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Biophys J, October 2000, p. 1954-1966, Vol. 79, No. 4
Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York 10461 USA
Gap junctions formed of connexin46 (Cx46) and connexin50
(Cx50) in lens fiber cells are crucial for maintaining lens
transparency. We determined the functional properties of homotypic
Cx46, heterotypic Cx46/Cx50, and heteromeric Cx46/Cx50 channels in a
communication-deficient neuroblastoma (N2A) cell line, using dual
whole-cell recordings. N2A cultures were stably and/or transiently
transfected with Cx46, Cx50, and green fluorescent protein (EGFP). The
macroscopic voltage sensitivity of homotypic Cx46 conformed to the
two-state model (Boltzmann parameters:
Gmin = 0.11, V0 = ± 48.1 mV, gating charge = 2). Cx46 single channels showed a main-state conductance of 140 ± 8 pS and multiple subconductance states ranging from 
10 pS to 60 pS.
Conservation of homotypic properties in heterotypic Cx46/Cx50 cell
pairs allowed the determination of a positive relative gating polarity
for the dominant gating mechanisms in Cx46 and Cx50. Observed gating
properties were consistent with a second gating mechanism in Cx46
connexons. Moreover, rectification was observed in heterotypic cell
pairs. Some cell pairs in cultures simultaneously transfected with Cx46
and Cx50 exhibited junctional properties not observed in other
preparations, suggesting the formation of heteromeric channels. We
conclude that different combinations of Cx46 and Cx50 within gap
junction channels lead to unique biophysical properties.
Biophys J, October 2000, p. 1954-1966, Vol. 79, No. 4
© 2000 by the Biophysical Society 0006-3495/00/10/1954/13 $2.00
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