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M212390200v1
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Papers In Press, published online ahead of print January 15, 2004
J. Biol. Chem, 10.1074/jbc.M212390200
Submitted on December 5, 2002
Revised on January 15, 2004
Accepted on January 15, 2004

Induction of G1 arrest and apoptosis in human Jurkat T cells by pentagalloylglucose through inhibiting proteasome activity and elevating p27Kip1, p21Cip1/WAF1 and Bax proteins

Wei-Jen Chen and Jen-Kun Lin

Institute of Biochemistry and Molecular Biology, National Taiwan Univresity, Taipei, Taiwan

Corresponding Author: jklin{at}ha.mc.ntu.edu.tw

Pentagalloylglucose, which is found in many medicinal plants, can arrest the cell cycle at G1 phase through downregulation of cyclin-dependent kinases 2 and 4, and upregulation of the cyclin-dependent kinase inhibitors p27Kip1 and p21Cip1/WAF1 in human breast cancer cells. Pentagalloylglucose also induces apoptosis in human leukemic cells. Yet the mechanisms by which pentagalloylglucose induces these effects is unclear. We now show that pentagalloylglucose inhibits the activities of purified 20S and 26S proteasomes in vitro, the 26S proteasome in Jurkat T cell lysates, and chymotrypsin-like activity of the 26S proteasome in intact Jurkat T cells. The turnover of p27Kip1 and p21Cip1/WAF1, which is necessary for cell cycle progression mediated by proteasome degradation, was disrupted by treatment of human Jurkat T cells with pentagalloylglucose. This was shown by cycloheximide treatment and in vivo pulse-chase labeling experiments and this effect correlated with the arrest of proliferation of Jurkat T cells at G1. Inhibition of the proteasome by pentagalloylglucose and by the proteasome inhibitor MG132 caused accumulation of ubiquitin-tagged proteins in Jurkat T cells. Addition of pentagalloylglucose to Jurkat T cells enhanced the stability of the proteasome substrate Bax, and increased cytochrome C release and apoptosis. Our findings suggest a mechanism for the effect of pentagalloylglucose on the cell cycle in human leukemic cells – that pentagalloylglucose downregulates proteasome-mediated pathways because it is a proteasome inhibitor.


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