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- W2034259506 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." @default.
- W2034259506 created "2016-06-24" @default.
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- W2034259506 date "1996-01-01" @default.
- W2034259506 modified "2023-10-16" @default.
- W2034259506 title "Adaptation cardiovasculaire du transplanté cardiaque à l'exercice dynamique" @default.
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- W2034259506 doi "https://doi.org/10.1016/0765-1597(96)81274-3" @default.
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