ArticlePflugers Archiv : European journal of physiology2005
Domain near TM1 influences agonist and antagonist responses of peptide-gated Na+ channels.
Article in Pflugers Archiv : European journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The trial behind it
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Who cites it
8 citing papers in PubMed.
- A conserved peptide-binding pocket in HyNaC/ASIC ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Aromatic amino acids in the finger domain of the FMRFamide-gated NaPflugers Archiv : European journal of physiology · 2023Article
- The FMRF-NH2 gated sodium channel of Biomphalaria glabrata: Localization and expression following infection by Schistosoma mansoni.PLoS neglected tropical diseases · 2023Article
- Comparative analysis defines a broader FMRFamide-gated sodium channel family and determinants of neuropeptide sensitivity.The Journal of biological chemistry · 2022Article
- The nonproton ligand of acid-sensing ion channel 3 activates mollusk-specific FaNaC channels via a mechanism independent of the native FMRFamide peptide.The Journal of biological chemistry · 2017Article
- Exploration of the Peptide Recognition of an Amiloride-sensitive FMRFamide Peptide-gated Sodium Channel.The Journal of biological chemistry · 2016Article
- Insight into DEG/ENaC channel gating from genetics and structure.Physiology (Bethesda, Md.) · 2012Review
- Heterologous expression of the invertebrate FMRFamide-gated sodium channel as a mechanism to selectively activate mammalian neurons.Neuroscience · 2008Article
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
A molecular biological approach was used to analyse the importance of different amino acids for ligand activation and for determining the action of amiloride on peptide- (Phe-Met-Arg-Phe-NH(2), FMRFamide)-gated Na(+) channels, members of the degenerin/epithelial Na channel (DEG/ENaC) family. Amiloride is a low-affinity blocker of most DEG/ENa channels, but has an unusual enhancing effect on responses of some of them. Chimeras were expressed in Xenopus oocytes and studied electrophysiologically. Differences in properties of channels from Helix aspersa and Helisoma trivolvis highlighted a sequence of 50 residues of the extracellular domain, near the first transmembrane segment (TM1), that affected sensitivity to FMRFamide, and whether amiloride blocked or enhanced the response to FMRFamide. Comparisons of chimeras prepared from H. aspersa and the extracellular domains of two other species, Aplysia californica and Lymnaea stagnalis and the preparation of further constructs, showed that amino acids 128-134 in the H. aspersa sequence are important in determining the predominant effect of amiloride and influencing the EC(50) of FMRFamide. The results also showed that amino acids in this region are influenced by amino acids in other regions of the extracellular domain so as to affect not only the magnitude of responses, but also their time course and desensitisation.
Indexed as
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15843991What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.