TY - JOUR
T1 - p202, an interferon-inducible protein, inhibits E2F1-mediated apoptosis in prostate cancer cells
AU - Yan, Duen Hwa
AU - Abramian, Aram
AU - Li, Zheng
AU - Ding, Yi
AU - Wen, Yong
AU - Liu, Ta Jen
AU - Hunt, Kelly
N1 - Funding Information:
This work was supported by the University Cancer Foundation at the University of Texas M.D. Anderson Cancer Center, Department of Defense DAMD17-99-1-9270, and Texas Advanced Technology Program under Grant No. 003657-0082-1999 (to D.-H.Y.), Department of Defense DAMD BC961478 (to K.H.)
PY - 2003/3/28
Y1 - 2003/3/28
N2 - p202, an interferon (IFN) inducible protein, is a phosphonuclear protein involved in the regulation of cell cycle, apoptosis, and differentiation. E2F1 belongs to the E2F family of proteins that are important cell cycle regulators in promoting cell growth. On the other hand, the deregulated expression of E2F1 also triggers apoptosis independent of p53 status. It has been well documented that p202 is able to inhibit cell growth by binding to E2F1 and abolishing the E2F1-mediated transcriptional activation of S-phase genes. However, it is not known whether E2F1-mediated apoptosis can be counteracted by p202 expression. Here, we show that E2F1-mediated apoptosis induced by the infection of an E2F1-expressing adenoviral vector (Ad-E2F1) was greatly diminished in p202-expressing prostate cancer cells. The E2F1-mediated caspase-3 activation was also reduced in p202-expressing cells infected with Ad-E2F1. Since caspase-3 is one of the E2F1 transcriptional targets, this result is consistent with the ability of p202 to inhibit the transcriptional activity of E2F1. Therefore, our results suggest a possible link between the IFN and E2F pathways in regulating apoptosis.
AB - p202, an interferon (IFN) inducible protein, is a phosphonuclear protein involved in the regulation of cell cycle, apoptosis, and differentiation. E2F1 belongs to the E2F family of proteins that are important cell cycle regulators in promoting cell growth. On the other hand, the deregulated expression of E2F1 also triggers apoptosis independent of p53 status. It has been well documented that p202 is able to inhibit cell growth by binding to E2F1 and abolishing the E2F1-mediated transcriptional activation of S-phase genes. However, it is not known whether E2F1-mediated apoptosis can be counteracted by p202 expression. Here, we show that E2F1-mediated apoptosis induced by the infection of an E2F1-expressing adenoviral vector (Ad-E2F1) was greatly diminished in p202-expressing prostate cancer cells. The E2F1-mediated caspase-3 activation was also reduced in p202-expressing cells infected with Ad-E2F1. Since caspase-3 is one of the E2F1 transcriptional targets, this result is consistent with the ability of p202 to inhibit the transcriptional activity of E2F1. Therefore, our results suggest a possible link between the IFN and E2F pathways in regulating apoptosis.
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U2 - 10.1016/S0006-291X(03)00320-6
DO - 10.1016/S0006-291X(03)00320-6
M3 - Article
C2 - 12646190
AN - SCOPUS:0037470832
SN - 0006-291X
VL - 303
SP - 219
EP - 222
JO - Biochemical and biophysical research communications
JF - Biochemical and biophysical research communications
IS - 1
ER -