In:
Biochemical Journal, Portland Press Ltd., Vol. 328, No. 3 ( 1997-12-15), p. 721-732
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0264-6021
,
1470-8728
Language:
English
Publisher:
Portland Press Ltd.
Publication Date:
1997
detail.hit.zdb_id:
1473095-9
SSG:
12
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