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From the Department of Pharmacology, SUNY Health Science Center at Syracuse, Syracuse, New York 13210
The relative permeability sequences of the rat connexin 43 (rCx43) gap junction channel to seven
cations and chloride were examined by double whole cell patch clamp recording of single gap junction channel currents in rCx43 transfected neuroblastoma 2A (N2A) cell pairs. The measured maximal single channel
slope conductances (
j, in pS) of the junctional current-voltage relationships in 115 mM XCl were RbCl (103) 
CsCl (102) > KCl (97) > NaCl (79) LiCl (78) > TMACl (65) > TEACl (53) and for 115 mM KY were KBr (105) > KCl (97) > Kacetate (77) > Kglutamate (61). The single channel conductance-aqueous mobility relationships for
the test cations and anions were linear. However, the predicted minimum anionic and cationic conductances of
these plots did not accurately predict the rCx43 channel conductance in 115 mM KCl. Instead, the conductance
of the rCx43 channel in 115 mM KCl was accurately predicted from cationic and anionic conductance-mobility
plots by applying a mobility scaling factor Dx/Do, which depends upon the relative radii of the permeant ions to
an estimated pore radius. Relative permeabilities were determined for all of the monovalent cations and anions
tested from asymmetric salt reversal potential measurements and the Goldman-Hodgkin-Katz voltage equation.
These experiments estimate the relative chloride to potassium permeability to be 0.13. The relationship between
the relative cation permeability and hydrated radius was modeled using the hydrodynamic equation assuming a
pore radius of 6.3 ± 0.4 Å. Our data quantitatively demonstrate that the rCx43 gap junction channel is permeable
to monovalent atomic and organic cations and anions and the relative permeability sequences are consistent with
an Eisenman sequence II or I, respectively. These predictions about the rCx43 channel pore provide a useful basis
for future investigations into the structural determinants of the conductance and permeability properties of the
connexin channel pore.
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