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The delta isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload
Journal article   Open access   Peer reviewed

The delta isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload

Johannes Backs, Thea Backs, Stefan Neef, Michael M Kreusser, Lorenz H Lehmann, David M Patrick, Chad E Grueter, Xiaoxia Qi, James A Richardson, Joseph A Hill, …
Proceedings of the National Academy of Sciences - PNAS, Vol.106(7), pp.2342-2347
02/17/2009
DOI: 10.1073/pnas.0813013106
PMCID: PMC2650158
PMID: 19179290
url
https://doi.org/10.1073/pnas.0813013106View
Published (Version of record) Open Access

Abstract

Acute and chronic injuries to the heart result in perturbation of intracellular calcium signaling, which leads to pathological cardiac hypertrophy and remodeling. Calcium/calmodulin-dependent protein kinase II (CaMKII) has been implicated in the transduction of calcium signals in the heart, but the specific isoforms of CaMKII that mediate pathological cardiac signaling have not been fully defined. To investigate the potential involvement in heart disease of CaMKIIdelta, the major CaMKII isoform expressed in the heart, we generated CaMKIIdelta-null mice. These mice are viable and display no overt abnormalities in cardiac structure or function in the absence of stress. However, pathological cardiac hypertrophy and remodeling are attenuated in response to pressure overload in these animals. Cardiac extracts from CaMKIIdelta-null mice showed diminished kinase activity toward histone deacetylase 4 (HDAC4), a substrate of stress-responsive protein kinases and suppressor of stress-dependent cardiac remodeling. In contrast, phosphorylation of the closely related HDAC5 was unaffected in hearts of CaMKIIdelta-null mice, underscoring the specificity of the CaMKIIdelta signaling pathway for HDAC4 phosphorylation. We conclude that CaMKIIdelta functions as an important transducer of stress stimuli involved in pathological cardiac remodeling in vivo, which is mediated, at least in part, by the phosphorylation of HDAC4. These findings point to CaMKIIdelta as a potential therapeutic target for the maintenance of cardiac function in the setting of pressure overload.
Phosphorylation Signal Transduction Calcium - metabolism Cardiomegaly - pathology Histone Deacetylases - metabolism Protein Kinase C - antagonists & inhibitors Calcium-Calmodulin-Dependent Protein Kinase Type 2 - antagonists & inhibitors Mice, Knockout Myocardial Infarction Animals Calcium-Calmodulin-Dependent Protein Kinase Type 2 - chemistry Models, Biological Protein Kinase C - metabolism Recombination, Genetic Protein Isoforms Mice Models, Genetic Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism

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