| First Author | Sorimachi H | Year | 1997 |
| Journal | Biochem J | Volume | 328 ( Pt 3) |
| Pages | 721-32 | PubMed ID | 9396712 |
| Mgi Jnum | J:45058 | Mgi Id | MGI:1101675 |
| Doi | 10.1042/bj3280721 | Citation | Sorimachi H, et al. (1997) Structure and physiological function of calpains. Biochem J 328(Pt 3):721-32 |
| abstractText | 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, mu- and m-calpains, still attract intensive interest because of their unique characteristics, various distinct homologues to the protease domain of mu- 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. |
