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Am J Physiol Cell Physiol 274: C799-C809, 1998;
0363-6143/98 $5.00
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Vol. 274, Issue 3, C799-C809, March 1998

Electrodiffusional ATP movement through the cystic fibrosis transmembrane conductance regulator

Horacio F. Cantiello1,2, George R. Jackson Jr.2, Claudio F. Grosman3, Adriana G. Prat1,2, Steven C. Borkan4, Yihan Wang4, Ignacio L. Reisin3, Catherine R. O'Riordan5, and Dennis A. Ausiello1,2

1 Renal Unit, Massachusetts General Hospital East, Charlestown 02129; 2 Department of Medicine, Harvard Medical School, Boston 02115; 4 Renal Section, Boston Medical Center, Boston 02118; 5 Genzyme Corporation, Framingham, Massachusetts 01701; and 3 Departamento de Química General e Inorgánica, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, 1113 Buenos Aires, Argentina

Expression of the cystic fibrosis transmembrane conductance regulator (CFTR), and of at least one other member of the ATP-binding cassette family of transport proteins, P-glycoprotein, is associated with the electrodiffusional movement of the nucleotide ATP. Evidence directly implicating CFTR expression with ATP channel activity, however, is still missing. Here it is reported that reconstitution into a lipid bilayer of highly purified CFTR of human epithelial origin enables the permeation of both Cl- and ATP. Similar to previously reported data for in vivo ATP currents of CFTR-expressing cells, the reconstituted channels displayed competition between Cl- and ATP and had multiple conductance states in the presence of Cl- and ATP. Purified CFTR-mediated ATP currents were activated by protein kinase A and ATP (1 mM) from the "intracellular" side of the molecule and were inhibited by diphenylamine-2-carboxylate, glibenclamide, and anti-CFTR antibodies. The absence of CFTR-mediated electrodiffusional ATP movement may thus be a relevant component of the pleiotropic cystic fibrosis phenotype.

adenosine 5'-triphosphate channels; adenosine 5'-triphosphate-binding cassette transporters; nucleotide transport


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