CacyBP/SIP inhibits Doxourbicin‐induced apoptosis of glioma cells due to activation of ERK1/2

Tang, Yuan; Zhan, Wenjian; Cao, Tong; Tang, Tianjin; Gao, Yong; Qiu, Zhichao; Fu, Chunling; Qian, Fengyuan; Yu, Rutong; Shi, Hengliang

doi:10.1002/iub.1477

Cited by 11 publications

(12 citation statements)

References 36 publications

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“…As Cacybp is an E3 ubiquitin ligase, we hypothesized that the 46 downregulated genes may include ubiquitinated substrates of Cacybp. The current focus of research is mainly Cacybp nuclear transfer (11,13,21,22) and phosphorylation activities (23)(24)(25)(26), which is consistent with our results. Using Cytoscape software we identified biological processes and molecular functions that may be affected by Cacybp.…”

Section: Discussionsupporting

confidence: 91%

“…We identified genes closely related to Cacybp expression through bioinformatics software analysis, but determining which of these differential genes are targets of Cacybp and which are ubiquitinated substrates requires further study. The current focus of research is mainly Cacybp nuclear transfer (11,13,21,22) and phosphorylation activities (23)(24)(25)(26), which is consistent with our results. In addition, we also found that Cacybp is involved in cell secretion and examined Cacybp expression in glioma patients and its relationship with prognosis.…”

Section: Discussionsupporting

confidence: 91%

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Bioinformatic analysis of Cacybp‐associated proteins using human glioma databases

Xuan¹,

Gao²,

Jin³

et al. 2019

IUBMB Life

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The ubiquitin‐proteasome system is the primary cellular pathway for protein degradation, mediating 80% of intracellular protein degradation. Because of the widespread presence of ubiquitin‐modified protein substrates, ubiquitination can regulate a variety of cellular activities including cell proliferation, apoptosis, autophagy, endocytosis, DNA damage repair, and immune responses. With the continuous generation of genomics data in recent years it has become particularly important to analyze these data effectively and reasonably. Cacybp forms a complex with the E3 ubiquitinated ligase Siah1 to participate in ubiquitination. We analyzed Cacybp‐associated genes using the Gene Expression Omnibus (GEO) and CGGA (Chinese Glioma Genome Atlas) databases and identified 121 differentially expressed genes (DEGs), of which 46 were downregulated and 75 were upregulated. The biological processes, molecular functions, and protein–protein interaction (PPI) network of differential genes were analyzed by Cytoscape software and STRING software. We found no difference in Cacybp expression among different grades of gliomas and there was no significant association between the expression level of Cacybp and the prognosis of patients with glioma in LGG and GBM. © 2019 IUBMB Life, 1–8, 2019

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Section: Discussionsupporting

confidence: 91%

Section: Discussionsupporting

confidence: 91%

Bioinformatic analysis of Cacybp‐associated proteins using human glioma databases

Xuan¹,

Gao²,

Jin³

et al. 2019

IUBMB Life

Self Cite

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“…Previously, our group focused on the V protein mediated host apoptosis. CacyBP/SIP was reported to participate in apoptosis (Chen et al, 2013 ; Fu et al, 2016 ; Tang et al, 2016 ). Among the 30 clones identified, four clones corresponded to CacyBP/SIP, we chose it for further study due to its involvement in the cell apoptosis adjustment.…”

Section: Resultsmentioning

confidence: 99%

“…CacyBP/SIP is involved in protein de-phosphorylation, ubiquitination, cytoskeletal dynamics, and all of these functions have been implicated in a wide range of cellular processes, such as cell proliferation, tumorigenesis, cell differentiation and gene expression (Shi et al, 2014 ; Topolskawoś et al, 2016 ). In some tumor cells, CacyBP/SIP has been shown to be involved in cell apoptosis, but the promotion or suppression of cancer apoptosis by CacyBP/SIP may depend on cell type (Chen et al, 2013 ; Fu et al, 2016 ; Tang et al, 2016 ). The role of CacyBP/SIP in DF-1 cell apoptosis and the effects of CacyBP/SIP on NDV replication efficiency in these cells remains to be determined.…”

Section: Introductionmentioning

confidence: 99%

Newcastle Disease Virus V Protein Inhibits Cell Apoptosis and Promotes Viral Replication by Targeting CacyBP/SIP

Chu

Wang

Tang

et al. 2018

Front. Cell. Infect. Microbiol.

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Newcastle disease virus (NDV) has been classified by the World Organization for Animal Health (OIE) as a notable disease-causing virus, and this virus has the ability to infect a wide range of birds. V protein is a non-structural protein of NDV. V protein has been reported to inhibit cell apoptosis (Park et al., 2003a) and promote viral replication (Huang et al., 2003), however, the mechanisms of action of V protein have not been elucidated. In the present study, a yeast two-hybrid screen was performed, and V protein was found to interact with the CacyBP/SIP protein. The results of co-immunoprecipitation and immuno-colocalization assays confirmed the interaction between V protein and CacyBP/SIP. The results of quantitative-PCR and viral plaque assays showed that overexpression of CacyBP/SIP inhibited viral replication in DF-1 cells. Overexpression of CacyBP/SIP in DF-1 cells induced caspase3-dependent apoptosis. The effect of knocking down CacyBP/SIP by siRNA was the opposite of that observed upon overexpression. Moreover, it is known that NDV induces cell apoptosis via multiple caspase-dependent pathways. Furthermore, V protein inhibited cell apoptosis and downregulated CacyBP/SIP expression in DF-1 cells. Taken together, the findings of the current study indicate that V protein interacts with CacyBP/SIP, thereby regulating cell apoptosis and viral replication.

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“…With respect to cancer, apoptosis has become a popular target for many treatment strategies as there is a close relationship with apoptosis and many of the processes involved in cancer progression [22–27]. …”

Section: Resultsmentioning

confidence: 99%

Insights into the Roles of Midazolam in Cancer Therapy

Jiao

Wang

Sun

et al. 2017

Evidence-Based Complementary and Alternative Medicine

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With its high worldwide mortality and morbidity, cancer has gained increasing attention and novel anticancer drugs have become the focus for cancer research. Recently, studies have shown that most anesthetic agents can influence the activity of tumor cells. Midazolam is a γ-aminobutyric acid A (GABAA) receptor agonist, used widely for preoperative sedation and as an adjuvant during neuraxial blockade. Some studies have indicated the potential for midazolam as a novel therapeutic cancer drug; however, the mechanism by which midazolam affects cancer cells needs to be clarified. This systematic review aims to summarize the progress in assessing the molecular mechanism of midazolam as an anticancer agent.

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CacyBP/SIP inhibits Doxourbicin‐induced apoptosis of glioma cells due to activation of ERK1/2

Cited by 11 publications

References 36 publications

Bioinformatic analysis of Cacybp‐associated proteins using human glioma databases

Bioinformatic analysis of Cacybp‐associated proteins using human glioma databases

Newcastle Disease Virus V Protein Inhibits Cell Apoptosis and Promotes Viral Replication by Targeting CacyBP/SIP

Insights into the Roles of Midazolam in Cancer Therapy

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