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Expression and Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein in Saccharomyces cerevisiae
14:56

Expression and Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein in Saccharomyces cerevisiae

Published on: March 10, 2012

Electrodiffusional ATP movement through the cystic fibrosis transmembrane conductance regulator

H F Cantiello1, G R Jackson, C F Grosman

  • 1Renal Unit, Massachusetts General Hospital East, Charlestown, Massachusetts 02129, USA.

The American Journal of Physiology
|April 8, 1998
PubMed

Insights

Cystic fibrosis transmembrane conductance regulator (CFTR) facilitates ATP and chloride ion transport across cell membranes. This discovery may explain cystic fibrosis symptoms.

Area of Science:

  • Molecular biology
  • Cell physiology
  • Ion channel function

Background:

  • Cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette transporter.
  • CFTR expression is linked to ATP movement, but direct evidence for CFTR's role in ATP channel activity is lacking.

Purpose of the Study:

  • To investigate the direct role of purified CFTR in ATP permeation.
  • To characterize the properties of CFTR-mediated ATP transport.

Main Methods:

  • Reconstitution of highly purified human epithelial CFTR into lipid bilayers.
  • Electrophysiological recordings to measure ion and ATP flux.
  • Biochemical assays to study channel modulation.

Main Results:

  • Reconstituted CFTR channels allow permeation of both chloride (Cl-) and adenosine triphosphate (ATP).
  • CFTR-mediated ATP currents exhibit competition with Cl- and multiple conductance states.
  • ATP currents are activated by protein kinase A and ATP, and inhibited by specific blockers and antibodies.

Conclusions:

  • Purified CFTR directly mediates electrodiffusional ATP movement.
  • This CFTR-dependent ATP transport mechanism may contribute to the diverse symptoms of cystic fibrosis.

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