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J Biol Chem, Vol. 274, Issue 6, 3711-3719, February 5, 1999
From the Thomas C. Jenkins Department of Biophysics, The Johns
Hopkins University, Baltimore, Maryland 21218
Protonated aminosulfonate compounds directly
inhibit connexin channel activity. This was demonstrated by
pH-dependent connexin channel activity in Good's pH
buffers (MES (4-morpholineethanesulfonic acid), HEPES, and TAPS
(3-{[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]amino]-1-propanesulfonic acid)) that have an aminosulfonate moiety in common and by the absence
of pH-dependent channel activity in pH buffers without an
aminosulfonate moiety (maleate, Tris, and bicarbonate). The pH-activity
relation was shifted according to the pKa of each
aminosulfonate pH buffer. At constant pH, increased aminosulfonate concentration inhibited channel activity. Taurine, a ubiquitous cytoplasmic aminosulfonic acid, had the same effect at physiological concentrations. These data raise the possibility that effects on
connexin channel activity previously attributed to protonation of
connexin may be mediated instead by protonation of cytoplasmic regulators, such as taurine. Modulation by aminosulfonates is specific
for heteromeric connexin channels containing connexin-26; it does not
occur significantly for homomeric connexin-32 channels. The
identification of taurine as a cytoplasmic compound that directly interacts with and modulates connexin channel activity is likely to
facilitate understanding of cellular modulation of connexin channels
and lead to the development of reagents for use in structure-function studies of connexin protein.
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