Fractional Ca(2+) current through human neuronal alpha7 nicotinic acetylcholine receptors

Cell Calcium. 2003 Aug;34(2):205-9. doi: 10.1016/s0143-4160(03)00071-x.

Abstract

The neuronal alpha7 nicotinic acetylcholine (ACh) receptor is believed to be a highly Ca(2+) permeable ligand-gated receptor-channel. However, the contribution of Ca(2+) to cationic current generated by ACh has not yet been directly measured to date. Simultaneous fluorescence and whole-cell current measurements using the Ca(2+) indicator dye fura-2 were made in GH4C1 pituitary cells stably expressing human alpha7 receptors and the fractional Ca(2+) current (the proportion of whole-cell current carried by Ca(2+); P(f)) was determined. We report that the P(f) value was 11.4+/-1.3%. This value was significantly larger than P(f) of human L248Talpha7 receptor mutant (P(f)=6.3+/-1.0%) and of rat alpha7 receptor (P(f)=8.8+/-1.5%) both determined in transiently transfected GH4C1 cells. In our knowledge, the findings here reported indicate the human alpha7 receptors are the most Ca(2+) conductive homomeric ligand-gated receptor-channels expressed in a heterologous cell system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium / metabolism*
  • Cell Line
  • Cell Membrane Permeability
  • Fura-2
  • Humans
  • Neurons / metabolism*
  • Patch-Clamp Techniques
  • Pituitary Gland
  • Rats
  • Receptors, Nicotinic / metabolism*
  • Transfection
  • alpha7 Nicotinic Acetylcholine Receptor

Substances

  • Chrna7 protein, human
  • Chrna7 protein, rat
  • Receptors, Nicotinic
  • alpha7 Nicotinic Acetylcholine Receptor
  • Calcium
  • Fura-2