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J Biol Chem, Vol. 273, Issue 5, 2808-2816, January 30, 1998
From the Intercellular connexin channels (gap junction
channels) have long been thought to mediate molecular signaling between
cells, but the nature of the signaling has been unclear. This study
shows that connexin channels from native tissue have selective
permeabilities, partially based on pore diameter, that discriminate
among cytoplasmic second messenger molecules. Permeability was assessed
by measurement of selective loss/retention of tracers from liposomes
containing reconstituted connexin channels. The tracers employed were
tritiated cyclic nucleotides and a series of oligomaltosaccharides
derivatized with a small uncharged fluorescent moiety. The data define
different size cut-off limits for permeability through homomeric
connexin-32 channels and through heteromeric connexin-32/connexin-26
channels. Connexin-26 contributes to a narrowed pore. Both cAMP and
cGMP were permeable through the homomeric connexin-32 channels. cAMP was permeable through only a fraction of the heteromeric channels. Surprisingly, cGMP was permeable through a substantially greater fraction of the heteromeric channels than was cAMP. The data suggest that isoform stoichiometry and/or arrangement within a connexin channel
determines whether cyclic nucleotides can permeate, and which ones.
This is the first evidence for connexin-specific selectivity among
biological signaling molecules.
Isoform Composition of Connexin Channels Determines Selectivity
among Second Messengers and Uncharged Molecules
,
, and
Thomas C. Jenkins Department of Biophysics,
Johns Hopkins University, Baltimore, Maryland 21218, the
§ Department of Enzyme Technology, Gesellschaft für
Biotechnologische Forschung, Mascheroder Weg 1, 38124 Braunschweig,
Germany, and the Department of Biochemistry, Yeungnam
University, 214-1 Daedong, Kyoungsan, Republic of Korea
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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V. Abraham, M. L. Chou, K. M. DeBolt, and M. Koval Phenotypic control of gap junctional communication by cultured alveolar epithelial cells Am J Physiol Lung Cell Mol Physiol, May 1, 1999; 276(5): L825 - L834. [Abstract] [Full Text] [PDF]
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D. Y. Kim, Y. Kam, S. K. Koo, and C. O. Joe Gating Connexin 43 Channels Reconstituted in Lipid Vesicles by Mitogen-activated Protein Kinase Phosphorylation J. Biol. Chem., February 26, 1999; 274(9): 5581 - 5587. [Abstract] [Full Text] [PDF]
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C. G. Bevans and A. L. Harris Regulation of Connexin Channels by pH. DIRECT ACTION OF THE PROTONATED FORM OF TAURINE AND OTHER AMINOSULFONATES J. Biol. Chem., February 5, 1999; 274(6): 3711 - 3719. [Abstract] [Full Text] [PDF]
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C. G. Bevans and A. L. Harris Direct High Affinity Modulation of Connexin Channel Activity by Cyclic Nucleotides J. Biol. Chem., February 5, 1999; 274(6): 3720 - 3725. [Abstract] [Full Text] [PDF]
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