Functional characterization of canine connexin45.
Three gap junctional proteins have been identified in canine ventricular myocytes: connexin 43 (Cx43), connexin 45 (Cx45), and connexin 40 (Cx40). We have characterized the functional properties of canine Cx45 and examined how Cx45 functionally interacts with Cx43 in Xenopus oocyte pairs. Homotypic pairs expressing Cx45 were well coupled. Heterotypic pairs composed of Cx45 paired with either Cx43 or Cx38 also developed high levels of conductance. Junctional currents in the heterotypic pairs displayed a highly asymmetrical voltage dependence. The kinetics and steadystate voltage dependence of the heterotypic channels more closely resembled those of the Cx45 channels when the Cx45 cRNA-injected cell was relatively negative suggesting that the Cx45 connexin closes for relative negativity at the cytoplasmic end of the channel. We also show that homotypic and heterotypic channels composed of Cx45 and Cx43 exhibit differences in pHi sensitivity.
Steiner
E
E
Department of Pharmacology, Columbia University, New York, NY 10032, USA.
Ebihara
L
L
D000818:Animals; D018031:Connexin 43 / Q000378:metabolism; D017630:Connexins / Q000378:metabolism*; D004285:Dogs; D004594:Electrophysiology; D006863:Hydrogen-Ion Concentration; D015640:Ion Channel Gating; D011233:Precipitin Tests; D011994:Recombinant Proteins / Q000378:metabolism; D014981:Xenopus
D018031:Connexin 43; D017630:Connexins; D011994:Recombinant Proteins; C082920:connexin 45