the ubiquitin-conjugating enzyme e2-epf is overexpressed in primary breast cancer and modulates sensitivity to topoisomerase ii inhibition
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ID: 144075
2007
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Abstract
We identified the ubiquitin-conjugating enzyme E2EPF mRNA as differentially expressed in breast tumors relative to normal tissues and performed studies to elucidate its putative role in cancer. We demonstrated that overexpression of E2-EPF protein correlated with estrogen receptor (ER) negativity in breast cancer specimens and that its expression is cell cycleregulated, suggesting a potential function for E2-EPF in cell cycle progression. However, reduction of E2EPF protein levels by > 80% using RNAi had no significant effects on the proliferation of HeLa cervical cancer cells or ER- MDA-MB-231 or MDA-MB-453 breast cancer cells. Because E2-EPF protein levels were elevated during the G2/M phase of the cell cycle and because E2-EPF mRNA in tumor specimens was frequently coexpressed with genes involved in cell cycle control, spindle assembly, and mitotic surveillance, the possibility that E2-EPF might have a function in the cellular response to agents that induce a G2 checkpoint or an M checkpoint was investigated. E2-EPF knockdown sensitized HeLa cells to the topoisomerase (topo) II inhibitors etoposide and doxorubicin and also increased topo IIα protein levels. These data suggest that combined administration of topo II-directed drugs and E2-EPF inhibitors may enhance their clinical effectiveness.
| Reference Key |
tedesco2007neoplasia:the
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| Authors | ;Donato Tedesco;Jianhuan Zhang;Lan Trinht;Guita Lalehzadeh;Rene Meisner;Ken D. Yamaguchi;Daniel L. Ruderman;Harald Dinter;Deborah A. Zajchowski |
| Journal | ACS chemical neuroscience |
| Year | 2007 |
| DOI |
10.1593/neo.07385
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| URL | |
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