Western blotting and immunocytochemistry were used to confirm and clarify the AQPs expression and localization. Water and H₂O₂ permeability was tested by stopped flow light scattering method and by the CM-H2DCFDA (5-(and-6)-chloromethyl-2',7'-dichlorodihydro-fluorescein diacetate, acetyl ester) H₂O₂ fluorescence probe, respectively. AQP3, -7, -8, and -11 proteins were found in human sperm cells and localized in the head (AQP7), in the middle piece (AQP8) and in the tail (AQP3 and -11) in both the plasma membrane and in intracellular structures. Sperm cells showed water and H₂O₂ permeability which was reversibly inhibited by H₂O₂, heat stress and the AQP inhibitor HgCl₂. Reduced functionality was observed in patients with compromised basal semen parameters. Present findings suggest that AQPs are involved in both volume regulation and ROS elimination. The relationship between sperm number and motility and AQP functioning was also demonstrated.

Indexed as

Aquaporin 3AquaporinsBiological TransportBlotting, WesternCell MembraneCell Membrane PermeabilityHumansHydrogen PeroxideImmunohistochemistryInfertility, MaleMaleMercuric ChlorideOxidantsReactive Oxygen SpeciesSpermatozoaSperm HeadAQP11 protein, humanAQP3 protein, humanAQP7 protein, humanAquaporin 3aquaporin 8AquaporinsHydrogen PeroxideMercuric ChlorideOxidantsReactive Oxygen SpeciesWateraquaporins-7aquaporins-8oxidative stresssperm motilitysterilitywater channel

Identifiers

PMID28042826
PMCPMC5297701
OpenAlexW2562698717

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.