Journal
CARDIOVASCULAR RESEARCH
Volume 96, Issue 1, Pages 11-22Publisher
OXFORD UNIV PRESS
DOI: 10.1093/cvr/cvs157
Keywords
Calpain; Intracellular proteolysis; Sarcomere; Transgenic mice; Calcium
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Funding
- JSPS KAKENHI [22770139, 20370055, 23247021]
- Toray Science Foundation
- Takeda Science Foundation
- Japan Society for the Promotion of Science
- Grants-in-Aid for Scientific Research [20370055, 22770139, 23247021] Funding Source: KAKEN
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Calpains, a family of Ca-2-dependent cytosolic cysteine proteases, can modulate their substrates structure and function through limited proteolytic activity. In the human genome, there are 15 calpain genes. The most-studied calpains, referred to as conventional calpains, are ubiquitous. While genetic studies in mice have improved our understanding about the conventional calpains physiological functions, especially those essential for mammalian life as in embryogenesis, many reports have pointed to overactivated conventional calpains as an exacerbating factor in pathophysiological conditions such as cardiovascular diseases and muscular dystrophies. For treatment of these diseases, calpain inhibitors have always been considered as drug targets. Recent studies have introduced another aspect of calpains that calpain activity is required to protect the heart and skeletal muscle against stress. This review summarizes the functions and regulation of calpains, focusing on the relevance of calpains to cardiovascular disease.
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