Sirtuin 1 regulates cardiac electrical activity by deacetylating the cardiac sodium channel

钠通道 锡尔图因 乙酰化 西妥因1 内科学 医学 心脏功能不全 心脏病学 化学 生物 基因 遗传学 心力衰竭 下调和上调 有机化学
作者
Ajit Vikram,Christopher M. Lewarchik,Jin‐Young Yoon,Asma Naqvi,Santosh Kumar,Gina Morgan,Julia S. Jacobs,Qiuxia Li,Young‐Rae Kim,Modar Kassan,Jing Liu,Mohanad Gabani,Ajay Kumar,Haider Mehdi,Xiaodong Zhu,Xiaoqun Guan,William Kutschke,Xiaoming Zhang,Ryan L. Boudreau,Shengchuan Dai,Daniel S. Matasic,Sungyup Jung,Kenneth B. Margulies,Vikas Kumar,Markus Bachschmid,Barry London,Kaikobad Irani
出处
期刊:Nature Medicine [Nature Portfolio]
卷期号:23 (3): 361-367 被引量:62
标识
DOI:10.1038/nm.4284
摘要

Intracellular trafficking of the voltage-gated cardiac Na+ channel Nav1.5 is regulated by lysine deacetylation mediated by Sirt1, thereby affecting sodium current and cardiac electrical activity. The voltage-gated cardiac Na+ channel (Nav1.5), encoded by the SCN5A gene, conducts the inward depolarizing cardiac Na+ current (INa) and is vital for normal cardiac electrical activity. Inherited loss-of-function mutations in SCN5A lead to defects in the generation and conduction of the cardiac electrical impulse and are associated with various arrhythmia phenotypes1. Here we show that sirtuin 1 deacetylase (Sirt1) deacetylates Nav1.5 at lysine 1479 (K1479) and stimulates INa via lysine-deacetylation-mediated trafficking of Nav1.5 to the plasma membrane. Cardiac Sirt1 deficiency in mice induces hyperacetylation of K1479 in Nav1.5, decreases expression of Nav1.5 on the cardiomyocyte membrane, reduces INa and leads to cardiac conduction abnormalities and premature death owing to arrhythmia. The arrhythmic phenotype of cardiac-Sirt1-deficient mice recapitulated human cardiac arrhythmias resulting from loss of function of Nav1.5. Increased Sirt1 activity or expression results in decreased lysine acetylation of Nav1.5, which promotes the trafficking of Nav1.5 to the plasma membrane and stimulation of INa. As compared to wild-type Nav1.5, Nav1.5 with K1479 mutated to a nonacetylatable residue increases peak INa and is not regulated by Sirt1, whereas Nav1.5 with K1479 mutated to mimic acetylation decreases INa. Nav1.5 is hyperacetylated on K1479 in the hearts of patients with cardiomyopathy and clinical conduction disease. Thus, Sirt1, by deacetylating Nav1.5, plays an essential part in the regulation of INa and cardiac electrical activity.

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