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Science 27 November 1992:
Vol. 258. no. 5087, pp. 1477 - 1479
DOI: 10.1126/science.1279809
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Articles

Science, Vol 258, Issue 5087, 1477-1479
Copyright © 1992 by American Association for the Advancement of Science

articles

A multifunctional aqueous channel formed by CFTR

H Hasegawa, W Skach, O Baker, MC Calayag, V Lingappa, and AS Verkman

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

The cystic fibrosis gene product (CFTR) is a complex protein that functions as an adenosine 3,5-monophosphate (cAMP)-stimulated ion channel and possibly as a regulator of intracellular processes. In order to determine whether the CFTR molecule contains a functional aqueous pathway, anion, water, and urea transport were measured in Xenopus oocytes expressing CFTR. Cyclic AMP agonists induced a Cl- conductance of 94 microsiemens and an increase in water permeability of 4 x 10(-4) centimeter per second that was inhibited by a Cl- channel blocker and was dependent on anion composition. CFTR has a calculated single channel water conductance of 9 x 10(-13) cubic centimeter per second, suggesting a pore-like aqueous pathway. Oocytes expressing CFTR also showed cAMP-stimulated transport of urea but not the larger solute sucrose. Thus CFTR contains a cAMP-stimulated aqueous pore that can transport anions, water, and small solutes. The results also provide functional evidence for water movement through an ion channel.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)