English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  Different relevance of inactivation and F468 residue in the mechanisms of hEag1 channel blockage by astemizole, imipramine and dofetilide

Gomez-Varela, D., Contreras-Jurado, C., Furini, S., Garcia-Ferreiro, R., Stuhmer, W., & Pardo, L. A. (2006). Different relevance of inactivation and F468 residue in the mechanisms of hEag1 channel blockage by astemizole, imipramine and dofetilide. FEBS Lett, 580(21), 5059-66. doi:10.1016/j.febslet.2006.08.030.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/21.11116/0000-0009-F221-0 Version Permalink: https://hdl.handle.net/21.11116/0000-0009-F222-F
Genre: Journal Article

Files

show Files

Locators

show
hide
Locator:
https://www.ncbi.nlm.nih.gov/pubmed/16949586 (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Gomez-Varela, D.1, Author
Contreras-Jurado, C.1, Author
Furini, S.1, Author
Garcia-Ferreiro, R.1, Author
Stuhmer, W.1, Author
Pardo, L. A.1, Author
Affiliations:
1Max Planck Society, ou_persistent13              

Content

show
hide
Free keywords: Astemizole/chemistry/*pharmacology Benzopyrans/pharmacology Ether-A-Go-Go Potassium Channels/*metabolism Humans Imipramine/*pharmacology Ion Channel Gating/*drug effects Models, Molecular Phenethylamines/*pharmacology Piperidines/pharmacology Point Mutation/*genetics Potassium Channel Blockers/*pharmacology Structure-Activity Relationship Sulfonamides/*pharmacology
 Abstract: The relevance of a point mutation at the C-terminal end of the S6 helix (F468) and the introduction of C-type inactivation in the blockage of hEag1 channels by astemizole, imipramine and dofetilide was tested. C-type inactivation decreased block by astemizole and dofetilide but not imipramine, suggesting different binding sites in the channel. F468C mutation increased IC(50) for astemizole and imipramine but in contrast to HERG channels, only slightly for dofetilide. Together with measurements on recovery of blocking, our observations indicate that the mechanism of hEag1 blockage by each of these drugs is different, and suggest relevant structural differences between hEag1 and HERG channels.

Details

show
hide
Language(s):
 Dates: 2006-09-182006-08-28
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: 16949586
DOI: 10.1016/j.febslet.2006.08.030
ISSN: 0014-5793 (Print) 0014-5793 (Linking)
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: FEBS Lett
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 580 (21) Sequence Number: - Start / End Page: 5059 - 66 Identifier: -