Work

Structure and physiological function of calpains

Year: 1997

Type: article

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, 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.

Source: Biochemical Journal

DOI: 10.1042/bj3280721

Authors: Hiroyuki SORIMACHI, Shoichi ISHIURA, Koichi SUZUKI

Institutions: Institute for Quantitative Biosciences, The University of Tokyo, The University of Tokyo

Language: English

Topic: Calpain Protease Function and Regulation

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W1758246291

FWCI: 8.85

Cites: 179

Cited by: 716

Related to: 10