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Originally published In Press as doi:10.1074/jbc.M511235200 on December 22, 2005
J. Biol. Chem., Vol. 281, Issue 10, 6673-6681, March 10, 2006
Selective Permeability of Different Connexin Channels to the Second Messenger Cyclic AMP*
Peter Bedner 1,
Heiner Niessen ,
Benjamin Odermatt ,
Markus Kretz ,
Klaus Willecke 2, and
Hartmann Harz
From the
Institut für Genetik, Abteilung Molekulargenetik, Universität Bonn, Römerstrasse 164, 53117 Bonn and BioImaging Zentrum der Ludwig-Maximilians-Universität München, Am Klopferspitz 19, 82152 Martinsried, Germany
Gap junctions are intercellular conduits that are formed in vertebrates by connexin proteins and allow diffusion exchange of intracellular ions and small molecules. At least 20 different connexin genes in the human and mouse genome are cell-type specifically expressed with overlapping expression patterns. A possible explanation for this diversity could be different permeability of biologically important molecules, such as second messenger molecules. We have recently demonstrated that cyclic nucleotide-gated channels can be used to quantify gap junction-mediated diffusion of cyclic AMP. Using this method we have compared the relative permeability of gap junction channels composed of connexin 26, 32, 36, 43, 45, or 47 proteins toward the second messenger cAMP. Here we show that cAMP permeates through the investigated connexin channels with up to 30-fold different efficacy. Our results suggest that intercellular cAMP signaling in different cell types can be affected by the connexin expression pattern.
Received for publication, October 16, 2005
, and in revised form, December 15, 2005.
* This work was supported in part by grants of the Deutsche Forschungsgemeinschaft (SFB 284, C1, and Wi 270/26-1,2), by European Commission FP6 Integrated Project EuroHear LSHG-CT-20054-512063, and by Funds of the Chemical Industry (to K. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 Recipient of a stipend of the Graduiertenkolleg Funktionelle Proteindomänen. Present address: Johns Hopkins University School of Medicine, Dept. of Biomedical Engineering, 720 Rutland Ave., Baltimore, MD 21205.
2 To whom correspondence should be addressed: Institut für Genetik, Universität Bonn, Römerstr. 164, 53117 Bonn, Germany. Tel.: 49-228-734210; Fax: 49-228-734263; E-mail: genetik{at}uni-bonn.de.

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Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
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