Skip to main content

Identification of N-terminal protein acetylation and arginine methylation of the voltage-gated sodium channel in end-stage heart failure human heart

Chiva, Critina; Perez-Serra, Alexandra; Perez-Villa, Felix; Sabido, Eduard; Beltran-Alvarez, Pedro; Tarradas, Anna; Chiva, Cristina; Pérez-Serra, Alexandra; Batlle, Montserrat; Pérez-Villa, Félix; Schulte, Uwe; Sabidó, Eduard; Brugada, Ramon; Pagans, Sara

Authors

Critina Chiva

Alexandra Perez-Serra

Felix Perez-Villa

Eduard Sabido

Anna Tarradas

Cristina Chiva

Alexandra Pérez-Serra

Montserrat Batlle

Félix Pérez-Villa

Uwe Schulte

Eduard Sabidó

Ramon Brugada

Sara Pagans



Abstract

The α subunit of the cardiac voltage-gated sodium channel, Naᵥ1.5, provides the rapid sodium inward current that initiates cardiomyocyte action potentials. Here, we analyzed for the first time the post-translational modifications of Naᵥ1.5 purified from end-stage heart failure human cardiac tissue. We identified R526 methylation as the major post-translational modification of any Naᵥ1.5 arginine or lysine residue. Unexpectedly, we found that the N terminus of Naᵥ1.5 was: 1) devoid of the initiation methionine, and 2) acetylated at the resulting initial alanine residue. This is the first evidence for N-terminal acetylation in any member of the voltage-gated ion channel superfamily. Our results open the door to explore Naᵥ1.5 N-terminal acetylation and arginine methylation levels as drivers or markers of end-stage heart failure.

Publication Date Nov 1, 2014
Journal Journal of molecular and cellular cardiology
Print ISSN 0022-2828
Electronic ISSN 1095-8584
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 76
Pages 126-129
APA6 Citation Beltran-Alvarez, P., Tarradas, A., Chiva, C., Pérez-Serra, A., Batlle, M., Pérez-Villa, F., …Pagans, S. (2014). Identification of N-terminal protein acetylation and arginine methylation of the voltage-gated sodium channel in end-stage heart failure human heart. Journal of Molecular and Cellular Cardiology, 76, 126-129. https://doi.org/10.1016/j.yjmcc.2014.08.014
DOI https://doi.org/10.1016/j.yjmcc.2014.08.014
Keywords Voltage-gated sodium channel, Proteomics, Post-translational modification, N-terminal acetylation, Arginine methylation, Heart failure
Publisher URL http://www.sciencedirect.com/science/article/pii/S0022282814002612
Copyright Statement © 2014, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/
Additional Information Author's accepted manuscript of article published in: Journal of molecular and cellular cardiology, 2014, v.76

Files

Article.pdf (512 Kb)
PDF

Copyright Statement
© 2014, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/



You might also like



Downloadable Citations

;