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A multifunctional aqueous channel formed by CFTR.

H Hasegawa1, W Skach, O Baker

  • 1Department of Medicine, University of California, San Francisco 94143-0532.

Science (New York, N.Y.)
|November 27, 1992
PubMed
Summary
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The cystic fibrosis transmembrane conductance regulator (CFTR) protein facilitates cAMP-stimulated transport of anions, water, and urea. This study confirms CFTR contains a functional aqueous pore, providing evidence for water movement through ion channels.

Area of Science:

  • Molecular Biology
  • Physiology
  • Biophysics

Background:

  • The cystic fibrosis gene product (CFTR) is a cAMP-stimulated ion channel.
  • Its role in regulating intracellular processes and its potential for aqueous transport are not fully understood.

Purpose of the Study:

  • To determine if the CFTR molecule possesses a functional aqueous pathway.
  • To investigate the transport of anions, water, and urea through CFTR.

Main Methods:

  • Transport assays were performed using Xenopus oocytes expressing CFTR.
  • Measurements included anion, water, and urea permeability.
  • The effects of cAMP agonists and Cl- channel blockers were assessed.

Main Results:

Related Experiment Videos

  • cAMP stimulation induced significant Cl- conductance and increased water permeability in CFTR-expressing oocytes.
  • Water permeability was dependent on anion composition and inhibited by a Cl- channel blocker.
  • CFTR demonstrated cAMP-stimulated transport of urea but not sucrose, indicating a pore-like pathway.

    • Conclusions:

    • CFTR functions as a cAMP-stimulated aqueous pore capable of transporting anions, water, and small solutes like urea.
    • These findings provide functional evidence for water movement through an ion channel.
    • The study elucidates the transport capabilities of the CFTR protein.