@article { , title = {Identification of N-terminal protein acetylation and arginine methylation of the voltage-gated sodium channel in end-stage heart failure human heart}, 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.}, doi = {10.1016/j.yjmcc.2014.08.014}, eissn = {1095-8584}, issn = {0022-2828}, journal = {Journal of molecular and cellular cardiology}, pages = {126-129}, publicationstatus = {Published}, publisher = {Elsevier}, url = {https://hull-repository.worktribe.com/output/412671}, volume = {76}, keyword = {Health and Health Inequalities, Voltage-gated sodium channel, Proteomics, Post-translational modification, N-terminal acetylation, Arginine methylation, Heart failure}, year = {2014}, author = {Beltran-Alvarez, Pedro and Tarradas, Anna and Chiva, Cristina and Pérez-Serra, Alexandra and Batlle, Montserrat and Pérez-Villa, Félix and Schulte, Uwe and Sabidó, Eduard and Brugada, Ramon and Pagans, Sara} }