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Increase of cyclin B by overexpression of cystatin α
Author(s) -
Hiwasa Takaki,
Ma Jun,
Ike Yoshimasa,
Katunuma Nobuhiko,
Sakiyama Shigeru
Publication year - 1995
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.290130411
Subject(s) - cystatin , calpain , transfection , cathepsin b , microbiology and biotechnology , cyclin d , cystatin c , cyclin , cyclin d1 , cathepsin , cyclin b , chemistry , cysteine protease , proteasome , cyclin e , proteases , biology , biochemistry , cell cycle , gene , enzyme , renal function
Degradation of cyclin B was effectively suppressed when cells were treated with ALLN ( N ‐acetylleucylleucylnorleucinal) which inhibits proteasome, calpain and cysteine proteinase cathepsins. In order to examine which protease degrades cyclin B, the effect of a cathepsin inhibitor, cystatin α, was investigated. The cystatin α gene was inserted into an inducible expression vector, pMSG, and transfected into NIH3T3 mouse fibroblasts. The expression of cystatin α was induced effectively in the transfected cells after treatment with dexamethasone. Overexpression of cystatin α resulted in an increase of the amount of cyclin B, suggesting that cysteine proteinase cathepsins might be involved in the degradation of cyclin B.