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Involvement of calpain in diamide‐induced cataract in cultured lenses
Author(s) -
Azuma Mitsuyoshi,
Shearer Thomas R.
Publication year - 1992
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(92)80703-j
Subject(s) - calpain , proteolysis , crystallin , cysteine protease , protease , lens (geology) , biochemistry , biology , chemistry , microbiology and biotechnology , enzyme , paleontology
Lenses cultured in diamide first developed outer cortical opacities followed by nuclear cataract. Lens hydration and total calcium were markedly increased by diamide. Proteolysis or crystallins were observed in nuclear cataract lenses. Calpain in the soluble fraction of lenses cultured with diamide was decreased, while calpain in the insoluble fraction was increased. Co‐culture with E64d, an inhibitor of cysteine protease such as calpain, especially prevented nuclear opacities and proteolysis of crystallins, indicating that calpain was involved in cataract formation by diamide.