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Degradation of actin and vimentin by calpain II, a Ca 2+ ‐dependent cysteine proteinase, in bovine lens
Author(s) -
Yoshida Haruko,
Murachi Takashi,
Tsukahara Isamu
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81324-1
Subject(s) - calpain , calpastatin , vimentin , cytoskeleton , actin , cleavage (geology) , proteolysis , cysteine , polyacrylamide gel electrophoresis , gel electrophoresis , chemistry , biochemistry , microbiology and biotechnology , biology , enzyme , cell , immunohistochemistry , immunology , paleontology , fracture (geology)
Calpain II, a high Ca 2+ ‐requiring form of Ca 2+ ‐dependent cysteine proteinase (EC 3.4.22.17), isolated from bovine lens was found to cleave actin and vimentin, two major cytoskeletal elements of the lens. Polyacrylamide gel electrophoresis revealed that actin ( M r 43000) was broken down through intermediary products of approximate M r 42000 and 40000, while vimentin ( M r 57000) was rapidly cleaved into several fragments ranging from M r 44000 to 20000. The cleavage was dependent on Ca 2+ and could be blocked by calpastatin, a calpain‐specific inhibitor. These findings suggest that calpain might play a role in age‐related degradation of the lens cytoskeleton.