Evidence map›Paper›PMID 12096045›Full record

ReviewThe Journal of physiology2002

Transport of volatile solutes through AQP1.

Gordon J Cooper, Yuehan Zhou, Patrice Bouyer, Irina I Grichtchenko, Walter F Boron

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023
    Article
  5. Article
  6. Review
  7. Longitudinal [NeuroImage. Clinical · 2021
    Article
  8. Article
  9. Article
  10. pH sensing and regulation in cancer.Frontiers in physiology · 2013
    Review
  11. Article
  12. Review
  13. Sharpey-Schafer lecture: gas channels.Experimental physiology · 2010
    Article
  14. Article
  15. Review
  16. Aquaporin biology and nervous system.Current neuropharmacology · 2010
    Article
  17. Review
  18. Article
  19. Article
  20. Angiotensin II and hypertonicity modulate proximal tubular aquaporin 1 expression.American journal of physiology. Renal physiology · 2009
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Gordon J CooperDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026, USA.
Yuehan Zhou
Patrice Bouyer
Irina I Grichtchenko
Walter F Boron
Yale University · US

Funding

The Regulation of Renal Epithelial Cell Junction Assembly and PolarizationP01DK017433 · NIDDK · YALE UNIVERSITY · PI FORBUSH, BLISS · 1986 to 2018
$29.5M
TRAINING PROGRAM IN MOLECULAR NEUROPHYSIOLOGYT32NS007455 · NINDS · YALE UNIVERSITY · PI SIGWORTH, FREDERICK J · 1999 to 2003
$723k
REGULATION OF INTRACELLULAR PH IN RENAL PROXIMAL TUBULER01DK030344 · NIDDK · YALE UNIVERSITY · PI BORON, WALTER F. · 1986 to 2001
$660k
NIDDK NIH HHS P01 DK017433NIDDK NIH HHS P01 DK17433NIDDK NIH HHS R01 DK030344NIDDK NIH HHS R01 DK30344NINDS NIH HHS T32 NS007455NINDS NIH HHS T32 NS07455
6 · The paper itself

Abstract

For almost a century it was generally assumed that the lipid phases of all biological membranes are freely permeable to gases. However, recent observations challenge this dogma. The apical membranes of epithelial cells exposed to hostile environments, such as gastric glands, have no demonstrable permeability to the gases CO2 and NH3. Additionally, the water channel protein aquaporin 1 (AQP1), expressed at high levels in erythrocytes, can increase membrane CO2 permeability when expressed in Xenopus oocytes. Similarly, nodulin-26, which is closely related to AQP1, can act as a conduit for NH3. A key question is whether aquaporins, which are abundant in virtually every tissue that transports O2 and CO2 at high levels, ever play a physiologically significant role in the transport of small volatile molecules. Preliminary data are consistent with the hypothesis that AQP1 enhances the reabsorption of HCO3- by the renal proximal tubule by increasing the CO2 permeability of the apical membrane. Other preliminary data on Xenopus oocytes heterologously expressing the electrogenic Na+-HCO3- cotransporter (NBC), AQP1 and carbonic anhydrases are consistent with the hypothesis that the macroscopic cotransport of Na+ plus two HCO3- occurs as NBC transports Na+ plus CO3(2-) and AQP1 transports CO2 and H2O. Although data - obtained on AQP1 reconstituted into liposomes or on materials from AQP1 knockout mice - appear inconsistent with the model that AQP1 mediates substantial CO2 transport in certain preparations, the existence of unstirred layers or perfusion-limited conditions may have masked the contribution of AQP1 to CO2 permeability.

Indexed as

AnimalsAquaporin 1AquaporinsBiological TransportBlood Group AntigensCarbon DioxideGasesHumansPermeabilityWaterAQP1 protein, humanAquaporin 1AquaporinsBlood Group AntigensCarbon DioxideGasesWater

Identifiers

PMID12096045
PMCPMC2290406
OpenAlexW2067008989

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.