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The muscle-specific chaperone protein melusin is a potent cardioprotective agent

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Abstract

Melusin is a protein selectively expressed in skeletal muscles and heart and highly conserved in vertebrates. Melusin is part of the heat shock protein 90 machinery and acts as molecular chaperone in controlling cardiomyocyte survival and adaptive hypertrophy signaling pathways in the heart in response to different stress conditions. The role of melusin has been extensively investigated in genetically modified mice over the past years disclosing an important cardioprotective function of this unique muscle-specific chaperone protein in different pathological conditions. This review highlights the findings in animal models and the molecular mechanisms underlying melusin cardioprotective function.

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Acknowledgments

This work was supported by funding from Telethon grant GGP12047 to GT, MIUR Prin 2010RNXM9C_002 to GT; MIUR PRIN 2010J8RYS7_007 to MB.

Conflict of interest

Mara Brancaccio and Guido Tarone are cofounders and scientific consultants for Target Heart Biotec, a company that develops melusin recombinant protein as a drug to counteract cardiomyopathies.

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  1. Department of Molecular Biotechnology and Health Sciences, University of Torino, Via Nizza 52, 10126, Turin, Italy

    Guido Tarone & Mara Brancaccio

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  1. Guido Tarone
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  2. Mara Brancaccio
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Correspondence to Guido Tarone.

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Tarone, G., Brancaccio, M. The muscle-specific chaperone protein melusin is a potent cardioprotective agent. Basic Res Cardiol 110, 10 (2015). https://doi.org/10.1007/s00395-015-0466-9

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