[Functional characteristic and molecular topology of voltage independent sodium channels]

Tsitologiia. 1999;41(8):658-66.
[Article in Russian]

Abstract

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.

Publication types

  • English Abstract
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Membrane / physiology
  • Electrophysiology
  • Humans
  • Molecular Sequence Data
  • Organ Specificity
  • Sequence Alignment
  • Sodium Channels / physiology*

Substances

  • Sodium Channels