For a long time now, two ubiquitously expressed mammalian calpain isoenzymes have been used to explore the structure and function of calpain. Although these two calpains, μ- and m-calpains, still attract intensive interest because of their unique characteristics, various distinct homologues to the protease domain of μ- and m-calpains have been identified in a variety of organisms. Some of these ‘novel’ calpain homologues are involved in important biological functions. For example, p94 (also called calpain 3), a mammalian calpain homologue predominantly expressed in skeletal muscle, is genetically proved to be responsible for limb-girdle muscular dystrophy type 2A. Tra-3, a calpain homologue in nematodes, is involved in the sex determination cascade during early development. PalB, a key gene product involved in the alkaline adaptation of Aspergillus nidulans, is the first example of a calpain homologue present in fungi. These findings indicate various important functional roles for intracellular proteases belonging to the calpain superfamily.
Review Article| December 15 1997
Structure and physiological function of calpains
Biochem J (1997) 328 (3): 721–732.
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Hiroyuki SORIMACHI, Shoichi ISHIURA, Koichi SUZUKI; Structure and physiological function of calpains. Biochem J 15 December 1997; 328 (3): 721–732. doi: https://doi.org/10.1042/bj3280721
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