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Am J Physiol Cell Physiol 296: C250-C255, 2009. First published October 22, 2008; doi:10.1152/ajpcell.00433.2008
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MEMBRANE TRANSPORTERS, ION CHANNELS, AND PUMPS

A permeant regulating its permeation pore: inhibition of pannexin 1 channels by ATP

Feng Qiu and Gerhard Dahl

Department of Physiology and Biophysics, University of Miami, School of Medicine, Miami, Florida

Submitted 22 August 2008 ; accepted in final form 15 October 2008

Pannexin 1 forms a large membrane channel that, based on its biophysical properties and its expression pattern, is a prime candidate to represent an ATP release channel. Pannexin 1 channel activity is potentially deleterious for cells as indicated by its involvement in the P2X7 death complex. Here we describe a negative feedback loop controlling pannexin 1 channel activity. ATP, permeant to pannexin 1 channels, was found to inhibit its permeation pathway when applied extracellularly to oocytes expressing pannexin 1 exogenously. ATP analogues, including benzoylbenzoyl-ATP, suramin, and brilliant blue G were even more effective inhibitors of pannexin 1 currents than ATP. These compounds also attenuated the uptake of dyes by erythrocytes, which express pannexin 1. The rank order of the compounds in attenuation of pannexin 1 currents was similar to their binding affinities to the P2X7 receptor, except that receptor agonists and antagonists both were inhibitory to the channel. Mutational analysis identified R75 in pannexin 1 to be critical for ATP inhibition of pannexin 1 currents.

ATP release; brilliant blue G; benzylbenzoyl-ATP; P2X7 receptor; erythrocyte


Address for reprint requests and other correspondence: G. Dahl, Dept. of Physiology and Biophysics, Univ. of Miami School of Medicine, PO Box 016430, Miami, FL 33101 (E-mail: gdahl{at}miami.edu)




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G. R. Dubyak
Both sides now: multiple interactions of ATP with pannexin-1 hemichannels. Focus on "A permeant regulating its permeation pore: inhibition of pannexin 1 channels by ATP"
Am J Physiol Cell Physiol, February 1, 2009; 296(2): C235 - C241.
[Full Text] [PDF]


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