Evidence map›Paper›PMID 12754312›Full record

ArticleThe Journal of physiology2003

Aquaporin-1 and HCO3(-)-Cl- transporter-mediated transport of CO2 across the human erythrocyte membrane.

Michael E Blank, Heimo Ehmke

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-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

19 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Review
  3. Are Aquaporins the Missing Transmembrane Osmosensors?The Journal of membrane biology · 2015
    Review
  4. Review
  5. Article
  6. Cloning and characterization of a zebrafish homologue of human AQP1: a bifunctional water and gas channel.American journal of physiology. Regulatory, integrative and comparative physiology · 2010
    Article
  7. Article
  8. Review
  9. Aquaporins and neurodegenerative diseases.Current neuropharmacology · 2010
    Article
  10. Review
  11. Article
  12. Expression of the gas-transporting proteins, Rh B glycoprotein and Rh C glycoprotein, in the murine lung.American journal of physiology. Lung cellular and molecular physiology · 2009
    Article
  13. Relative CO2/NH3 selectivities of AQP1, AQP4, AQP5, AmtB, and RhAG.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. Article
  15. Carbon dioxide transport through membranes.The Journal of biological chemistry · 2008
    Article
  16. Article
  17. Article
  18. Does CO2 permeate through aquaporin-1?Biophysical journal · 2006
    Article
  19. What are aquaporins for?The Journal of membrane biology · 2004
    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

2 authors at 1 institution in 1 country.

Michael E BlankInstitut für Vegetative Physiologie und Pathophysiologie, Universität Hamburg, Martinistrasse 52, D-20246 Hamburg, Germany.
Heimo Ehmke
Universität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent studies have suggested that aquaporin-1 (AQP1) as well as the HCO3(-)-Cl- transporter may be involved in CO2 transport across biological membranes, but the physiological importance of this route of gas transport remained unknown. We studied CO2 transport in human red blood cell ghosts at physiological temperatures (37 degrees C). Replacement of inert with CO2-containing gas above a stirred cell suspension caused an outside-to-inside directed CO2 gradient and generated a rapid biphasic intracellular acidification. The gradient of the acidifying gas was kept small to favour high affinity entry of CO2 passing the membrane. All rates of acidification except that of the approach to physicochemical equilibrium of the uncatalysed reaction were restricted to the intracellular environment. Inhibition of carbonic anhydrase (CA) demonstrated that CO2-induced acidification required the catalytic activity of CA. Blockade of the function of either AQP1 (by HgCl2 at 65 microM) or the HCO3(-)-Cl- transporter (by DIDS at 15 microM) completely prevented fast acidification. These data indicate that, at low chemical gradients for CO2, nearly the entire CO2 transport across the red cell membrane is mediated by AQP1 and the HCO3--Cl- transporter. Therefore, these proteins may function as high affinity sites for CO2 transport across the erythrocyte membrane.

Indexed as

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAdultAquaporin 1AquaporinsBiological Transport, ActiveBlood Group AntigensCarbon DioxideCarbonic Anhydrase InhibitorsChloride-Bicarbonate AntiportersErythrocyte MembraneFluoresceinsFluorescent DyesHumansHydrogen-Ion ConcentrationIn Vitro TechniquesKinetics2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAQP1 protein, humanAquaporin 1AquaporinsBlood Group AntigensCarbon DioxideCarbonic Anhydrase InhibitorsChloride-Bicarbonate AntiportersFluoresceinsFluorescent DyesMercuric ChlorideSodium-Calcium Exchanger

Identifiers

PMID12754312
PMCPMC2343058
OpenAlexW1994914508

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.