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lüll Calpain chronicle--an enzyme family under multidisciplinary characterization Sorimachi H; Hata S; Ono YProc Jpn Acad Ser B Phys Biol Sci 2011[]; 87 (6): 287-327Calpain is an intracellular Ca2+-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02) discovered in 1964. It was also called CANP (Ca2+-activated neutral protease) as well as CASF, CDP, KAF, etc. until 1990. Calpains are found in almost all eukaryotes and a few bacteria, but not in archaebacteria. Calpains have a limited proteolytic activity, and function to transform or modulate their substrates' structures and activities; they are therefore called, "modulator proteases." In the human genome, 15 genes--CAPN1, CAPN2, etc.--encode a calpain-like protease domain. Their products are calpain homologs with divergent structures and various combinations of functional domains, including Ca2+-binding and microtubule-interaction domains. Genetic studies have linked calpain deficiencies to a variety of defects in many different organisms, including lethality, muscular dystrophies, gastropathy, and diabetes. This review of the study of calpains focuses especially on recent findings about their structure-function relationships. These discoveries have been greatly aided by the development of 3D structural studies and genetic models.|*Calpain/chemistry/classification/genetics/metabolism[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Disease[MESH]|Enzyme Activation[MESH]|Humans[MESH]|Molecular Sequence Data[MESH]|Organ Specificity[MESH]|Protein Structure, Tertiary[MESH] |