[Functional characteristic and molecular topology of voltage independent sodium channels].
The channel proteins so far known are transmembrane oligomers arranged in a manner that the polar residues are lining the central ion-conducting hydrophilic pore. In the last decade, electrophysiology and molecular biology studies revealed the principal similarity in the functional properties and membrane topology within a large family of sodium-conducting channels. Amiloride-sensitive channels are expressed in the apical membranes of renal epithelia. Moreover, in different mammalian cells non-voltage-gated sodium-selective channels have been recently found. According to molecular cloning of the respective DNAs and amino acid sequence analysis, epithelial channel subunits, degenerins and some other channel proteins display a significant homology in the regions forming two presumable transmembrane domains. This paper reviews some relevant data and current opinions of the superfamily of sodium-conducting cation channels.
Vedernikova
E A
EA
Institute of Cytology, Russian Academy of Sciences, St. Petersburg.
Maksimov
A V
AV
Neguliaev
Iu A
IuA
D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000502:physiology; D004594:Electrophysiology; D006801:Humans; D008969:Molecular Sequence Data; D009928:Organ Specificity; D016415:Sequence Alignment; D015222:Sodium Channels / Q000502:physiology*
D015222:Sodium Channels