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Journal Article

Different relevance of inactivation and F468 residue in the mechanisms of hEag1 channel blockage by astemizole, imipramine and dofetilide

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Contreras-Jurado,  Constanza
Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Furini,  Simone
Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society;

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García-Ferreiro,  Rafael
Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Stühmer,  Walter
Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Pardo,  Luis A.
Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Citation

Gómez-Varela, D., Contreras-Jurado, C., Furini, S., García-Ferreiro, R., Stühmer, 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 Letters, 580(21), 5059-5066.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-2576-D
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 asternizole and dofetilide but not imipramine, suggesting different binding sites in the channel. F468C mutation increased IC50 for asternizole 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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.