Anderson Mark E
University of Iowa, Carver College of Medicine, Department of Internal Medicine, 200 Hawkins Drive, E315-A1 GH, Iowa City, IA 52242 USA.
Cardiovasc Res. 2007 Mar 1;73(4):657-66. doi: 10.1016/j.cardiores.2006.12.009. Epub 2006 Dec 12.
The multifunctional Ca(2+) calmodulin-dependent protein kinase II (CaMKII) has emerged as a pro-arrhythmic signaling molecule. CaMKII can participate in arrhythmia signaling by effects on ion channel proteins, intracellular Ca(2+) uptake and release, regulation of cell death, and by activation of hypertrophic signaling pathways. The pleuripotent nature of CaMKII is reminiscent of another serine-threonine kinase, protein kinase A (PKA), which shares many of the same protein targets and is the downstream kinase most associated with beta-adrenergic receptor stimulation. The ability of CaMKII to localize and coordinate activity of multiple protein targets linked to Ca(2+) signaling set CaMKII apart from other "traditional" arrhythmia drug targets, such as ion channel proteins. This review will discuss some of the biology of CaMKII and focus on work that has been done on molecular, cellular, and whole animal models that together build a case for CaMKII as a pro-arrhythmic signal and as a potential therapeutic target for arrhythmias and structural heart disease.
多功能钙/钙调蛋白依赖性蛋白激酶II(CaMKII)已成为一种促心律失常信号分子。CaMKII可通过影响离子通道蛋白、细胞内钙摄取和释放、调节细胞死亡以及激活肥厚信号通路来参与心律失常信号传导。CaMKII的多能性让人联想到另一种丝氨酸 - 苏氨酸激酶,蛋白激酶A(PKA),它与许多相同的蛋白质靶点相互作用,并且是与β - 肾上腺素能受体刺激最相关的下游激酶。CaMKII能够定位并协调与钙信号相关的多个蛋白质靶点的活性,这使CaMKII有别于其他“传统”心律失常药物靶点,如离子通道蛋白。本综述将讨论CaMKII的一些生物学特性,并重点关注在分子、细胞和整体动物模型上所做的工作,这些工作共同证明了CaMKII作为促心律失常信号以及心律失常和结构性心脏病潜在治疗靶点的合理性。