Abstract
The second FMRFamide-gated Na+ channel (HtFaNaC), from Helisoma trivolvis, has been cloned. HtFaNaC has some different pharmacological properties to HaFaNaC, from Helix aspersa, which has enabled a rational approach to be made to start to identify the FMRFamide recognition site. Several chimeras were made by switching sections between the channels. The differences in sensitivity to FMRFamide, and amiloride, were assessed after expression in Xenopus oocytes, The data suggest that a recognition site for FMRFamide, and the potentiating action of amiloride, resides in a sequence of about 120 amino acids in the extracellular loop proximal to the first transmembrane segment. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
| Original language | English |
|---|---|
| Pages (from-to) | 71-74 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 489 |
| Publication status | Published - 26 Jan 2001 |
Keywords
- FaNaC
- FMRFamide recognition
- amiloride
- Na+ channel
- SODIUM-CHANNEL
- ION CHANNELS
- AMILORIDE
- CLONING
- EXPRESSION
- NEURON