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The proteasome controls the expression of a proliferation‐associated nuclear antigen Ki‐67
Author(s) -
Wu Yulian,
Luo Hongyu,
Kanaan Nada,
Wu Jiangping
Publication year - 2000
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(20000315)76:4<596::aid-jcb8>3.0.co;2-n
Subject(s) - proteasome , lactacystin , cell growth , cdk inhibitor , microbiology and biotechnology , chemistry , ubiquitin , protein degradation , cell cycle , cyclin dependent kinase , proteasome inhibitor , biology , cell , cancer research , biochemistry , gene
The proteasome is a protease complex responsible for rapid, selective, and irreversible removal of regulatory proteins, as well as many other cellular proteins. In this study, we have demonstrated that a proliferation‐associated nuclear protein Ki‐67 depended on the proteasome for its rapid degradation. A proteasome‐specific inhibitor lactacystin augmented Ki‐67 protein levels in pancreatic cancer BxPC‐3 cells while repressed the level of steady‐state Ki‐67 mRNA. Inhibition of the proteasome also led to accumulation of two CDK inhibitors p27 kip1 and p21 cip1 in the BxPC‐3 cells. Failed reduction of Ki‐67 protein and enhanced levels of the two CDK inhibitors are likely contributing factors for the suppressed BxPC‐3 proliferation after proteasome inhibition. J. Cell. Biochem. 76:596–604, 2000. © 2000 Wiley‐Liss, Inc.