Role of Ca2+/calmodulin-dependent protein kinase II in cardiac hypertrophy and heart failure

生物 心力衰竭 细胞生物学 钙调蛋白 心脏病学 蛋白激酶A 肌肉肥大 内科学 钙 激酶 内分泌学 医学 心肌肥大
作者
Teng Zhang
出处
期刊:Cardiovascular Research [Oxford University Press]
卷期号:63 (3): 476-486 被引量:307
标识
DOI:10.1016/j.cardiores.2004.04.026
摘要

Ca2+/calmodulin-dependent protein kinase II (CaMKII), a critical transducer of Ca2+ signaling, is a multifunctional protein kinase which can phosphorylate a wide range of substrates and regulate numerous cellular functions. The delta isoforms of CaMKII predominate in the heart and two splice variants of CaMKIIdelta, deltaB and deltaC, have been demonstrated to be present in the adult mammalian myocardium. The deltaB isoform contains a nuclear localization signal (NLS) that is absent from deltaC, and consequently, the two isoforms have different subcellular localization. Recent work from our laboratory and others has implicated CaMKII in the development of cardiac hypertrophy and heart failure. The specific roles of these CaMKII isoforms in regulating cardiac function appear to be determined by their subcellular localization. The nuclear deltaB isoform plays a key role in hypertrophic gene expression, whereas the cytoplasmic deltaC isoform can affect excitation-contraction (E-C) coupling through phosphorylation of Ca2+ regulatory proteins and may also transduce signals leading to apoptosis. In addition, the nuclear deltaB and the cytoplasmic deltaC isoforms of CaMKII are differentially regulated in pressure overload-induced cardiac hypertrophy. This review focuses on evidence that CaMKII plays an essential role in transcriptional activation associated with cardiac hypertrophy, as well as the aberrant Ca2+ handling and apoptosis that may contribute to heart failure. The hypothesis that CaMKII isoform selective activation, localization and substrate phosphorylation lead to specificity in the resultant signaling pathways is discussed.
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