Knockdown of Efp by DNA-modified small interfering RNA inhibits breast cancer cell proliferation and in vivo tumor growth

Ueyama, Kazuhiro; Ikeda, Kazuhiro; Sato, Wataru; Nakasato, Norie; Horie‐Inoue, Kuniko; Takeda, Satoru; Inoue, Satoshi

doi:10.1038/cgt.2010.19

Cited by 34 publications

(31 citation statements)

References 33 publications

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“…In the present in vivo tumor growth analysis, we used siRNA/DNA, since it has been reported that siRNA/DNA can overcome the disadvantages of usual siRNAs such as the problems of instability [48], induction of silencing of unintended genes (off-target effects) [49], or induction of immune response in vivo [50]. On the other hand, it has previously been reported that gene silencing induced by siRNA/DNA is likely to be less effective than that induced by its unmodified counterparts, because siRNA/DNA exhibits weaker activity for formation of am RNA-induced silencing complex [13,51]. Considering these facts, we adopted a multiple siRNA/ DNA injection protocol (in the present study, thrice, at days 0, 7, and 14) as described elsewhere [51,52].…”

Section: Discussionmentioning

confidence: 99%

“…On the other hand, it has previously been reported that gene silencing induced by siRNA/DNA is likely to be less effective than that induced by its unmodified counterparts, because siRNA/DNA exhibits weaker activity for formation of am RNA-induced silencing complex [13,51]. Considering these facts, we adopted a multiple siRNA/ DNA injection protocol (in the present study, thrice, at days 0, 7, and 14) as described elsewhere [51,52].…”

Section: Discussionmentioning

confidence: 99%

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Downregulation of KIF23 suppresses glioma proliferation

et al. 2011

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To identify therapeutic molecular targets for glioma, we performed modified serological identification of antigens by recombinant complementary DNA (cDNA) expression cloning using sera from a mouse glioma model. Two clones, kinesin family member 23 (Kif23) and structural maintenance of chromosomes 4 (Smc4), were identified as antigens through immunological reaction with sera from mice harboring synergic GL261 mouse glioma and intratumoral inoculation with a mutant herpes simplex virus. The human Kif23 homolog KIF23 is a nuclear protein that localizes to the interzone of mitotic spindles, acting as a plus-end-directed motor enzyme that moves antiparallel microtubules in vitro. Expression analysis revealed a higher level of KIF23 expression in glioma tissues than in normal brain tissue. The introduction of small interfering RNA (siRNA) targeting KIF23 into two different glioma cell lines, U87MG and SF126, downregulated KIF23 expression, which significantly suppressed glioma cell proliferation in vitro. KIF23 siRNA-treated glioma cells exhibited larger cell bodies with two or more nuclei compared with control cells. In vivo analysis using mouse xenograft showed that KIF23 siRNA/DNA chimera-treated tumors were significantly smaller than tumors treated with control siRNA/DNA chimera. Taken together, our results indicate that downregulation of KIF23 decreases proliferation of glioma cells and that KIF23 may be a novel therapeutic target in malignant glioma.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Downregulation of KIF23 suppresses glioma proliferation

et al. 2011

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“…9 More recently expression of TRIM25 has also been associated with ovarian and breast cancer and is thought to positively promote cell growth by targeting the cell cycle regulator 14-3-3 sigma for proteasomal degradation. [10][11][12] Therefore, TRIM25 may act as a tumor promoter, but whether TRIM25 has a function in lung cancer development remains unknown.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of TRIM25 in Lung Cancer Regulates Tumor Cell Progression

Qin

Zhang

2016

Technol Cancer Res Treat

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Lung cancer is one of the most common causes of cancer-related deaths worldwide. Although great efforts and progressions have been made in the study of the lung cancer in the recent decades, the mechanism of lung cancer formation remains elusive. To establish effective therapeutic methods, new targets implied in lung cancer processes have to be identified. Tripartite motifcontaining 25 has been associated with ovarian and breast cancer and is thought to positively promote cell growth by targeting the cell cycle. However, whether tripartite motif-containing 25 has a function in lung cancer development remains unknown. In this study, we found that tripartite motif-containing 25 was overexpressed in human lung cancer tissues. Expression of tripartite motifcontaining 25 in lung cancer cells is important for cell proliferation and migration. Knockdown of tripartite motif-containing 25 markedly reduced proliferation of lung cancer cells both in vitro and in vivo and reduced migration of lung cancer cells in vitro. Meanwhile, tripartite motif-containing 25 silencing also increased the sensitivity of doxorubicin and significantly increased death and apoptosis of lung cancer cells by doxorubicin were achieved with knockdown of tripartite motif-containing 25. We also observed that tripartite motif-containing 25 formed a complex with p53 and mouse double minute 2 homolog (MDM2) in both human lung cancer tissues and in lung cancer cells and tripartite motif-containing 25 silencing increased the expression of p53. These results provide evidence that tripartite motif-containing 25 contributes to the pathogenesis of lung cancer probably by promoting proliferation and migration of lung cancer cells. Therefore, targeting tripartite motif-containing 25 may provide a potential therapeutic intervention for lung cancer.

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“…EFP is a well-established downstream target gene of estrogen-ERα signaling [18, 29]. The expression of EFP mRNA and protein can be efficiently induced in response to estrogen treatment in human breast cancer cells and positively associated with ERα expression status in human primary breast cancer tumors [17, 20].…”

Section: Discussionmentioning

confidence: 99%

Oestrogen causes ATBF1 protein degradation through the oestrogen-responsive E3 ubiquitin ligase EFP

Dong

Fan

et al. 2012

Biochemical Journal

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We previously revealed that tumor suppressor ATBF1 formed an autoregulatory feedback loop with estrogen-ERα signaling to regulate estrogen-dependent cell proliferation in breast cancer cells. In this loop, ATBF1 inhibits the function of estrogen-ERα signaling while ATBF1 protein levels are fine-tuned by estrogen-induced transcriptional upregulation as well as ubiquitin proteasome pathway (UPP)-mediated protein degradation. Here we show that the estrogen-responsive finger protein (EFP) is an E3 ubiquitin ligase mediating estrogen-induced ATBF1 protein degradation. Knockdown increases but overexpression of EFP decreases ATBF1 protein levels. EFP interacts with and ubiquitinates ATBF1 protein. Furthermore, we show that EFP is an important factor in estrogen-induced ATBF1 protein degradation in which some other factors are also involved. In human primary breast tumors, due to both as directly-upregulated ERα target gene products, the levels of ATBF1 protein are positively correlated with the levels of EFP protein. However, the ratio of ATBF1 protein to EFP protein is negatively correlated with EFP protein levels. Functionally, ATBF1 antagonizes EFP-mediated cell proliferation. These findings not only establish EFP as the E3 ubiquitin ligase for estrogen-induced ATBF1 protein degradation, but further support the autoregulatory feedback loop between ATBF1 and estrogen-ERα signaling and thus implicate ATBF1 in estrogen-dependent breast development and carcinogenesis.

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Knockdown of Efp by DNA-modified small interfering RNA inhibits breast cancer cell proliferation and in vivo tumor growth

Cited by 34 publications

References 33 publications

Downregulation of KIF23 suppresses glioma proliferation

Downregulation of KIF23 suppresses glioma proliferation

Overexpression of TRIM25 in Lung Cancer Regulates Tumor Cell Progression

Oestrogen causes ATBF1 protein degradation through the oestrogen-responsive E3 ubiquitin ligase EFP

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