Ion permeability of ciliary membrane vesicles isolated from Tetrahymena. Single-channel recording study on the membrane reconstituted into a planar lipid bilayer.
An ion channel in ciliary membrane vesicles isolated from Tetrahymena pyriformis NT-1 was characterized with a single-channel recording technique applied to the membrane reconstituted into a planar lipid bilayer made of soybean phospholipid. The gating of this channel is independent of membrane potential and it spends most of the time in its open-channel state. It is selective for metal cations over gluconate anion although it little distinguishes cations, Ca2+, Ba2+, Mg2+, and K+. This channel seems to be identical to the monovalent cation channel in Tetrahymena thermophila BII cilia, which was recently reported by Oosawa and Sokabe (Am. J. Physiol. 249, C177-C179, 1985). The channel conductance saturates with increasing ion concentration. The maximum value (in pS) for the single-channel conductance obtained in symmetric solutions of sufficiently high concentration is in the order of K+(212) greater than Ba2+(41) greater than Ca2+(22) greater than Mg2+(20). On the other hand, the affinity of the channel for these ions is in the reverse order.
D002118:Calcium / Q000378:metabolism; D002463:Cell Membrane Permeability; D002923:Cilia / Q000378:metabolism; D004553:Electric Conductivity; D007473:Ion Channels / Q000187:drug effects / Q000378:metabolism*; D008051:Lipid Bilayers / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism*; D013768:Tetrahymena / Q000378:metabolism*
D007473:Ion Channels; D008051:Lipid Bilayers; D008563:Membrane Lipids; D002118:Calcium