Learn More
Amiloride-sensitive Na+ channels constitute a new class of proteins known as the ENaC-Deg family of ion channels. All members in this family share a common protein structure but differ in their ion selectivity, their affinity for the blocker amiloride, and in their gating mechanisms. These channels are expressed in many tissues of invertebrate and(More)
The epithelial sodium channel (ENaC) provides the rate-limiting step in the reabsorption of sodium by many epithelia. The number of channels at the cell surface is tightly regulated; most cells express only a few channels. We have examined the biosynthesis and cell surface expression of ENaC in Xenopus oocytes. The subunits of ENaC are readily synthesized(More)
With two new monoclonal antibodies and flow cytometry, we defined three subpopulations among B cells expressing binding sites for peanut agglutinin (i.e., B cells of the germinal center). On monoclonal antibody (5B5) binds globotriaosyl ceramide. The B lymphocytes binding 5B5 have binding sites for peanut agglutinin on the surface and express only small(More)
The epithelial sodium channel (ENaC) is the prototype of a new family of ion channels known as the Mec-ENaC superfamily. This new family of proteins are involved in a wide variety of functions that range from maintenance of sodium homeostasis to transduction of mechanical stimuli and nociceptive pain by specialized neurons. They show distinct tissue- and(More)
We have examined the effect of extracellular protons on the activity of epithelial sodium channels (ENaCs). We found that alphabeta channels, but not alphabetagamma or alphagamma channels, are inhibited by low extracellular pH. External protons induced short and long closed states that markedly decreased the open probability of alphabeta channels. External(More)
The epithelial sodium channel (ENaC) is the prototype of a new class of ion channels known as the ENaC/Deg family. The hallmarks of ENaC are a high selectivity for Na(+), block by amiloride, small conductance, and slow kinetics that are voltage-independent. We have investigated the contribution of the second hydrophobic domain of each of the homologous(More)
  • 1